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14132426 | Aspartate-semialdehyde dehydrogenase | Amino-acid-synthesizing enzyme in fungi, plants and prokaryota
In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces diaminopimelate which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.
The enzyme catalyzes the reversible chemical reaction
-aspartate 4-semialdehyde + phosphate + NADP+ formula_0 -4-aspartyl phosphate + NADPH + H+
The 3 substrates of this enzyme are -aspartate 4-semialdehyde, phosphate, and NADP+, whereas its 3 products are -4-aspartyl phosphate, NADPH, and H+.
However, under physiological conditions the reaction runs in the opposite direction.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is -aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, -aspartate-beta-semialdehyde:NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis.
Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes.
Protein families.
This domain contains both "N"-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also contains the yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acetyl-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a dimerisation domain of semialdehyde dehydrogenase.
Structural studies.
As of late 2007, 24 structures have been solved for this class of enzymes, with PDB accession codes 1BRM, 1GL3, 1MB4, 1MC4, 1NWC, 1NWH, 1NX6, 1OZA, 1PQP, 1PQU, 1PR3, 1PS8, 1PU2, 1Q2X, 1T4B, 1T4D, 1TA4, 1TB4, 1YS4, 2EP5, 2GYY, 2GZ1, 2GZ2, and 2GZ3.
References.
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14132450 | Benzaldehyde dehydrogenase (NAD+) | Enzyme
In enzymology, a benzaldehyde dehydrogenase (NAD+) (EC 1.2.1.28) is an enzyme that catalyzes the chemical reaction
benzaldehyde + NAD+ + H2O formula_0 benzoate + NADH + 2 H+
The 3 substrates of this enzyme are benzaldehyde, NAD+, and H2O, whereas its 3 products are benzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzaldehyde:NAD+ oxidoreductase. Other names in common use include benzaldehyde (NAD+) dehydrogenase, and benzaldehyde dehydrogenase (NAD+). This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation.
References.
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14132480 | Benzaldehyde dehydrogenase (NADP+) | In enzymology, a benzaldehyde dehydrogenase (NADP+) (EC 1.2.1.7) is an enzyme that catalyzes the chemical reaction
benzaldehyde + NADP+ + H2O formula_0 benzoate + NADPH + 2 H+
The 3 substrates of this enzyme are benzaldehyde, NADP+, and H2O, whereas its 3 products are benzoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzaldehyde:NADP+ oxidoreductase. Other names in common use include NADP+-linked benzaldehyde dehydrogenase, and benzaldehyde dehydrogenase (NADP+). This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation.
References.
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14132508 | Betaine-aldehyde dehydrogenase | Enzyme
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction
betaine aldehyde + NAD+ + H2O formula_0 betaine + NADH + 2 H+
The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is betaine-aldehyde:NAD+ oxidoreductase. Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies.
As of late 2007[ [update]], 4 structures have been solved for this class of enzymes, with PDB accession codes 1A4S, 1BPW, 1WNB, and 1WND.
References.
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14132529 | Butanal dehydrogenase | Class of enzymes
In enzymology, a butanal dehydrogenase (EC 1.2.1.57) is an enzyme that catalyzes the chemical reaction
butanal + CoA + NAD(P)+ formula_0 butanoyl-CoA + NAD(P)H + H+
The 4 substrates of this enzyme are butanal, CoA, NAD+, and NADP+, whereas its 4 products are butanoyl-CoA, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanal:NAD(P)+ oxidoreductase (CoA-acylating). This enzyme participates in butanoate metabolism.
References.
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14132547 | Carbon monoxide dehydrogenase | Class of enzymes
In enzymology, carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
CO + H2O + A formula_0 CO2 + AH2
The chemical process catalyzed by carbon monoxide dehydrogenase is similar to the water-gas shift reaction.
The 3 substrates of this enzyme are CO, H2O, and A, whereas its two products are CO2 and AH2.
A variety of electron donors/receivers (Shown as "A" and "AH2" in the reaction equation above) are observed in micro-organisms which utilize CODH. Several examples of electron transfer cofactors have been proposed, including Ferredoxin, NADP+/NADPH and flavoprotein complexes like flavin adenine dinucleotide (FAD) as well as hydrogenases. CODHs support the metabolisms of diverse prokaryotes, including methanogens, aerobic carboxidotrophs, acetogens, sulfate-reducers, and hydrogenogenic bacteria. The bidirectional reaction catalyzed by CODH plays a role in the carbon cycle allowing organisms to both make use of CO as a source of energy and utilize CO2 as a source of carbon. CODH can form a monofunctional enzyme, as is the case in "Rhodospirillum rubrum", or can form a cluster with acetyl-CoA synthase as has been shown in "M. thermoacetica". When acting in concert, either as structurally independent enzymes or in a bifunctional CODH/ACS unit, the two catalytic sites are key to carbon fixation in the reductive acetyl-CoA pathway. Microbial organisms (Both aerobic and anaerobic) encode and synthesize CODH for the purpose of carbon fixation (CO oxidation and CO2 reduction). Depending on attached accessory proteins (A,B,C,D-Clusters), serve a variety of catalytic functions, including reduction of [4Fe-4S] clusters and insertion of nickel.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include anaerobic carbon monoxide dehydrogenase, carbon monoxide oxygenase, carbon-monoxide dehydrogenase, and carbon-monoxide:(acceptor) oxidoreductase.
Diversity.
CODH are a rather diverse group of enzymes, containing two unrelated types of CODH. A copper-molybdenum flavoenzymes is found in some aerobic carboxydotrophic bacteria. Anaerobic bacteria utilize nickel-iron based CODHs. Both classes of CODH catalyze the conversion of carbon monoxide (CO) to carbon dioxide (CO2). Only the Ni containing CODH is able to also catalyze the back reaction. CODHs exist in both monofunctional and bifunctional forms. An example for the latter case, Ni,Fe-CODHs form a bifunctional cluster with acetyl-CoA synthase, as has been well characterized in the anaerobic bacteria "Moorella thermoacetica", "Clostridium autoethanogenum" and "Carboxydothermus hydrogenoformans" "." While the ACS subunits of the complex of "C. autoethanogenum" show a rather extended arrangement those of the "M. thermoacetica" and "C. hydrogenoformans" complex are closer to the CODH subunits forming a tight tunnel network connecting cluster C and cluster A.
Ni,Fe-CODH.
Nickel containing CODH (Ni,Fe-CODH) can be further divided into structural clades, dependent on their phylogenetic relationship
Structure.
Ni,Fe-CODH.
Homodimeric Ni,Fe-CODHs contain five-metal clusters. They exist either in a homodimeric form (also called monofunctional) or in a bifunctional α2β2-tetrameric complex with acetyl-CoA synthase (ACS).
Monofunctional.
The best studied monofunctional CODHs are those of "Desulfovibrio vulgaris", "Rhodospirillum rubrum" and "Carboxydothermus hydrogenoformans." "" They are homodimers of around 130 kDa sharing a central [4Fe4S]-cluster at the surface of the protein - cluster D. The electrons are probably transferred to another [4Fe4S]-cluster (cluster B) located 10 A inside the protein and from there to the active site - cluster C, being an [Ni4Fe4S]-cluster. ""
Bifunctional.
The CODH/ACS complex is an α2β2 tetrameric enzyme. The structures of CODH/ACS complexes of the anaerobic bacteria "Moorella thermoacetica", "Clostridium autoethanogenum" and "Carboxydothermus hydrogenoformans" have been solved. The two CODH subunits form the central core of the enzyme to which an ACS subunit is attached at each side. Each α unit contains a single metal cluster. Together, the two β units contains five clusters of three types. CODH catalytic activity occurs at the Ni-[3Fe-4S] C-clusters while the interior [4Fe-4S] B and D clusters transfer electrons away from the C-cluster to external electron carriers such as ferredoxin. The ACS activity occurs in A-cluster located in the outer two α units.
All CODH/ACS complexes have a gas tunnel connecting the multiple active sites, while the tunnel system in the "C. autoethanogenum" enzyme is comparatively open and those of "M. thermoacetica" and "C. hydrogenoformans" rather tight. For the "Moorella" enzyme the rate of acetyl-CoA synthase activity from CO2 is not affected by the addition of hemoglobin, which would compete for CO in bulk solution, and isotopic labeling studies show that carbon monoxide derived from the C-cluster is preferentially used at the A-cluster over unlabeled CO in solution. Protein engineering of the CODH/ACS in "M.thermoacetica" revealed that mutating residues, so as to functionally block the tunnel, stopped acetyl-CoA synthesis when only CO2 was present. The discovery of a functional CO tunnel places CODH on a growing list of enzymes that independently evolved this strategy to transfer reactive intermediates from one active site to another.
Reaction mechanisms.
Ni,Fe-CODH.
The CODH catalytic site, referred to as the C-cluster, is a [3Fe-4S] cluster bonded to a Ni-Fe moiety. Two basic amino acids (Lys587 and His 113 in "M.thermoacetica") reside in proximity to the C-cluster and facilitate acid-base chemistry required for enzyme activity. Furthermore, other residues (i.e. an isoleucine apical to the Ni atom) fine-tune the binding and conversion of CO. Based on IR spectra suggesting the presence of an Ni-CO complex, the proposed first step in the oxidative catalysis of CO to CO2 involves the binding of CO to Ni2+ and corresponding complexing of Fe2+ to a water molecule.
It has been proposed that CO binds to square-planar nickel where it converts to a carboxy bridge between the Ni and Fe atom. A decarboxylation leads to the release of CO2 and the reduction of the cluster.
The electrons in the reduced C-cluster are transferred to nearby B and D [4Fe-4S] clusters, returning the Ni-[3Fe-4S] C-cluster to an oxidized state and reducing the single electron carrier ferredoxin.
Given CODH's role in CO2 fixation, the reductive mechanism is sometimes inferred as the “direct reverse” of the oxidative mechanism by the ”principle of microreversibility.”
Environmental relevance.
Carbon monoxide dehydrogenase regulates atmospheric CO and CO2 levels. Anaerobic micro-organisms like Acetogens undergo the Wood-Ljungdahl Pathway, relying on CODH to produce CO by reduction of CO2 needed for the synthesis of Acetyl-CoA from a methyl, coenzyme a (CoA) and corrinoid iron-sulfur protein. Other types show CODH being utilized to generate a proton motive force for the purposes of energy generation. CODH is used for the CO oxidation, producing two protons which are subsequently reduced to form dihydrogen (H2.
References.
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Further reading.
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14132561 | Carbon-monoxide dehydrogenase (cytochrome b-561) | Enzyme
In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) (EC 1.2.2.4) is an enzyme that catalyzes the chemical reaction
CO + H2O + 2 ferricytochrome b-561 formula_0 CO2 + 2 H+ + 2 ferrocytochrome b-561
The 3 substrates of this enzyme are CO, H2O, and ferricytochrome b-561, whereas its 3 products are CO2, H+, and ferrocytochrome b-561.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, CO dehydrogenase, and carbon-monoxide dehydrogenase.
References.
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14132576 | Carbon-monoxide dehydrogenase (ferredoxin) | Enzyme
In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
CO + H2O + oxidized ferredoxin formula_0 CO2 + reduced ferredoxin
The three substrates of this enzyme are CO, H2O, and oxidized ferredoxin, whereas its two products are CO2 and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is carbon-monoxide,water:ferredoxin oxidoreductase.
References.
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14132593 | Carboxylate reductase | In enzymology, a carboxylate reductase (EC 1.2.99.6) is an enzyme that catalyzes the chemical reaction
an aldehyde + acceptor + H2O formula_0 a carboxylate + reduced acceptor
The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, tungsten.
References.
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14132629 | Coniferyl-aldehyde dehydrogenase | Enzyme
In enzymology, a coniferyl-aldehyde dehydrogenase (EC 1.2.1.68) is an enzyme that catalyzes the chemical reaction
coniferyl aldehyde + H2O + NAD(P)+ formula_0 ferulate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are coniferyl aldehyde, H2O, NAD+, and NADP+, whereas its 4 products are ferulate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase.
References.
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14132653 | Fluoroacetaldehyde dehydrogenase | In enzymology, a fluoroacetaldehyde dehydrogenase (EC 1.2.1.69) is an enzyme that catalyzes the chemical reaction
fluoroacetaldehyde + NAD+ + H2O formula_0 fluoroacetate + NADH + 2 H+
The 3 substrates of this enzyme are fluoroacetaldehyde, NAD+, and H2O, whereas its 3 products are fluoroacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is fluoroacetaldehyde:NAD+ oxidoreductase.
References.
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14132676 | Formaldehyde dehydrogenase | Enzyme
In enzymology, a formaldehyde dehydrogenase (EC 1.2.1.46) is an enzyme that catalyzes the chemical reaction
formaldehyde + NAD+ + H2O formula_0 formate + NADH + H+
The 3 substrates of this enzyme are formaldehyde, NAD+, and H2O, whereas its 3 products are formate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase. Other names in common use include NAD+-linked formaldehyde dehydrogenase, s-nitrosoglutathione reductase (GSNO reductase) and NAD+-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism.
Ubiquitous function.
S-nitrosoglutathione reductase (GSNOR) is a class III alcohol dehydrogenase (ADH) encoded by the ADH5 gene in humans. It is a primordial ADH that is ubiquitously expressed in plant and animals alike. GSNOR reduces S-nitrosoglutathione (GSNO) to the unstable intermediate, S-hydroxylaminoglutathione, which then rearranges to form glutathione sulfinamide, or in the presence of GSH, forms oxidized glutathione (GSSG) and hydroxyl amine. Through this catabolic process, GSNOR regulates the cellular concentrations of GSNO and plays a central role in regulating the levels of endogenous S-nitrosothiols and controlling protein S-nitrosylation-based signaling. As an example of S-nitrosylation-based signaling, Barglow et al. showed that GSNO selectively S-nitrosylates reduced thioredoxin at cysteine 62. Nitrosylated thioredoxin, via directed protein-protein interaction, trans-nitrosylates the active site cysteine of caspase-3 thus inactivating caspase-3 and preventing induction of apoptosis.
As might be expected of an enzyme involved in regulating NO levels and signaling, pleiotropic effects are observed in GSNOR knockout models. Deleting the GSNOR gene from both yeast and mice increased the cellular levels of GSNO and nitrosylated proteins, and the yeast cells showed increased susceptibility to nitrosative stress. Null mice show increased levels of S-nitrosated proteins, increased beta adrenergic receptor numbers in lung and heart, diminished tachyphylaxis to β2-adrenergic receptor agonists, hyporesponsiveness to methacholine and allergen challenge and reduced infarct size after occlusion of the coronary artery. In addition, null mice show increased tissue damage and mortality following challenge with bacteria or endotoxin and are hypotensive under anesthesia yet normotensive in the conscious state. More related to its alcohol dehydrogenase activity, GSNOR null mice show a 30% reduction in the LD50 for formaldehyde and a decreased capacity to metabolize retinol, although it is clear from these studies that other pathways exist for the metabolism of these compounds.
Role in disease.
It has been shown that GSNOR may have an important role in respiratory diseases such as asthma. GSNOR expression has been inversely correlated with "S"-nitrosothiol (SNO) levels in the alveolar lining fluid in the lung and with responsiveness to methacholine challenge in patients with mild asthma compared to normal subjects. Furthermore, there are lowered SNOs in tracheal irrigations in asthmatic children with respiratory failure in comparison to normal children undergoing elective surgery and NO species are elevated in asthma patients when exposed to antigen.
Assessing the gene expression of the ADHs in nonalcoholic steatohepatitis (NASH) patients has shown elevated levels of all ADHs, but primarily ADH1 and ADH4 (up to 40-fold increased). ADH5 showed a ~4-fold increase in gene expression.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1KOL.
References.
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Further reading.
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14132692 | Formaldehyde dismutase | In enzymology, a formaldehyde dismutase (EC 1.2.99.4) is an enzyme that catalyzes the chemical reaction
2 formaldehyde formula_0 formate + methanol
Hence, this enzyme has one substrate, formaldehyde, and two products, formate and methanol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is formaldehyde:formaldehyde oxidoreductase. Other names in common use include aldehyde dismutase, and cannizzanase.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DPH.
References.
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14132711 | Formate dehydrogenase (cytochrome) | Type of enzyme
In enzymology, a formate dehydrogenase (cytochrome) (EC 1.2.2.1) is an enzyme that catalyzes the chemical reaction
formate + 2 ferricytochrome b1 formula_0 CO2 + 2 ferrocytochrome b1 + 2 H+
Thus, the two substrates of this enzyme are formate and ferricytochrome b1, whereas its 3 products are CO2, ferrocytochrome b1, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References.
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14132748 | Formate dehydrogenase (cytochrome-c-553) | In enzymology, a formate dehydrogenase (cytochrome-c-553) (EC 1.17.2.3) is an enzyme that catalyzes the chemical reaction
formate + ferricytochrome c-553 formula_0 CO2 + ferrocytochrome c-553
Thus, the two substrates of this enzyme are formate and ferricytochrome c-553, whereas its two products are CO2 and ferrocytochrome c-553.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase.
References.
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14132765 | Formate dehydrogenase (NADP+) | Enzyme
In enzymology, a formate dehydrogenase (NADP+) (EC 1.17.1.10) is an enzyme that catalyzes the chemical reaction
formate + NADP+ formula_0 CO2 + NADPH
Thus, the two substrates of this enzyme are formate and NADP+, whereas its two products are CO2 and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formate:NADP+ oxidoreductase. Other names in common use include NADP+-dependent formate dehydrogenase, and formate dehydrogenase (NADP+). This enzyme participates in methane metabolism. It has 3 cofactors: iron, Tungsten, and Selenium.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GSD.
References.
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14132802 | Gamma-guanidinobutyraldehyde dehydrogenase | In enzymology, a gamma-guanidinobutyraldehyde dehydrogenase (EC 1.2.1.54) is an enzyme that catalyzes the chemical reaction
4-guanidinobutanal + NAD+ + H2O formula_0 4-guanidinobutanoate + NADH + 2 H+
The 3 substrates of this enzyme are 4-guanidinobutanal, NAD+, and H2O, whereas its 3 products are 4-guanidinobutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-guanidinobutanal:NAD+ 1-oxidoreductase. Other names in common use include alpha-guanidinobutyraldehyde dehydrogenase, 4-guanidinobutyraldehyde dehydrogenase, and GBAL dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.
References.
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14132828 | Glutamate-5-semialdehyde dehydrogenase | In enzymology, a glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction
L-glutamate 5-semialdehyde + phosphate + NADP+ formula_0 L-glutamyl 5-phosphate + NADPH + H+
The 3 substrates of this enzyme are L-glutamate 5-semialdehyde, phosphate, and NADP+, whereas its 3 products are L-glutamyl 5-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include beta-glutamylphosphate reductase, gamma-glutamyl phosphate reductase, beta-glutamylphosphate reductase, glutamate semialdehyde dehydrogenase, and glutamate-gamma-semialdehyde dehydrogenase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1O20, 1VLU, and 2H5G.
References.
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14132844 | Glutamyl-tRNA reductase | A glutamyl-tRNA reductase (EC 1.2.1.70) is an enzyme that catalyzes the chemical reaction
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu formula_0 L-glutamyl-tRNAGlu + NADPH + H+
The 3 substrates of this enzyme are L-glutamate 1-semialdehyde, NADP+, and tRNA(Glu), whereas its 3 products are L-glutamyl-tRNA(Glu), NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate-semialdehyde: NADP+ oxidoreductase (L-glutamyl-tRNAGlu-forming). This enzyme participates in porphyrin and chlorophyll metabolism.
References.
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| https://en.wikipedia.org/wiki?curid=14132844 |
14132857 | Glutarate-semialdehyde dehydrogenase | In enzymology, a glutarate-semialdehyde dehydrogenase (EC 1.2.1.20) is an enzyme that catalyzes the chemical reaction
glutarate semialdehyde + NAD+ + H2O formula_0 glutarate + NADH + 2 H+
The 3 substrates of this enzyme are glutarate semialdehyde, NAD+, and H2O, whereas its 3 products are glutarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutarate-semialdehyde:NAD+ oxidoreductase. This enzyme is also called glutarate semialdehyde dehydrogenase. This enzyme participates in lysine degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14132857 |
14132874 | Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin formula_0 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
The 3 substrates of this enzyme are D-glyceraldehyde-3-phosphate, H2O, and oxidized ferredoxin, whereas its 3 products are 3-phospho-D-glycerate, H+, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase. Other names in common use include GAPOR, glyceraldehyde-3-phosphate Fd oxidoreductase, and glyceraldehyde-3-phosphate ferredoxin reductase.
References.
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| https://en.wikipedia.org/wiki?curid=14132874 |
14132889 | Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (EC 1.2.1.59) is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ formula_0 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
The 4 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, NAD+, and NADP+, whereas its 4 products are 3-phospho-D-glyceroyl phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating). Other names in common use include (phosphorylating), triosephosphate dehydrogenase (NAD(P)), and glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating).
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CZC.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14132889 |
14132911 | Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) (EC 1.2.1.13) is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NADP+ formula_0 3-phospho-D-glyceroyl phosphate + NADPH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NADP+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADPH, and H+.
Function.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway.
Nomenclature.
The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating). Other names in common use include:
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
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{
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| https://en.wikipedia.org/wiki?curid=14132911 |
14132929 | Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) | In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + phosphate + NAD+ formula_0 3-phospho-D-glyceroyl phosphate + NADH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NAD+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADH, and H+. This enzyme participates in glycolysis / gluconeogenesis.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
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{
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| https://en.wikipedia.org/wiki?curid=14132929 |
14132949 | Glycolaldehyde dehydrogenase | In enzymology, a glycolaldehyde dehydrogenase (EC 1.2.1.21) is an enzyme that catalyzes the chemical reaction
glycolaldehyde + NAD+ + H2O formula_0 glycolate + NADH + H+
The 3 substrates of this enzyme are glycolaldehyde, NAD+, and H2O, whereas its 3 products are glycolate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolaldehyde:NAD+ oxidoreductase. This enzyme is also called glycol aldehyde dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2HG2, 2ILU, and 2IMP.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
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| https://en.wikipedia.org/wiki?curid=14132949 |
14132982 | Glyoxylate dehydrogenase (acylating) | In enzymology, a glyoxylate dehydrogenase (acylating) (EC 1.2.1.17) is an enzyme that catalyzes the chemical reaction
glyoxylate + CoA + NADP+ formula_0 oxalyl-CoA + NADPH + H+
The 3 substrates of this enzyme are glyoxylate, CoA, and NADP+, whereas its 3 products are oxalyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glyoxylate:NADP+ oxidoreductase (CoA-oxalylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14132982 |
14133005 | Glyoxylate oxidase | In enzymology, a glyoxylate oxidase (EC 1.2.3.5) is an enzyme that catalyzes the chemical reaction
glyoxylate + H2O + O2 formula_0 oxalate + H2O2
The 3 substrates of this enzyme are glyoxylate, H2O, and O2, whereas its two products are oxalate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133005 |
14133021 | Hexadecanal dehydrogenase (acylating) | Enzyme
In enzymology, a hexadecanal dehydrogenase (acylating) (EC 1.2.1.42) is an enzyme that catalyzes the chemical reaction
hexadecanal + CoA + NAD+ formula_0 hexadecanoyl-CoA + NADH + H+
The 3 substrates of this enzyme are hexadecanal, CoA, and NAD+, whereas its 3 products are hexadecanoyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanal:NAD+ oxidoreductase (CoA-acylating). This enzyme is also called fatty acyl-CoA reductase.
References.
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| https://en.wikipedia.org/wiki?curid=14133021 |
14133042 | Indole-3-acetaldehyde oxidase | In enzymology, an indole-3-acetaldehyde oxidase (EC 1.2.3.7) is an enzyme that catalyzes the chemical reaction
(indol-3-yl)acetaldehyde + H2O + O2 formula_0 (indol-3-yl)acetate + H2O2
The 3 substrates of this enzyme are (indol-3-yl)acetaldehyde, H2O, and O2, whereas its two products are (indol-3-yl)acetate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is (indol-3-yl)acetaldehyde:oxygen oxidoreductase. Other names in common use include indoleacetaldehyde oxidase, IAAld oxidase, AO1, and indole-3-acetaldehyde:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism. It has 3 cofactors: FAD, Heme, and Molybdenum.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133042 |
14133053 | Indolepyruvate ferredoxin oxidoreductase | In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin formula_0 S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are (indol-3-yl)pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are S-2-(indol-3-yl)acetyl-CoA, CO2, and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating). Other names in common use include 3-(indol-3-yl)pyruvate synthase (ferredoxin), and IOR.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133053 |
14133071 | Lactaldehyde dehydrogenase | In enzymology, a lactaldehyde dehydrogenase (EC 1.2.1.22) is an enzyme that catalyzes the chemical reaction
(S)-lactaldehyde + NAD+ + H2O formula_0 (S)-lactate + NADH + 2 H+
The 3 substrates of this enzyme are (S)-lactaldehyde, NAD+, and H2O, whereas its 3 products are (S)-lactate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2HG2, 2ILU, 2IMP, and 2OPX.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133071 |
14133083 | L-aminoadipate-semialdehyde dehydrogenase | In enzymology, a L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) is an enzyme that catalyzes the chemical reaction
L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O formula_0 L-2-aminoadipate + NAD(P)H + H+
The 4 substrates of this enzyme are L-2-aminoadipate 6-semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are L-2-aminoadipate, NADH, NADPH, and H+.
This enzyme participates in lysine biosynthesis and biodegradation.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase. Other names in common use include:
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133083 |
14133101 | Long-chain-fatty-acyl-CoA reductase | In enzymology, a long-chain-fatty-acyl-CoA reductase (EC 1.2.1.50) is an enzyme that catalyzes the chemical reaction
a long-chain aldehyde + CoA + NADP+ formula_0 a long-chain acyl-CoA + NADPH + H+
The 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP+, whereas its 3 products are long-chain acyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common use include acyl-CoA reductase, and acyl coenzyme A reductase.
References.
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| https://en.wikipedia.org/wiki?curid=14133101 |
14133115 | Malonate-semialdehyde dehydrogenase | In enzymology, a malonate-semialdehyde dehydrogenase (EC 1.2.1.15) is an enzyme that catalyzes the chemical reaction
3-oxopropanoate + NAD(P)+ + H2O formula_0 malonate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are 3-oxopropanoate, NAD+, NADP+, and H2O, whereas its 4 products are malonate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase. This enzyme participates in beta-alanine metabolism.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133115 |
14133135 | Malonate-semialdehyde dehydrogenase (acetylating) | In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical reaction
3-oxopropanoate + CoA + NAD(P)+ formula_0 acetyl-CoA + CO2 + NAD(P)H
The 4 substrates of this enzyme are 3-oxopropanoate, CoA, NAD+, and NADP+, whereas its 4 products are acetyl-CoA, CO2, NADH, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxopropanoate:NAD(P)+ oxidoreductase (decarboxylating, CoA-acetylating). This enzyme is also called malonic semialdehyde oxidative decarboxylase. This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine metabolism, and propanoate metabolism.
References.
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Further reading.
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| https://en.wikipedia.org/wiki?curid=14133135 |
14133168 | Mycothiol-dependent formaldehyde dehydrogenase | In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction
formaldehyde + mycothiol + NAD+ formula_0 S-formylmycothiol + NADH + 2 H+
The 3 substrates of this enzyme are formaldehyde, mycothiol, and NAD+, whereas its 3 products are S-formylmycothiol, NADH, and H+. This enzyme catalyses the following chemical reaction
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase (mycothiol-formylating). This enzyme is also called NAD/factor-dependent formaldehyde dehydrogenase or S-(hydroxymethyl)mycothiol dehydrogenase.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133168 |
14133191 | N-acetyl-gamma-glutamyl-phosphate reductase | In enzymology, a N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) is an enzyme that catalyzes the chemical reaction
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate formula_0 N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
The 3 substrates of this enzyme are N-acetyl-L-glutamate 5-semialdehyde, NADP+, and phosphate, whereas its 3 products are N-acetyl-L-glutamyl 5-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating). Other names in common use include reductase, acetyl-gamma-glutamyl phosphate, N-acetylglutamate 5-semialdehyde dehydrogenase, N-acetylglutamic gamma-semialdehyde dehydrogenase, N-acetyl-L-glutamate gamma-semialdehyde:NADP+ oxidoreductase, and (phosphorylating). This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1VKN, 2CVO, 2G17, 2I3A, 2I3G, 2NQT, 2OZP, and 2Q49.
References.
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| https://en.wikipedia.org/wiki?curid=14133191 |
14133206 | Oxalate oxidase | In enzymology, an oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:
oxalate + O2 + 2 H+ formula_0 2 CO2 + H2O2
The 3 substrates of this enzyme are oxalate, O2, and H+, whereas its two products are CO2 and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo dehydrogenase, and oxalic acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It uses Manganese as a cofactor.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1FI2, 2ET1, 2ET7, and 2ETE.
References.
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| https://en.wikipedia.org/wiki?curid=14133206 |
14133218 | Oxoglutarate dehydrogenase (NADP+) | In enzymology, an oxoglutarate dehydrogenase (NADP+) (EC 1.2.1.52) is an enzyme that catalyzes the chemical reaction
2-oxoglutarate + CoA + NADP+ formula_0 succinyl-CoA + CO2 + NADPH
The 3 substrates of this enzyme are 2-oxoglutarate, CoA, and NADP+, whereas its 3 products are succinyl-CoA, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating). This enzyme is also called oxoglutarate dehydrogenase (NADP+).
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133218 |
14133250 | Phenylacetaldehyde dehydrogenase | In enzymology, a phenylacetaldehyde dehydrogenase (EC 1.2.1.39) is an enzyme that catalyzes the chemical reaction
phenylacetaldehyde + NAD+ + H2O formula_0 phenylacetate + NADH + 2 H+
The 3 substrates of this enzyme are phenylacetaldehyde, NAD+, and H2O, whereas its 3 products are phenylacetate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylacetaldehyde:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism and styrene degradation.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133250 |
14133270 | Phenylglyoxylate dehydrogenase (acylating) | In enzymology, a phenylglyoxylate dehydrogenase (acylating; EC 1.2.1.58) is an enzyme that catalyzes the chemical reaction
phenylglyoxylate + NAD+ + CoA-SH formula_0 benzoyl-S-CoA + CO2 + NADH
The three substrates of this enzyme are phenylglyoxylate, NAD+, and CoA-SH, whereas its 3 products are benzoyl-S-CoA, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylglyoxylate:NAD+ oxidoreductase. It has 3 cofactors: FAD, Thiamin diphosphate, and Iron-sulfur.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133270 |
14133292 | Pyridoxal oxidase | Class of enzymes
In enzymology, a pyridoxal oxidase (EC 1.2.3.8) is an enzyme that catalyzes the chemical reaction
pyridoxal + H2O + O2 formula_0 4-pyridoxate + (?)
The 3 substrates of this enzyme are pyridoxal, H2O, and O2, whereas its product is 4-pyridoxate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, molybdenum.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133292 |
14133328 | Pyruvate dehydrogenase (cytochrome) | In enzymology, a pyruvate dehydrogenase (cytochrome) (EC 1.2.2.2) is an enzyme that catalyzes the chemical reaction
pyruvate + ferricytochrome b1 + H2O formula_0 acetate + CO2 + ferrocytochrome b1
The 3 substrates of this enzyme are pyruvate, ferricytochrome b1, and H2O, whereas its 3 products are acetate, CO2, and ferrocytochrome b1.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
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| https://en.wikipedia.org/wiki?curid=14133328 |
14133347 | Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction
pyruvate + phosphate + O2 formula_0 acetyl phosphate + CO2 + H2O2
The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.
Structural studies.
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1POW, 1POX, 1V5E, 1V5F, 1V5G, 1Y9D, 2DJI, 2EZ4, 2EZ8, 2EZ9, 2EZT, and 2EZU.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14133347 |
14133365 | Pyruvate oxidase (CoA-acetylating) | A pyruvate oxidase is basically an enzyme that speeds up a chemical reaction.
The by products of this reaction are carbon dioxide , hydrogen peroxide etc.
In enzymology, a pyruvate oxidase (CoA-acetylating) (EC 1.2.3.6) is an enzyme that catalyzes the chemical reaction
pyruvate + CoA + O2 formula_0 acetyl-CoA + CO2 + H2O2
The 3 substrates of this enzyme are pyruvate, CoA, and O2, whereas its 3 products are acetyl-CoA, CO2, and H2O2.
This enzyme belongs to the family of oxidoreductases , specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2 - oxidoreductase (CoA-acetylating). This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14133365 |
14133384 | Pyruvate synthase | Class of enzymes
In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).
The relevant equilibrium catalysed by PFOR is:
pyruvate + CoA + oxidized ferredoxin formula_0 acetyl-CoA + CO2 + reduced ferredoxin
The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are acetyl-CoA, CO2, and reduced ferredoxin.
Function.
This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle (CO2 fixation).
Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate (TPP) but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters. This process links glycolysis to the Wood–Ljungdahl pathway.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use include:
Structure.
PFOR adopts a dimeric structure, while each monomeric subunit is composed of one or multiple chain(s) of polypeptides. Each monomeric subunit of PFOR consists of six domains binding one TPP molecule and three [4Fe-4S] clusters.
Catalytic Mechanism.
An PFOR reaction starts with the nucleophilic attack of C2 of TPP on the 2-oxo carbon of pyruvate, which forms a lactyl-TPP adduct. Next, the lactyl-TPP adduct releases the CO2 moiety, forming an anionic intermediate, which then transfer an electron to a [4Fe-4S] cluster. These steps lead to a stable radical intermediate that can be observed by electron paramagnetic resonance (EPR) experiments. The radical intermediate reacts with a CoA molecule, transfers another electron from the radical intermediate to a [4Fe-4S] cluster and forms an acetyl-CoA product.
References.
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Further reading.
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| https://en.wikipedia.org/wiki?curid=14133384 |
14133406 | (R)-dehydropantoate dehydrogenase | Class of enzymes
In enzymology, a (R)-dehydropantoate dehydrogenase (EC 1.2.1.33) is an enzyme that catalyzes the chemical reaction
(R)-4-dehydropantoate + NAD+ + H2O formula_0 (R)-3,3-dimethylmalate + NADH + 2 H+
The 3 substrates of this enzyme are (R)-4-dehydropantoate, NAD+, and H2O, whereas its 3 products are (R)-3,3-dimethylmalate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-4-dehydropantoate:NAD+ 4-oxidoreductase. Other names in common use include D-aldopantoate dehydrogenase, D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine, and nucleotide (DPN+) oxidoreductase. This enzyme participates in pantothenate and coa biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14133406 |
14133420 | Retinal dehydrogenase | In enzymology, a retinal dehydrogenase, also known as retinaldehyde dehydrogenase (RALDH), catalyzes the chemical reaction converting retinal to retinoic acid. This enzyme belongs to the family of oxidoreductases, specifically the class acting on aldehyde or oxo- donor groups with NAD+ or NADP+ as acceptor groups, the systematic name being retinal:NAD+ oxidoreductase. This enzyme participates in retinol metabolism. The general scheme for the reaction catalyzed by this enzyme is:
retinal + NAD+ + H2O formula_0 retinoic acid + NADH + H+
Structure.
Retinal dehydrogenase is a tetramer of identical units, consisting of a dimer of dimers. Retinal dehydrogenase monomers are composed of three domains: a nucleotide-binding domain, a tetramerization domain, and a catalytic domain. The dimer can be pictured as an "X" with the dimers forming upper and lower halves that cross over each other. Interestingly, the nucleotide-binding domain of retinal dehydrogenase contains 5 instead of the usual 6 β-strands in the Rossman fold. This appears to be conserved across many aldehyde dehydrogenases. The tetramerization domains lie equatorially along the "X" and the nucleotide binding regions appear on the tips of the "X". Nearby the tetramerization domain lies a 12 Å deep tunnel that gives the substrate access to the key catalytic regions. Residues near the C-terminal end of the catalytic domain have been found to impart specificity in other aldehyde dehydrogenases. Common to many aldehyde dehydrogenases is a catalytic cysteine, which was found to be present in RALDH2, a specific retinal dehydrogenase for which the structure has been solved.
Specificity.
There are three general classes of aldehyde dehydrogenases: class 1 (ALDH1) comprises cytosolic proteins, class 2 (ALDH2) includes mitochondrial proteins, and class 3 (ALDH3) includes tumor-related proteins. ALDH1 enzymes show a high specificity for all-trans retinal and 9-cis retinal in kinetic studies of sheep liver aldehyde dehydrogenases while ALDH2 enzymes show little affinity for retinal and instead appears to be mainly involved in the oxidation of acetaldehyde. The entrance tunnel to the enzyme active site appears to provide the specificity observed in ALDH1 for retinal as a substrate. The size of the tunnel is key in imparting this specificity: the solvent-accessible diameter of the entrance tunnel is 150 Å3 in ALDH1, so the relatively large retinal can be accommodated while the solvent accessible diameter in ALDH2 is only 20 Å3 which limits accessibility to retinal but amply accommodates acetaldehyde.
Mechanism.
The proposed mechanism of retinal dehydrogenase begins with a key cysteine residue in the active site attacking the aldehyde group in retinal to form a thiohemiacetal intermediate. Then, a hydride shift is facilitated by the enzyme to form NADH and a thioester intermediate. This hydride shift has been shown to be stereospecific in a subset (class 3) of retinal dehydrogenases. The thioester intermediate is then attacked by a water molecule, which is made more nucleophilic by a glutamate residue that lies near the active site. There has been some debate as to whether the glutamate residue near the active site acts as a general base during the reaction or whether it is more limited and merely deprotonates the catalytic cysteine to make the cysteine more nucleophilic. Kinetic studies have supported this mechanism by showing that the reaction follows an ordered sequential path with NAD+ binding first which is followed by the binding of retinal, the catalytic breakdown of retinal to retinoic acid, the release of retinoic acid, and finally the release of NADH.
Regulation.
Some of the strategies for regulating retinal dehydrogenases are only now becoming more clear after "in vivo" regulation remained mysterious for some time, though much of the current research on regulation has focused on the modulation of gene expression rather than direct protein regulation. Dendritic cells in the gut help in modulating immune tolerance through the activity of retinal dehydrogenase; expression in these cells may be driven by a TNF receptor, 4-1-BB. It was also shown that the expression of a certain retinal dehydrogenase found in humans, retinal short-chain dehydrogenase/reductase (retSDR1), is increased by tumor-suppressor proteins p53 and p63, suggesting that retSDR1 may have tumor-preventing activities. Expression of retinal dehydrogenase types 1 and 2 genes is enhanced by the addition of cholesterol or cholesterol derivatives. Disulfiram is a drug used to artificially regulate aldehyde dehydrogenase activity in patients with alcoholism by inhibiting the activity of aldehyde dehydrogenases, though it is not specific to retinal dehydrogenase. Other exogenous molecules have also been found to inhibit retinal dehydrogenase activity including nitrofen, 4-biphenyl carboxylic acid, bisdiamine, and SB-210661.
Clinical significance.
Retinal dehydrogenase plays a key role in the biosynthesis of retinoic acid, which in turn acts in cell signaling pathways. Retinoic acid is distinct from other cell signaling molecules in that it diffuses into the nucleus and binds directly to gene targets via retinoic acid receptors. This retinoic acid signaling pathway also appears to be unique to chordates, as suggested by the presence of retinal dehydrogenases exclusively in chordates. Retinoic acid signaling appears to control developmental processes like neurogenesis, cardiogenesis, forelimb bud development, foregut development, and eye development. Retinoic acid signaling is also important for maintaining adult neuronal and epithelium cell type. Retinoic acid is generated in organisms by first oxidizing retinol (Vitamin A) to retinal with an alcohol dehydrogenase. Then, a retinal dehydrogenase oxidizes retinal to retinoic acid. The production of retinoic acid from vitamin A must be tightly controlled as high levels of retinoic acid and vitamin A can lead to toxic effects, while vitamin A deficiency leads to its own issues in development. This provides a rationale for many of the transcriptional regulatory strategies discussed earlier. In humans, mutations in a gene coding for a certain retinal dehydrogenase ("RDH12") can also lead to Leber's congenital amaurosis, a retinal dystrophy responsible for many cases of congenital blindness.
Isoforms.
Different isoforms of retinal dehydrogenase exist and play a key role in development, as the types are differentially expressed inside a developing embryo. The enzyme retinal dehydrogenase type-2 (RALDH2) catalyzes much of the retinoic acid formation during development, but not all. RALDH2 is crucial for development midgestation and helps drive neural, heart, lung, and forelimb development; it is also responsible for all retinoic acid development during certain periods of midgestation. Later in development, retinal dehydrogenase type-1 (RALDH1) begins activity in the dorsal pit of the retina and retinal dehydrogenase type-3 (RALDH3) becomes active in the olfactory pit, ventral retina, and urinary tract. "Raldh2" gene knockouts are fatal in mice during development since the brain cannot develop normally. "Raldh3" gene knockout is fatal at birth in mice since nasal passages are not properly developed and instead are blocked. "Raldh1" knockouts are not fatal and, interestingly, have been shown to be protective against diet-induced obesity in mice in a retinoid-independent manner.
References.
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| https://en.wikipedia.org/wiki?curid=14133420 |
14133439 | Retinal oxidase | In enzymology, a retinal oxidase (EC 1.2.3.11) is an enzyme that catalyzes the chemical reaction
retinal + O2 + H2O formula_0 retinoic acid + H2O2
The 3 substrates of this enzyme are retinal, O2, and H2O, whereas its two products are retinoic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase. This enzyme participates in retinol metabolism.
References.
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| https://en.wikipedia.org/wiki?curid=14133439 |
14133450 | Succinate-semialdehyde dehydrogenase (NAD(P)+) | In enzymology, a succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16) is an enzyme that catalyzes the chemical reaction
succinate semialdehyde + NAD(P)+ + H2O formula_0 succinate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are succinate semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are succinate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate-semialdehyde:NAD(P)+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase (nicotinamide adenine, dinucleotide (phosphate)), and succinate-semialdehyde dehydrogenase [NAD(P)+]. This enzyme participates in 3 metabolic pathways: glutamate metabolism, tyrosine metabolism, and butanoate metabolism.
References.
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| https://en.wikipedia.org/wiki?curid=14133450 |
14133464 | Vanillin dehydrogenase | In enzymology, a vanillin dehydrogenase (EC 1.2.1.67) is an enzyme that catalyzes the chemical reaction
+ NAD+ + H2O formula_0 + NADH + H+
The 3 substrates of this enzyme are vanillin, NAD+, and H2O, whereas its 3 products are vanillate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vanillin:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14133464 |
1413480 | Parabolic SAR | Chart indicator
In stock and securities market technical analysis, parabolic SAR (parabolic stop and reverse) is a method devised by J. Welles Wilder Jr., to find potential reversals in the market price direction of traded goods such as securities or currency exchanges such as forex. It is a trend-following (lagging) indicator and may be used to set a trailing stop loss or determine entry or exit points based on prices tending to stay within a parabolic curve during a strong trend.
Similar to option theory's concept of time decay, the concept draws on the idea that "time is the enemy". Thus, unless a security can continue to generate more profits over time, it should be liquidated. The indicator generally works only in trending markets, and creates "whipsaws" during ranging or, sideways phases. Therefore, Wilder recommends first establishing the direction or change in direction of the trend through the use of parabolic SAR, and then using a different indicator such as the Average Directional Index to determine the strength of the trend.
A parabola below the price is generally bullish, while a parabola above is generally bearish. A parabola below the price may be used as support, whereas a parabola above the price may represent resistance.
Construction.
The parabolic SAR is calculated almost independently for each trend in the price. When the price is in an uptrend, the SAR emerges below the price and converges upwards towards it. Similarly, on a downtrend, the SAR emerges above the price and converges downwards.
At each step within a trend, the SAR is calculated one period in advance. That is, tomorrow's SAR value is built using data available today. The general formula used for this is:
formula_0,
where "SARn" and "SARn+1" represent the current period and the next period's SAR values, respectively.
"EP" (the extreme point) is a record kept during each trend that represents the highest value reached by the price during the current uptrend – or lowest value during a downtrend. During each period, if a new maximum (or minimum) is observed, the EP is updated with that value.
The "α" value represents the acceleration factor. Usually, this is set initially to a value of 0.02, but can be chosen by the trader. This factor is increased by 0.02 each time a new EP is recorded, which means that every time a new EP is observed, it will make the acceleration factor go up. The rate will then quicken to a point where the SAR converges towards the price. To prevent it from getting too large, a maximum value for the acceleration factor is normally set to 0.20. The traders can set these numbers depending on their trading style and the instruments being traded. Generally, it is preferable in stocks trading to set the acceleration factor to 0.01, so that it is not too sensitive to local decreases. For commodity or currency trading, the preferred value is 0.02.
The SAR is calculated in this manner for each new period. However, two special cases will modify the SAR value:
Upon a trend switch, the first SAR value for this new trend is set to the last EP recorded on the prior trend, EP is then reset accordingly to this period's maximum, and the acceleration factor is reset to its initial value of 0.02.
Statistical Results.
The parabolic SAR showed results at a 95% confidence level in a study of 17 years of data. This is a 2009 study using Excel for analysis. These findings are true over both the long term and short term studies evaluated by this research.
A modern study of parabolic SAR based on 2,880 years of backtesting over a 12-year period to 2023 on the Dow Jones Industrial Average 30 stocks, demonstrated using PSAR with a standard OHLC chart resulted in a 19% win rate. Using PSAR with a Heikin Ashi chart produced a 63% success rate.
References.
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| https://en.wikipedia.org/wiki?curid=1413480 |
14136 | Hydrophobe | Molecule or surface that has no attraction to water
In chemistry, hydrophobicity is the physical property of a molecule that is seemingly repelled from a mass of water (known as a hydrophobe). In contrast, hydrophiles are attracted to water.
Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle.
Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds.
Hydrophobic is often used interchangeably with lipophilic, "fat-loving". However, the two terms are not synonymous. While hydrophobic substances are usually lipophilic, there are exceptions, such as the silicones and fluorocarbons.
The term "hydrophobe" comes from the Ancient Greek (), "having a fear of water", constructed from grc " ὕδωρ (húdōr)" 'water' and grc " φόβος (phóbos)" 'fear'.
Chemical background.
The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute, causing the water to form a clathrate-like structure around the non-polar molecules. This structure formed is more highly ordered than free water molecules due to the water molecules arranging themselves to interact as much as possible with themselves, and thus results in a higher entropic state which causes non-polar molecules to clump together to reduce the surface area exposed to water and decrease the entropy of the system. Thus, the two immiscible phases (hydrophilic vs. hydrophobic) will change so that their corresponding interfacial area will be minimal. This effect can be visualized in the phenomenon called phase separation.
Superhydrophobicity.
Superhydrophobic surfaces, such as the leaves of the lotus plant, are those that are extremely difficult to wet. The contact angles of a water droplet exceeds 150°. This is referred to as the lotus effect, and is primarily a physical property related to interfacial tension, rather than a chemical property.
Theory.
In 1805, Thomas Young defined the contact angle "θ" by analyzing the forces acting on a fluid droplet resting on a solid surface surrounded by a gas.
formula_0
where
formula_1 = Interfacial tension between the solid and gas
formula_2 = Interfacial tension between the solid and liquid
formula_3 = Interfacial tension between the liquid and gas
"θ" can be measured using a contact angle goniometer.
Wenzel determined that when the liquid is in intimate contact with a microstructured surface, "θ" will change to "θ"W*
formula_4
where "r" is the ratio of the actual area to the projected area. Wenzel's equation shows that microstructuring a surface amplifies the natural tendency of the surface. A hydrophobic surface (one that has an original contact angle greater than 90°) becomes more hydrophobic when microstructured – its new contact angle becomes greater than the original. However, a hydrophilic surface (one that has an original contact angle less than 90°) becomes more hydrophilic when microstructured – its new contact angle becomes less than the original.
Cassie and Baxter found that if the liquid is suspended on the tops of microstructures, "θ" will change to "θ"CB*:
formula_5
where "φ" is the area fraction of the solid that touches the liquid. Liquid in the Cassie–Baxter state is more mobile than in the Wenzel state.
We can predict whether the Wenzel or Cassie–Baxter state should exist by calculating the new contact angle with both equations. By a minimization of free energy argument, the relation that predicted the smaller new contact angle is the state most likely to exist. Stated in mathematical terms, for the Cassie–Baxter state to exist, the following inequality must be true.
formula_6
A recent alternative criterion for the Cassie–Baxter state asserts that the Cassie–Baxter state exists when the following 2 criteria are met:1) Contact line forces overcome body forces of unsupported droplet weight and 2) The microstructures are tall enough to prevent the liquid that bridges microstructures from touching the base of the microstructures.
A new criterion for the switch between Wenzel and Cassie-Baxter states has been developed recently based on surface roughness and surface energy. The criterion focuses on the air-trapping capability under liquid droplets on rough surfaces, which could tell whether Wenzel's model or Cassie-Baxter's model should be used for certain combination of surface roughness and energy.
Contact angle is a measure of static hydrophobicity, and contact angle hysteresis and slide angle are dynamic measures. Contact angle hysteresis is a phenomenon that characterizes surface heterogeneity. When a pipette injects a liquid onto a solid, the liquid will form some contact angle. As the pipette injects more liquid, the droplet will increase in volume, the contact angle will increase, but its three-phase boundary will remain stationary until it suddenly advances outward. The contact angle the droplet had immediately before advancing outward is termed the advancing contact angle. The receding contact angle is now measured by pumping the liquid back out of the droplet. The droplet will decrease in volume, the contact angle will decrease, but its three-phase boundary will remain stationary until it suddenly recedes inward. The contact angle the droplet had immediately before receding inward is termed the receding contact angle. The difference between advancing and receding contact angles is termed contact angle hysteresis and can be used to characterize surface heterogeneity, roughness, and mobility. Surfaces that are not homogeneous will have domains that impede motion of the contact line. The slide angle is another dynamic measure of hydrophobicity and is measured by depositing a droplet on a surface and tilting the surface until the droplet begins to slide. In general, liquids in the Cassie–Baxter state exhibit lower slide angles and contact angle hysteresis than those in the Wenzel state.
Research and development.
Dettre and Johnson discovered in 1964 that the superhydrophobic lotus effect phenomenon was related to rough hydrophobic surfaces, and they developed a theoretical model based on experiments with glass beads coated with paraffin or TFE telomer. The self-cleaning property of superhydrophobic micro-nanostructured surfaces was reported in 1977. Perfluoroalkyl, perfluoropolyether, and RF plasma -formed superhydrophobic materials were developed, used for electrowetting and commercialized for bio-medical applications between 1986 and 1995. Other technology and applications have emerged since the mid-1990s. A durable superhydrophobic hierarchical composition, applied in one or two steps, was disclosed in 2002 comprising nano-sized particles ≤ 100 nanometers overlaying a surface having micrometer-sized features or particles ≤ 100 micrometers. The larger particles were observed to protect the smaller particles from mechanical abrasion.
In recent research, superhydrophobicity has been reported by allowing alkylketene dimer (AKD) to solidify into a nanostructured fractal surface. Many papers have since presented fabrication methods for producing superhydrophobic surfaces including particle deposition, sol-gel techniques, plasma treatments, vapor deposition, and casting techniques. Current opportunity for research impact lies mainly in fundamental research and practical manufacturing. Debates have recently emerged concerning the applicability of the Wenzel and Cassie–Baxter models. In an experiment designed to challenge the surface energy perspective of the Wenzel and Cassie–Baxter model and promote a contact line perspective, water drops were placed on a smooth hydrophobic spot in a rough hydrophobic field, a rough hydrophobic spot in a smooth hydrophobic field, and a hydrophilic spot in a hydrophobic field. Experiments showed that the surface chemistry and geometry at the contact line affected the contact angle and contact angle hysteresis, but the surface area inside the contact line had no effect. An argument that increased jaggedness in the contact line enhances droplet mobility has also been proposed.
Many hydrophobic materials found in nature rely on Cassie's law and are biphasic on the submicrometer level with one component air. The lotus effect is based on this principle. Inspired by it, many functional superhydrophobic surfaces have been prepared.
An example of a bionic or biomimetic superhydrophobic material in nanotechnology is nanopin film.
One study presents a vanadium pentoxide surface that switches reversibly between superhydrophobicity and superhydrophilicity under the influence of UV radiation. According to the study, any surface can be modified to this effect by application of a suspension of rose-like V2O5 particles, for instance with an inkjet printer. Once again hydrophobicity is induced by interlaminar air pockets (separated by 2.1 nm distances). The UV effect is also explained. UV light creates electron-hole pairs, with the holes reacting with lattice oxygen, creating surface oxygen vacancies, while the electrons reduce V5+ to V3+. The oxygen vacancies are met by water, and it is this water absorbency by the vanadium surface that makes it hydrophilic. By extended storage in the dark, water is replaced by oxygen and hydrophilicity is once again lost.
A significant majority of hydrophobic surfaces have their hydrophobic properties imparted by structural or chemical modification of a surface of a bulk material, through either coatings or surface treatments. That is to say, the presence of molecular species (usually organic) or structural features results in high contact angles of water. In recent years, rare earth oxides have been shown to possess intrinsic hydrophobicity. The intrinsic hydrophobicity of rare earth oxides depends on surface orientation and oxygen vacancy levels, and is naturally more robust than coatings or surface treatments, having potential applications in condensers and catalysts that can operate at high temperatures or corrosive environments.
Applications and potential applications.
Hydrophobic concrete has been produced since the mid-20th century.
Active recent research on superhydrophobic materials might eventually lead to more industrial applications.
A simple routine of coating cotton fabric with silica or titania particles by sol-gel technique has been reported, which protects the fabric from UV light and makes it superhydrophobic.
An efficient routine has been reported for making polyethylene superhydrophobic and thus self-cleaning. 99% of dirt on such a surface is easily washed away.
Patterned superhydrophobic surfaces also have promise for lab-on-a-chip microfluidic devices and can drastically improve surface-based bioanalysis.
In pharmaceuticals, hydrophobicity of pharmaceutical blends affects important quality attributes of final products, such as drug dissolution and hardness. Methods have been developed to measure the hydrophobicity of pharmaceutical materials.
The development of hydrophobic passive daytime radiative cooling (PDRC) surfaces, whose effectiveness at solar reflectance and thermal emittance is predicated on their cleanliness, has improved the "self-cleaning" of these surfaces. Scalable and sustainable hydrophobic PDRCs that avoid VOCs have further been developed.
References.
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| https://en.wikipedia.org/wiki?curid=14136 |
14136425 | Fåhræus–Lindqvist effect | The Fåhræus–Lindqvist effect () or sigma effect describes how the viscosity of a fluid, in this case blood, changes with the diameter of the tube it travels through. In particular there is a 'decrease in viscosity as the tube's diameter "decreases"' (although only with a tube diameter of between 10 and 300 micrometers). This is because erythrocytes move over to the centre of the vessel, leaving only plasma near the wall of the vessel.
History.
The effect was first documented by a German group in 1930. Shortly after, in 1931, it was reported independently by the Swedish scientists Robin Fåhræus and Torsten Lindqvist, after whom the effect is commonly named. Robert (Robin) Sanno Fåhræus was a Swedish pathologist and hematologist, born on October 15, 1888, in Stockholm. He died on September 18, 1968, in Uppsala, Sweden. Johan Torsten Lindqvist was a Swedish physician, who was born in 1906 and died in 2007. Fåhræus and Lindqvist published their article in the American Journal of Physiology in 1931 describing the effect. Their study represented an important advance in the understanding of hemodynamics which had widespread implications for the study of human physiology.
They forced blood through fine glass capillary tubes connecting two reservoirs. Capillary diameters were less than 250 μm, and experiments were conducted at sufficiently high shear rates (≥100 1/s) so that a similar flow in a large tube would be effectively Newtonian. After correcting for entrance effects, they presented their data in terms of an effective viscosity, derived from fitting measured pressure drop and volume flow rate to Hagen–Poiseuille equation for a tube of radius R
formula_0
where:
formula_1 is the volumetric flow rate
formula_2 is the pressure drop across the capillary
formula_3 is the length of capillary
formula_4 is the effective viscosity
formula_5 is the radius
formula_6 is the mathematical constant
Although the Hagen–Poiseuille equation is only valid for a Newtonian fluid, fitting experimental data to this equation provides a convenient method of characterizing flow resistance by a single number, namely formula_4. In general, formula_4 will depend on the fluid being tested, the capillary diameter, and the flow rate (or pressure drop). However, for a given fluid and a fixed pressure drop, data can be compared between capillaries of differing diameter.
Fahræus and Lindqvist noticed two unusual features of their data. First, formula_4 decreased with decreasing capillary radius, R. This decrease was most pronounced for capillary diameters < 0.5mm. Second, the tube hematocrit (i.e., the average hematocrit in the capillary) was always less than the hematocrit in the feed reservoir. The ratio of these two hematocrits, the tube relative hematocrit, formula_7, is defined as
formula_8
Explanation of phenomena.
These initially confusing results can be explained by the concept of a plasma cell-free layer, a thin layer adjacent to the capillary wall that is depleted of red blood cells. Because the cell-free layer is red cell-poor, its effective viscosity is lower than that of whole blood. This layer therefore acts to reduce flow resistance within the capillary. This has the net effect that the effective viscosity is less than that for whole blood. Because the cell-free layer is very thin (approximately 3 μm) this effect is insignificant in capillaries whose diameter is large. This explanation, while accurate, is ultimately unsatisfying, since it fails to answer the fundamental question of why a plasma cell-free layer exists. There are actually two factors which promote cell-free layer formation.
Cell-free marginal layer model is a mathematical model which tries to explain Fåhræus–Lindqvist effect mathematically.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" /> | [
{
"math_id": 0,
"text": " \\ Q = \\frac{ \\pi R^4 \\Delta P}{ 8 \\mu_{e} L } "
},
{
"math_id": 1,
"text": "Q"
},
{
"math_id": 2,
"text": "\\Delta P "
},
{
"math_id": 3,
"text": "L"
},
{
"math_id": 4,
"text": " \\mu_{e} "
},
{
"math_id": 5,
"text": "R"
},
{
"math_id": 6,
"text": " \\pi "
},
{
"math_id": 7,
"text": " H_{R} "
},
{
"math_id": 8,
"text": " \\mathrm{H_{R}} = { \\mbox{tube hematocrit} \\over \\mbox{feed reservoir hematocrit}} "
}
]
| https://en.wikipedia.org/wiki?curid=14136425 |
1413809 | Incomplete polylogarithm | In mathematics, the Incomplete Polylogarithm function is related to the polylogarithm function. It is sometimes known as the incomplete Fermi–Dirac integral or the incomplete Bose–Einstein integral. It may be defined by:
formula_0
Expanding about z=0 and integrating gives a series representation:
formula_1
where Γ(s) is the gamma function and Γ(s,x) is the upper incomplete gamma function. Since Γ(s,0)=Γ(s), it follows that:
formula_2
where Lis(.) is the polylogarithm function. | [
{
"math_id": 0,
"text": "\n\\operatorname{Li}_s(b,z) = \\frac{1}{\\Gamma(s)}\\int_b^\\infty \\frac{x^{s-1}}{e^{x}/z-1}~dx.\n"
},
{
"math_id": 1,
"text": "\n\\operatorname{Li}_s(b,z) = \\sum_{k=1}^\\infty \\frac{z^k}{k^s}~\\frac{\\Gamma(s,kb)}{\\Gamma(s)}\n"
},
{
"math_id": 2,
"text": "\n\\operatorname{Li}_s(0,z) =\\operatorname{Li}_s(z)\n"
}
]
| https://en.wikipedia.org/wiki?curid=1413809 |
14139597 | ABS methods | Methods for generating algorithms
ABS methods, where the acronym contains the initials of Jozsef Abaffy, Charles G. Broyden and Emilio Spedicato, have been developed since 1981 to generate a large class of algorithms for the following applications:
At the beginning of 2007 ABS literature consisted of over 400 papers and reports and two monographs, one due to Abaffy and Spedicato and published in 1989, one due to Xia and Zhang and published, in Chinese, in 1998. Moreover, three conferences had been organized in China.
Research on ABS methods has been the outcome of an international collaboration coordinated by Spedicato of university of Bergamo, Italy. It has involved over forty mathematicians from Hungary, UK, China, Iran and other countries.
The central element in such methods is the use of a special matrix transformation due essentially to the Hungarian mathematician Jenő Egerváry, who investigated its main properties in some papers that went unnoticed.
For the basic problem of solving a linear system of "m" equations in "n" variables, where formula_0, ABS methods use the following simple geometric idea:
Among the main results obtained so far:
Knowledge of ABS methods is still quite limited among mathematicians, but they have great potential for improving the methods currently in use. | [
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"text": "\\scriptstyle m \\,\\leq\\, n"
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| https://en.wikipedia.org/wiki?curid=14139597 |
14140948 | Arsenate reductase (azurin) | Arsenate reductase (azurin) (EC 1.20.9.1) is an enzyme that catalyzes the chemical reaction
arsenite + H2O + 2 azurinox formula_0 arsenate + 2 azurinred + 2 H+
The 3 substrates of this enzyme are arsenite, water, and oxidised azurin, whereas its 3 products are arsenate, reduced azurin, and hydrogen ion.
Classification.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with a copper protein as acceptor.
Nomenclature.
The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase.
Structure and function.
The enzyme contains a molybdopterin centre comprising two molybdopterin guanosine dinucleotide cofactors bound to molybdenum, a [3Fe-4S] cluster and a Rieske-type [2Fe-2S] cluster. Also uses a c-type cytochrome or O2 as acceptors.
References.
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| https://en.wikipedia.org/wiki?curid=14140948 |
14140963 | Arsenate reductase (donor) | Arsenate reductase (donor) (EC 1.20.99.1) is an enzyme that catalyzes the chemical reaction
arsenite + acceptor formula_0 arsenate + reduced acceptor
Thus, the two substrates of this enzyme are arsenite and an acceptor, whereas its two products are arsenate and a reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with other acceptors. The systematic name of this enzyme class is arsenate:acceptor oxidoreductase. This enzyme is also called arsenate:(acceptor) oxidoreductase.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14140963 |
14140974 | Arsenate reductase (glutaredoxin) | Enzyme family
Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction
arsenate + glutaredoxin formula_0 arsenite + glutaredoxin disulfide + H2O
Thus, the two substrates of this enzyme are arsenate and glutaredoxin, whereas its 3 products are arsenite, glutaredoxin disulfide, and water.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is glutaredoxin:arsenate oxidoreductase.
Structural studies.
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1RXE, 1RXI, 1S3C, 1S3D, 1SD8, 1SD9, 1SJZ, 1SK0, 1SK1, 1SK2, 1Z2D, and 1Z2E.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14140974 |
14140985 | Methylarsonate reductase | In enzymology, a methylarsonate reductase (EC 1.20.4.2) is an enzyme that catalyzes the chemical reaction
methylarsonate + 2 glutathione formula_0 methylarsonite + glutathione disulfide + H2O
Thus, the two substrates of this enzyme are methylarsonate and glutathione, whereas its 3 products are methylarsonite, glutathione disulfide, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is gluthathione:methylarsonate oxidoreductase. This enzyme is also called MMA(V) reductase.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
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"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14140985 |
14141001 | Phosphonate dehydrogenase | In enzymology, a phosphonate dehydrogenase (EC 1.20.1.1) is an enzyme that catalyzes the chemical reaction
phosphonate + NAD+ + H2O formula_0 phosphate + NADH + H+
The 3 substrates of this enzyme are phosphonate, NAD+, and H2O, whereas its 3 products are phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phosphonate:NAD+ oxidoreductase. Other names in common use include NAD:phosphite oxidoreductase, and phosphite dehydrogenase.
References.
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{
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"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141001 |
14141149 | 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase | Enzyme
In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase (EC 1.17.99.3) is an enzyme that catalyzes the chemical reaction
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor formula_0 (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor
The 3 substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA, H2O, and acceptor, whereas its two products are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:ac ceptor 24-oxidoreductase (24R-hydroxylating). Other names in common use include trihydroxycoprostanoyl-CoA oxidase, THC-CoA oxidase, THCA-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase. This enzyme participates in the ppar signaling pathway.
References.
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"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141149 |
14141159 | 4-Cresol dehydrogenase (hydroxylating) | Class of enzymes
In enzymology, a 4-cresol dehydrogenase (hydroxylating) (EC 1.17.99.1) is an enzyme that catalyzes the chemical reaction
4-cresol + acceptor + H2O formula_0 4-hydroxybenzaldehyde + reduced acceptor
The 3 substrates of this enzyme are 4-cresol, acceptor, and H2O, whereas its two products are 4-hydroxybenzaldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is 4-cresol:acceptor oxidoreductase (methyl-hydroxylating). Other names in common use include p"-cresol–(acceptor) oxidoreductase (hydroxylating), and p"-cresol methylhydroxylase. This enzyme participates in toluene and xylene degradation. It has 2 cofactors: FAD, and Cytochrome c.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1DII, 1DIQ, 1WVE, and 1WVF.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141159 |
14141179 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase | Class of enzymes
In enzymology, a 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (HMB-PP synthase, IspG, EC 1.17.7.1) is an enzyme that catalyzes the chemical reaction
2-C-methyl-D-erythritol 2,4-cyclodiphosphate + protein-dithiol formula_0 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + protein-disulfide
The substrate of this enzyme is 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MEcPP) and the product is (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate (HMB-PP). Electrons are donated by two reduced ferredoxin proteins per reaction.
This enzyme participates in the MEP pathway (non-mevalonate pathway) of Isoprenoid precursor biosynthesis.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with a disulfide as acceptor. The systematic name of this enzyme class is (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating).
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141179 |
14141196 | 6-hydroxynicotinate dehydrogenase | Class of enzymes
In enzymology, a 6-hydroxynicotinate dehydrogenase (EC 1.17.3.3) is an enzyme that catalyzes the chemical reaction
6-hydroxynicotinate + H2O + O2 formula_0 2,6-dihydroxynicotinate + H2O2
The 3 substrates of this enzyme are 6-hydroxynicotinate, H2O, and O2, whereas its two products are 2,6-dihydroxynicotinate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with oxygen as acceptor. The systematic name of this enzyme class is 6-hydroxynicotinate:O2 oxidoreductase. Other names in common use include 6-hydroxynicotinic acid hydroxylase, 6-hydroxynicotinic acid dehydrogenase, and 6-hydroxynicotinate hydroxylase.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141196 |
14141234 | CDP-4-dehydro-6-deoxyglucose reductase | CDP-4-dehydro-6-deoxyglucose reductase (EC 1.17.1.1) is an enzyme that catalyzes the chemical reaction
CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O formula_0 CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
The 4 substrates of this enzyme are CDP-4-dehydro-3,6-dideoxy-D-glucose, nicotinamide adenine dinucleotide ion, nicotinamide adenine dinucleotide phosphate ion, and water, whereas its 4 products are CDP-4-dehydro-6-deoxy-D-glucose, nicotinamide adenine dinucleotide, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is CDP-4-dehydro-3,6-dideoxy-D-glucose:NAD(P)+ 3-oxidoreductase. Other names in common use include CDP-4-keto-6-deoxyglucose reductase, cytidine diphospho-4-keto-6-deoxy-D-glucose reductase, cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase, CDP-4-keto-deoxy-glucose reductase, CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system, and NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase. This enzyme participates in starch and sucrose metabolism.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141234 |
14141245 | Cob(II)alamin reductase | In enzymology, a cob(II)alamin reductase (EC 1.16.1.4) is an enzyme that catalyzes the chemical reaction
2 cob(I)alamin + NAD+ formula_0 2 cob(II)alamin + NADH + H+
Thus, the two substrates of this enzyme are cob(I)alamin and NAD+, whereas its 3 products are cob(II)alamin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cob(I)alamin:NAD+ oxidoreductase. Other names in common use include vitamin B12r reductase, B12r reductase, and NADH2:cob(II)alamin oxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, FAD.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141245 |
14141258 | Cob(II)yrinic acid a,c-diamide reductase | In enzymology, a cob(II)yrinic acid a,c-diamide reductase (EC 1.16.8.1) is an enzyme that catalyzes the chemical reaction
2 cob(I)yrinic acid a,c-diamide + FMN + 3 H+ formula_0 2 cob(II)yrinic acid a,c-diamide + FMNH2
The three substrates of this enzyme are cob(I)yrinic acid a,c-diamide, flavin mononucleotide, and H+; its two products are cob(II)yrinic acid a,c-diamide and FMNH2.
Classification.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with a flavin as acceptor.
Nomenclature.
The systematic name of this enzyme class is cob(I)yrinic acid-a,c-diamide:FMN oxidoreductase. This enzyme is also called CobR and cob(II)yrinic acid-a,c-diamide:FMN oxidoreductase (incorrect).
Biological role.
This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141258 |
14141267 | Cyanocobalamin reductase (cyanide-eliminating) | In enzymology, a cyanocobalamin reductase (cyanide-eliminating) (EC 1.16.1.6) is an enzyme that catalyzes the chemical reaction
cob(I)alamin + cyanide + NADP+ formula_0 cyanocob(III)alamin + NADPH + H+
The 3 substrates of this enzyme are cob(I)alamin, cyanide, and NADP+, whereas its 3 products are cyanocob(III)alamin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those that oxidize metal ions and use NAD+ or NADP+ as an electron acceptor (for that oxidization reaction). The systematic name of this enzyme class is cob(I)alamin, cyanide:NADP+ oxidoreductase. Other names in common use include cyanocobalamin reductase, cyanocobalamin reductase (NADPH, cyanide-eliminating), cyanocobalamin reductase (NADPH, CN-eliminating), and NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating). This enzyme participates in porphyrin and chlorophyll metabolism. It uses one cofactor, FAD.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
"math_id": 0,
"text": "\\rightleftharpoons"
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| https://en.wikipedia.org/wiki?curid=14141267 |
14141273 | Diferric-transferrin reductase | In enzymology, a diferric-transferrin reductase (EC 1.16.1.2) is an enzyme that catalyzes the chemical reaction
transferrin[Fe(II)]2 + NAD+ + H+ formula_0 transferrin[Fe(III)]2 + NADH
The 3 substrates of this enzyme are transferrin[Fe(II)]2, NAD+, and H+, whereas its two products are transferrin[Fe(III)]2 and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is transferrin[Fe(II)]2:NAD+ oxidoreductase. Other names in common use include diferric transferrin reductase, NADH diferric transferrin reductase, and transferrin reductase. This enzyme participates in porphyrin and chlorophyll metabolism.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1L5T.
References.
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| https://en.wikipedia.org/wiki?curid=14141273 |
14141280 | Ethylbenzene hydroxylase | In enzymology, an ethylbenzene hydroxylase (EC 1.17.99.2) is an enzyme that catalyzes the chemical reaction
ethylbenzene + H2O + acceptor formula_0 (S)-1-phenylethanol + reduced acceptor
The 3 substrates of this enzyme are ethylbenzene, H2O, and acceptor, whereas its two products are (S)-1-phenylethanol and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is ethylbenzene:acceptor oxidoreductase. Other names in common use include ethylbenzene dehydrogenase, and ethylbenzene:(acceptor) oxidoreductase. This enzyme participates in ethylbenzene degradation by "Aromatoleum aromaticum", a denitrifying bacterium related to the genera "Azoarcus" and "Thauera". It is a molybdenum enzyme belonging to the DMSO reductase family. Molybdenum enzymes are distinguished by the presence of a unique active site containing molybdenum atom, one or two molybdopterins and additional ligands (i.e. aminoacid residue of Ser, Cys, SeCys or Asp and very often oxygen Mo=O ligand). EBDH is synthesized exclusively in cells grown anaerobically on ethylbenzene and has been identified as a soluble periplasmic protein.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2IVF. EBDH consists of three subunits of 96, 43, and 23 kDa, and contains a molybdenum cofactor and a heme b559 cofactor linked by a linear row of five iron-sulfur clusters.
Mechanism.
The reaction is catalyzed by the enzyme using a molybdenum cofactor (MoCo), which in the native state consists of a molybdenum (VI) nucleus ligated by two molybdopterin guanine dinucleotide (MGD) ligands and an aspartic acid residue. Two electrons acquired by the cofactor during the reaction, i.e., the hydroxylation of the hydrocarbon, are then transferred via a chain of iron-sulfur clusters connecting the molybdenum with a heme b cofactor in the alpha subunit, from which the electrons are donated to a yet-unknown acceptor. Notably, EBDH exhibits in vitro activity only with artificial electron acceptors of high redox potential, like the ferricenium ion (E0’= +380 mV). This suggests that its natural electron acceptor may be a periplasmic cytochrome c of similarly high potential, which would couple the ethylbenzene oxidation to the nitrate respiration of "A. aromaticum".
The EBDH catalytic cycle has two parts: i) oxidation part, where substrate is oxidized to alcohols and the enzyme is reduced to its catalytically inactive form, and ii) enzyme re-oxidation part, where EBDH active site (MoCo) is oxidized and restored to its catalytically active form.
Recent theoretical and experimental studies point toward radical C-H activation as the initial reaction and rate limiting step. A possible alternative hydride transfer seems to be less likely. The mechanism concludes with conversion of the hydrocarbon to a carbocation intermediate and rebound of a hydroxide to form the hydroxylated product. Moreover, a histidine residue (His192) of the active site seems to be involved in the reaction mechanism.
References.
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| https://en.wikipedia.org/wiki?curid=14141280 |
14141433 | Ferredoxin—NADP(+) reductase | In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction
2 reduced ferredoxin + NADP+ + H+ formula_0 2 oxidized ferredoxin + NADPH
The 3 substrates of this enzyme are reduced ferredoxin, NADP+, and H+, whereas its two products are oxidized ferredoxin and NADPH. It has a flavin cofactor, FAD.
This enzyme belongs to the family of oxidoreductases, that use iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors.
This enzyme participates in photosynthesis. FNR provides a major source of NADPH for photosynthetic organisms.
Nomenclature.
The systematic name of this enzyme class is ferredoxin:NADP+ oxidoreductase. Other names in common use include:
<templatestyles src="Div col/styles.css"/>
Mechanism.
During photosynthesis, electrons are removed from water and transferred to the single electron carrier ferredoxin. Ferredoxin: NADP+ reductase then transfers an electron from each of two ferredoxin molecules to a single molecule of the two electron carrier NADPH. FNR utilizes FAD, which can exist in an oxidized state, single electron reduced semiquinone state, and fully reduced state to mediate this electron transfer.
FNR has an induced-fit mechanism of catalysis. Binding of ferredoxin to the enzyme causes the formation of a hydrogen bond between a glutamate residue (E312) and a serine residue (S96) in the active site. The glutamate residue is highly conserved because it both stabilizes the semiquinone form of FAD and is a proton donor/acceptor in the reaction. The rate limiting step of the electron transfer reaction is the release of the first oxidized ferredoxin molecule after the reduction of FAD with one electron. This step is inhibited by the presence of oxidized ferredoxin and stimulated by the presence of NADP+. The binding of NADP+ to the enzyme lowers the binding affinity of the enzyme for ferredoxin.
This reaction can also operate in reverse to generate reduced ferredoxin, which can then be used in a variety of biosynthetic pathways. Some bacteria and algae use the molecule flavodoxin instead of ferredoxin as the single electron carrier molecule to be reduced or oxidized.
Structure.
Plant-type ferredoxin: NADP+ reductase has two structural domains. The first domain is an antiparallel beta barrel at the amino terminus of the protein that contains the binding domain for the FAD cofactor. The second domain is at the carboxyl terminus of the protein and contains an alpha helix-beta strand fold. This terminal domain is where the NADP+ binds. The active site for the enzyme occurs at the interface between the two domains.
Binding of the enzyme to the thylakoid membrane involves a polyproline type II helix created between two FNR monomers and several proline rich integral membrane proteins.
As of late 2007, 54 structures had been solved for this class of enzymes, with PDB accession codes 1B2R, 1BJK, 1BQE, 1BX0, 1BX1, 1CJC, 1E1L, 1E62, 1E63, 1E64, 1E6E, 1EWY, 1FDR, 1FNB, 1FNC, 1FND, 1FRN, 1FRQ, 1GAQ, 1GAW, 1GJR, 1GO2, 1GR1, 1H42, 1H85, 1JB9, 1OGI, 1OGJ, 1QFY, 1QFZ, 1QG0, 1QGA, 1QGY, 1QGZ, 1QH0, 1QUE, 1QUF, 1SM4, 1W34, 1W35, 1W87, 2B5O, 2BGI, 2BGJ, 2BMW, 2BSA, 2C7G, 2GQW, 2GR0, 2GR1, 2GR2, 2GR3, 2OK7, and 2OK8.
Function.
Ferredoxin: NADP+ reductase is the last enzyme in the transfer of electrons during photosynthesis from photosystem I to NADPH. The NADPH is then used as a reducing equivalent in the reactions of the Calvin cycle. Electron cycling from ferredoxin to NADPH only occurs in the light in part because FNR activity is inhibited in the dark. In nonphotosynthetic organisms, the FNR primarily works in reverse to provide reduced ferredoxin for various metabolic pathways. These pathways include nitrogen fixation, terpenoid biosynthesis, steroid metabolism, oxidative stress response, and iron–sulfur protein biogenesis.
FNR is a soluble protein that is found both free in the chloroplast stroma and bound to the thylakoid membrane. This binding occurs opposite to the active site of the enzyme and does not seem to affect the structure of the active site or have a significant impact on the enzyme's activity. When bound to the thylakoid membrane, the enzyme exists as a dimer, but when it is free in the stroma, it is monomeric. The binding of the FNR to the integral membrane proteins on the thylakoid membrane is enhanced under acidic conditions, so recruitment and binding of FNR to the thylakoid membrane may be a method of storing and stabilizing the enzyme in the dark when photosynthesis is not occurring. The chloroplast stroma varies from being slightly acidic in the dark to more alkaline in the light. Therefore, in the dark, more FNRs would be recruited and bound to the thylakoid membrane, and in the light, more FNRs would dissociate from the membrane and be free in the stroma.
Evolution.
Ferredoxin NADP+ reductases are present in many organisms, including plants, bacteria, and the mitochondria of eukaryotes. However, these proteins belong to two unrelated protein families and are an example of convergent evolution. The plant-type FNRs (InterPro: "IPR015701", InterPro: "IPR033892") include the plastidic FNRs seen in plants. The glutathione-reductase-type FNRs (InterPro: "IPR022890", InterPro: "IPR021163"), sometimes named adrenodoxin-NADP+ reductase for distinction, are seen in the mitochondria of eukaryotes. Both families are seen in bacteria. Two extra families, one thioredoxin reductase-like (TRLF) and the other with a unique mechanism (NfnAB), has been identified.
In the plant-like family of FNRs, selective evolutionary pressure has led to differences in the catalytic efficiency of FNRs in photosynthetic and nonphotosynthetic organisms. Electron transfer by FNR is a rate limiting step in photosynthesis, so the plastidic FNR in plants have evolved to be highly efficient. These plastidic FNRs are 20–100 fold more active than bacterial FNRs. This higher catalytic efficiency of the transfer of electrons from FAD to NADP+ is related to structural changes in the active site that reduce the distance between the N5 in FAD and the C4 in NADP+. The plastidic FNRs in plants have also evolved to have a high degree of substrate specificity for NADP+ over NAD+; studies of amino acid mutations have shown that the terminal tyrosine residue in plastidic FNRs plays a key role in this substrate specificity. In contrast, some nonphotosynthetic FNRs do not preferentially bind NADP+ and lack this tyrosine residue.
Disease relevance.
Several major human diseases are caused by the obligate intracellular protozoan parasites in the phylum Apicomplexa. The apicoplast organelle in these organisms is believed to have come from an endosymbiotic event in which an ancestral protozoan engulfed an algal cell. These apicoplasts contain plant-like FNRs that the protozoan uses to generate reduced ferredoxin, which is then used as a reductant in essential biosynthetic pathways. FNRs from two major parasites affecting humans, "Plasmodium falciparum", which causes malaria, and "Toxoplasma gondii", which causes toxoplasmosis, have been sequenced. Since humans do not have a homologous protein, these enzymes are possible new targets for drug therapies against these diseases.
References.
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Further reading.
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14141440 | Ferredoxin—NAD(+) reductase | In enzymology, a ferredoxin–NAD+ reductase (EC 1.18.1.3) is an enzyme that catalyzes the chemical reaction:
reduced ferredoxin + NAD+ formula_0 oxidized ferredoxin + NADH + H+
Thus, the two substrates of this enzyme are reduced ferredoxin and NAD+, whereas its 3 products are oxidized ferredoxin, NADH, and H+. This enzyme participates in fatty acid metabolism.
This enzyme belongs to the family of oxidoreductases, specifically those acting on iron-sulfur proteins as donor with NAD+ or NADP+ as acceptor.
The systematic name of this enzyme is ferredoxin:NAD+ oxidoreductase. There are a variety of names in common use:
When NAD molecule is in its reduced form, the enzyme is referred to as:
Other enzymes in the family include:
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1KRH.
References.
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14141451 | Ferric-chelate reductase | In enzymology, a ferric-chelate reductase (EC 1.16.1.7) is an enzyme that catalyzes the chemical reaction
2 Fe(II) + NAD+ formula_0 2 Fe(III) + NADH + H+
Thus, the two substrates of this enzyme are Fe(II) and NAD+, whereas its 3 products are Fe(III), NADH, and H+.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is Fe(II):NAD+ oxidoreductase. Other names in common use include:
Prokaryotes.
Most studied ferric reductases in bacteria are either specific for a ferric iron complex or non-specific flavin ferric reductases, with the latter being more common in bacteria. Both reductase forms are suitable complimentary soluble pathways for the efficient extraction of iron via siderophores.
Bacterial soluble flavin reductase in "E. coli".
Non-specific bacterial flavin reductase has been well researched within "E. coli", which is the NAD(P)H: flavin oxidoreductase (Fre). In "E. coli", NAD(P)H is reduced to either free FAD or riboflavin, which is known to reduce ferric iron to ferrous iron intracellularly. Fre is also structurally similar to ferredoxin-NADP+ reductase (Fpr), and bids flavin cofactor to reduce ferredoxin and siderophore bound ferric iron. Despite these hypothesized structural commonalities, not much is known regarding this enzymatic structure overall.
Bacterial flavin reductase in "Paracoccus denitrificans".
"Paracoccus denitrificans" contains two enzymes which aid in iron reduction - ferric reductase A and B (FerA and FerB). FerA binds to oxidized flavins (FMN and FAD). Unlike the many structural unknowns surrounding Fre, the crystal structure of FerA is well defined (see ). FerA consists of two protein subunits, with three alpha-helices and ten beta-sheets total.
Archaeal soluble flavin reductase in "Archaeoglobus fulgidus".
"Archaeoglobus fulgidus" has been shown to have a similar ferric reductase (FeR) to the NAD(P)H:flavin oxidoreductase family. FeR is archaea specific and reduces external, synthetic ferric iron complexes and Fe(III)-citrate with NAD(P)H and bound flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) cofactor.
Eukaryotes.
Soluble ferric reductase in yeast.
Ferric reductases are present in some unicellular eukaryotes, including pathogenic yeast which utilize ferric reductases during infection of a host. Contrary to archaea and bacteria, soluble ferric reductases are much more rare in fungi, with more research necessary to determine just how widespread soluble ferric reductase are amongst fungi. These soluble ferric reductases in fungi are known to operate extracellularly, as fungi are capable of excreting them to reduce iron in the environment. This mechanism of ferric reductase excretion allows the labilization of iron in the environment, and typically happens concurrently with fungal siderophore pathways and iron reduction on cellular surfaces, which occur with membrane-bound ferric reductases.
Membrane-bound ferric reductase in yeast.
Membrane-bound ferric reductases are fore more common in yeast cells relative to soluble ferric reductases. These reductases utilize NAD(P)H, falvin, and heme "b" cofactors in order to move reducing agents across their membranes to an extracellular Fe(III) source. After this, the reduced Fe(II) may be re-oxidized and rebound to be transported across the membrane again via both Cu-dependent ferroxidase and Fe(III) transport proteins. Alternatively, ferrous, unchelated iron can be transported via low-affinity proteins, however, this mechanism is less common than the former.
Membrane-bound ferric reductase in "Arabidopsis".
Most plants contain ferric-chelate reductase in order to uptake iron from the environment. "Arabidopsis" is capable of increasing the activity of ferric-chelate reductase, which is located in the membranes of root epidermal cells, in environments with limited iron availability. Additionally, it is hypothesized that the activity of this reductase stimulates iron release from organic compounds within the soils, releasing it for biological uptake. The crystalline structure of this enzyme in "Arabidopsis" has not yet been well constrained, however, it is hypothesized that, due to its similar functions, its structure is likely similar to ferric-chelate reductases in both yeast and human phagocytic NADPH oxidase gp91phox.
References.
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Further reading.
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14141467 | Leucoanthocyanidin reductase | In enzymology, a leucoanthocyanidin reductase (EC 1.17.1.3) (LAR, aka leucocyanidin reductase or LCR) is an enzyme that catalyzes the chemical reaction
(2R,3S)-catechin + NADP+ + H2O formula_0 2,3-trans-3,4-cis-leucocyanidin + NADPH + H+
The 3 substrates of this enzyme are (2R,3S)-catechin, NADP+, and H2O, whereas its 3 products are 2,3-trans-3,4-cis-leucocyanidin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2R,3S)-catechin:NADP+ 4-oxidoreductase. This enzyme is also called leucocyanidin reductase. This enzyme participates in flavonoid biosynthesis.
The enzyme can be found in the plant "Hedysarum sulphurescens" and in "Vitis vinifera" (grape).
References.
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Further reading.
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14141495 | (Methionine synthase) reductase | Class of enzymes
[Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine synthase inside human body. This enzyme is crucial for maintaining the one carbon metabolism, specifically the folate cycle. The enzyme employs one coenzyme, flavoprotein.
Mechanism.
MTRR works by catalyzing the following chemical reaction:
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ formula_0 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine
The 3 products of this enzyme are methionine synthase-methylcob(I)alamin, S-adenosylhomocysteine, and NADP+, whereas its 4 substrates are methionine synthase-cob(II)alamin, NADPH, H+, and S-adenosyl-L-methionine.
Physiologically speaking, one crucial enzyme participated in the folate cycle is methionine synthase, which incorporated a coenzyme, cobalamin, also known as Vitamin B12. The coenzyme utilizes its cofactor, cobalt to catalyze the transferring function, in which the cobalt will switch between having 1 or 3 valence electrons, dubbed cob(I)alamin, and cob(III)alamin.
Over time, the cob(I)alamin cofactor of methionine synthase becomes oxidized to cob(II)alamin, rendering the enzyme inactive. Therefore, regeneration of the enzyme is necessary. Regeneration requires reductive methylation via a reaction catalyzed by (methionine synthase) reductase in which S-adenosylmethionine is utilized as a methyl donor, reducing cob(II)alamin to cob(I)alamin.
Systematic naming.
This enzyme belongs to the family of oxidoreductases, to be specific those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is [methionine synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+ oxidoreductase. Other names in common use include methionine synthase cob(II)alamin reductase (methylating), methionine synthase reductase, [methionine synthase]-cobalamin methyltransferase (cob(II)alamin, and reducing).
References.
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14141524 | Nitrogenase (flavodoxin) | Nitrogenase (flavodoxin) (EC 1.19.6.1) is an enzyme with systematic name "reduced flavodoxin:dinitrogen oxidoreductase (ATP-hydrolysing)". This enzyme catalyses the following chemical reaction
6 reduced flavodoxin + 6 H+ + N2 + n ATP formula_0 6 oxidized flavodoxin + 2 NH3 + n ADP + n phosphate
The enzyme is a complex of two proteins containing iron-sulfur centres and molybdenum.
References.
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14141530 | Phenylacetyl-CoA dehydrogenase | In enzymology, a phenylacetyl-CoA dehydrogenase (EC 1.17.5.1) is an enzyme that catalyzes the chemical reaction
phenylacetyl-CoA + H2O + 2 quinone formula_0 phenylglyoxylyl-CoA + 2 quinol
The 3 substrates of this enzyme are phenylacetyl-CoA, H2O, and quinone, whereas its two products are phenylglyoxylyl-CoA and quinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with a quinone or similar compound as acceptor. The systematic name of this enzyme class is phenylacetyl-CoA:quinone oxidoreductase. This enzyme is also called phenylacetyl-CoA:acceptor oxidoreductase.
References.
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14141541 | Pteridine oxidase | In enzymology, a pteridine oxidase (EC 1.17.3.1) is an enzyme that catalyzes the chemical reaction
2-amino-4-hydroxypteridine + O2 formula_0 2-amino-4,7-dihydroxypteridine + (?)
Thus, the two substrates of this enzyme are 2-amino-4-hydroxypteridine and O2, whereas its product is 2-amino-4,7-dihydroxypteridine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with oxygen as acceptor. The systematic name of this enzyme class is 2-amino-4-hydroxypteridine:oxygen oxidoreductase (7-hydroxylating).
References.
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14141557 | Rubredoxin—NAD(P)(+) reductase | Enzyme
In enzymology, a rubredoxin—NAD(P)+ reductase (EC 1.18.1.4) is an enzyme that catalyzes the chemical reaction
reduced rubredoxin + NAD(P)+ formula_0 oxidized rubredoxin + NAD(P)H + H+
The 3 substrates of this enzyme are reduced rubredoxin, NAD+, and NADP+, whereas its 4 products are oxidized rubredoxin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on iron-sulfur proteins as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is rubredoxin:NAD(P)+ oxidoreductase. Other names in common use include rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase, rubredoxin-nicotinamide adenine, dinucleotide phosphate reductase, NAD(P)+-rubredoxin oxidoreductase, and NAD(P)H-rubredoxin oxidoreductase. This enzyme participates in fatty acid metabolism.
References.
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14141569 | Rubredoxin—NAD(+) reductase | Enzyme that catalyzes the chemical reaction
In enzymology, a rubredoxin-NAD+ reductase (EC 1.18.1.1) is an enzyme that catalyzes the chemical reaction.
2 reduced rubredoxin + NAD+ + H+ formula_0 2 oxidized rubredoxin + NADH
The 3 substrates of this enzyme are reduced rubredoxin, NAD+, and H+, whereas its two products are oxidized rubredoxin and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on iron-sulfur proteins as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is rubredoxin:NAD+ oxidoreductase. Other names in common use include rubredoxin reductase, rubredoxin-nicotinamide adenine dinucleotide reductase, dihydronicotinamide adenine dinucleotide-rubredoxin reductase, reduced nicotinamide adenine dinucleotide-rubredoxin reductase, NADH-rubredoxin reductase, rubredoxin-NAD reductase, NADH: rubredoxin oxidoreductase, DPNH-rubredoxin reductase, and NADH-rubredoxin oxidoreductase. This enzyme participates in fatty acid metabolism. It has 2 cofactors: FAD and Iron.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1BFY.
References.
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14141577 | Superoxide reductase | Superoxide reductase is an enzyme that catalyzes the conversion of highly reactive and toxic superoxide (O2−) into less toxic hydrogen peroxide (H2O2):
reduced rubredoxin + O2− + 2 H+ formula_0 rubredoxin + H2O2
Fe2+ + O2− + 2 H+ formula_0 Fe3++ H2O2
Hydrogen peroxide in turn is reduced to water by rubrerythrin. The 3 substrates of this enzyme are reduced rubredoxin, superoxide, and H+, whereas its two products are rubredoxin and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on superoxide as acceptor (only sub-subclass identified to date). The systematic name of this enzyme class is rubredoxin:superoxide oxidoreductase. Other names in common use include neelaredoxin, and desulfoferrodoxin.
Structural studies.
As of late 2007[ [update]], 9 structures have been solved for this class of enzymes, with PDB accession codes 1VZG, 1VZH, 1VZI, 1Y07, 2AMU, 2HVB, 2JI1, 2JI2, and 2JI3.
References.
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Further reading.
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1414279 | Absolute neutrophil count | Measure of the number of neutrophils present in blood
Absolute neutrophil count (ANC) is a measure of the number of neutrophil granulocytes (also known as polymorphonuclear cells, PMN's, polys, granulocytes, segmented neutrophils or segs) present in the blood. Neutrophils are a type of white blood cell that fights against infection.
The ANC is almost always a part of a larger blood panel called the complete blood count. The ANC is calculated from measurements of the total number of white blood cells (WBC), usually based on the combined percentage of mature neutrophils (sometimes called "segs", or segmented cells) and bands, which are immature neutrophils.
Clinical significance.
The reference range for ANC in adults varies by study, but 1500 to 8000 cells per microliter is typical. An ANC less than 1500 cells/μL is defined as neutropenia and increases risk of infection. Neutropenia is the condition of a low ANC, and the most common condition where an ANC would be measured is in the setting of chemotherapy for cancer.
Neutrophilia indicates an elevated count. While many clinicians refer to the presence of neutrophilia as a "left shift", this is imprecise, as a left shift indicates the presence of immature neutrophil forms, but neutrophilia refers to the entire mass of neutrophils, both mature and immature. Neutrophilia can be indicative of:
Calculation.
ANC = formula_0
or
ANC = ("Absolute-Polys + Absolute-Bands")
Related tests.
In some cases, a ratio is reported in addition to the sum. This is known as the "I/T ratio".
References.
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"text": "\n(\\%neutrophils + \\%bands)\\times (WBC)\\over (100)\n"
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| https://en.wikipedia.org/wiki?curid=1414279 |
14143029 | 1-hydroxy-2-naphthoate 1,2-dioxygenase | Class of enzymes
In enzymology, a 1-hydroxy-2-naphthoate 1,2-dioxygenase (EC 1.13.11.38) is an enzyme that catalyzes the chemical reaction
1-hydroxy-2-naphthoate + O2 formula_0 (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
Thus, the two substrates of this enzyme are 1-hydroxy-2-naphthoate and O2, whereas its product is (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate.
This enzyme participates in naphthalene and anthracene degradation. It employs one cofactor, iron.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing). Other names in common use include 1-hydroxy-2-naphthoate dioxygenase, 1-hydroxy-2-naphthoate-degrading enzyme, and 1-hydroxy-2-naphthoic acid dioxygenase.
References.
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14143048 | 2,3-dihydroxybenzoate 2,3-dioxygenase | Class of enzymes
In enzymology, a 2,3-dihydroxybenzoate 2,3-dioxygenase (EC 1.13.11.28) is an enzyme that catalyzes the chemical reaction
2,3-dihydroxybenzoate + O2 formula_0 2-carboxy-cis,cis-muconate
Thus, the two substrates of this enzyme are 2,3-dihydroxybenzoate and O2, whereas its product is 2-carboxy-cis,cis-muconate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (decyclizing). This enzyme is also called 2,3-dihydroxybenzoate 2,3-oxygenase.
References.
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14143060 | 2,3-dihydroxybenzoate 3,4-dioxygenase | Class of enzymes
In enzymology, a 2,3-dihydroxybenzoate 3,4-dioxygenase (EC 1.13.11.14) is an enzyme that catalyzes the chemical reaction
2,3-dihydroxybenzoate + O2 formula_0 3-carboxy-2-hydroxymuconate semialdehyde
Thus, the two substrates of this enzyme are 2,3-dihydroxybenzoate and O2, whereas its product is 3-carboxy-2-hydroxymuconate semialdehyde.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include o-pyrocatechuate oxygenase, 2,3-dihydroxybenzoate 1,2-dioxygenase, 2,3-dihydroxybenzoic oxygenase, and 2,3-dihydroxybenzoate oxygenase. This enzyme participates in benzoate degradation via hydroxylation.
References.
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14143078 | 2,3-dihydroxyindole 2,3-dioxygenase | Class of enzymes
In enzymology, a 2,3-dihydroxyindole 2,3-dioxygenase (EC 1.13.11.23) is an enzyme that catalyzes the chemical reaction
2,3-dihydroxyindole + O2 formula_0 anthranilate + CO2
Thus, the two substrates of this enzyme are 2,3-dihydroxyindole and O2, whereas its two products are anthranilate and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing). This enzyme participates in tryptophan metabolism.
References.
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14143101 | 2,4'-dihydroxyacetophenone dioxygenase | Class of enzymes
In enzymology, a 2,4'-dihydroxyacetophenone dioxygenase (EC 1.13.11.41) is an enzyme that catalyzes the chemical reaction
2,4'-dihydroxyacetophenone + O2 formula_0 4-hydroxybenzoate + formate
Thus, the two substrates of this enzyme are 2,4'-dihydroxyacetophenone and O2, whereas its two products are 4-hydroxybenzoate and formate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving). This enzyme is also called (4-hydroxybenzoyl)methanol oxygenase. This enzyme participates in bisphenol a degradation.
References.
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14143118 | 2,5-dihydroxypyridine 5,6-dioxygenase | Class of enzymes
In enzymology, a 2,5-dihydroxypyridine 5,6-dioxygenase (EC 1.13.11.9) is an enzyme that catalyzes the chemical reaction
2,5-dihydroxypyridine + O2 formula_0 N-formylmaleamic acid
The 2 substrates of this enzyme are 2,5-dihydroxypyridine and O2, whereas its product is N-formylmaleamic acid.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. It employs one cofactor, iron.
This enzyme participates in nicotinate and nicotinamide metabolism.
Nomenclature.
The systematic name of this enzyme class is 2,5-dihydroxypyridine:oxygen 5,6-oxidoreductase. Other names in common use include 2,5-dihydroxypyridine oxygenase, and pyridine-2,5-diol dioxygenase.
References.
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Further reading.
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14143130 | 2-nitropropane dioxygenase | Class of enzymes
In enzymology, a 2-nitropropane dioxygenase (EC 1.13.11.32) is an enzyme that catalyzes the chemical reaction
2 2-nitropropane + O2 formula_0 2 acetone + 2 nitrite
Thus, the two substrates of this enzyme are 2-nitropropane and O2, whereas its two products are acetone and nitrite.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 2-nitropropane:oxygen 2-oxidoreductase. This enzyme participates in nitrogen metabolism. It has 3 cofactors: FAD, Iron, and FMN.
Structural studies.
As of late 2007 Steve Fuhrer from the DHPA solved this very complex formula to find, two structures have been solved for this class of enzymes, with PDB accession codes 2GJL and 2GJN.
References.
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14143138 | 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase | Class of enzymes
In enzymology, a 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase (EC 1.13.11.25) is an enzyme that catalyzes the chemical reaction
3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 formula_0 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate
Thus, the two substrates of this enzyme are 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione and O2, whereas its product is .
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (decyclizing). Other names in common use include steroid 4,5-dioxygenase, and 3-alkylcatechol 2,3-dioxygenase. It employs one cofactor, iron.
References.
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| https://en.wikipedia.org/wiki?curid=14143138 |
14143232 | 3,4-dihydroxyphenylacetate 2,3-dioxygenase | Enzyme
In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) is an enzyme that catalyzes the chemical reaction
3,4-dihydroxyphenylacetate + O2 formula_0 2-hydroxy-5-carboxymethylmuconate semialdehyde
Thus, the two substrates of this enzyme are 3,4-dihydroxyphenylacetate and O2, whereas its product is 2-hydroxy-5-carboxymethylmuconate semialdehyde.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing). Other names in common use include 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, HPC dioxygenase, and homoprotocatechuate 2,3-dioxygenase. This enzyme participates in tyrosine metabolism. It employs one cofactor, iron.
Structural studies.
As of late 2007, eight structures have been solved for this class of enzymes, with PDB accession codes 1F1R, 1F1U, 1F1V, 1F1X, 1Q0C, 1Q0O, 2IG9, and 2IGA.
References.
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| https://en.wikipedia.org/wiki?curid=14143232 |
14143247 | 3-carboxyethylcatechol 2,3-dioxygenase | Class of enzymes
In enzymology, a 3-carboxyethylcatechol 2,3-dioxygenase (EC 1.13.11.16) is an enzyme that catalyzes the chemical reaction
3-(2,3-dihydroxyphenyl)propanoate + O2 formula_0 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
Thus, the two substrates of this enzyme are 3-(2,3-dihydroxyphenyl)propanoate and O2, whereas its product is 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing). Other names in common use include 2,3-dihydroxy-beta-phenylpropionic dioxygenase, 2,3-dihydroxy-beta-phenylpropionate oxygenase, and 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, iron.
References.
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| https://en.wikipedia.org/wiki?curid=14143247 |
14143264 | 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase | Class of enzymes
In enzymology, a 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase (EC 1.13.11.48) is an enzyme that catalyzes the chemical reaction
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 formula_0 N-acetylanthranilate + CO
Thus, the two substrates of this enzyme are 3-hydroxy-2-methyl-1H-quinolin-4-one and O2, whereas its two products are N-acetylanthranilate and CO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming). This enzyme is also called (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase.
References.
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| https://en.wikipedia.org/wiki?curid=14143264 |
14143285 | 3-hydroxy-4-oxoquinoline 2,4-dioxygenase | Class of enzymes
In enzymology, a 3-hydroxy-4-oxoquinoline 2,4-dioxygenase (EC 1.13.11.47) is an enzyme that catalyzes the chemical reaction
3-hydroxy-1H-quinolin-4-one + O2 formula_0 N-formylanthranilate + CO
Thus, the two substrates of this enzyme are 3-hydroxy-1H-quinolin-4-one and O2, whereas its two products are N-formylanthranilate and CO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming). Other names in common use include (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase, 3-hydroxy-4(1H)-one, 2,4-dioxygenase, and quinoline-3,4-diol 2,4-dioxygenase.
References.
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| https://en.wikipedia.org/wiki?curid=14143285 |
14143295 | HAAO | Enzyme
3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme encoded by the HAAO gene that catalyzes the chemical reaction
3-hydroxyanthranilate + O2 formula_0 2-amino-3-carboxymuconate semialdehyde
Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O2, whereas its product is 2-amino-3-carboxymuconate semialdehyde.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2.
The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3-hydroxyanthranilic acid oxidase and 3HAO. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1YFU, 1YFW, 1YFX, 1YFY, 1ZVF, and 2QNK.h
References.
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| https://en.wikipedia.org/wiki?curid=14143295 |
14143313 | 3-hydroxyanthranilate oxidase | Class of enzymes
In enzymology, a 3-hydroxyanthranilate oxidase (EC 1.10.3.5) (also called 3-HAO) is an enzyme that catalyzes the chemical reaction:
3-hydroxyanthranilate + O2 formula_0 6-imino-5-oxocyclohexa-1,3-dienecarboxylate + H2O2
Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O2, whereas its two products are 6-imino-5-oxocyclohexa-1,3-dienecarboxylate and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen oxidoreductase. This enzyme is also called 3-hydroxyanthranilic acid oxidase.
References.
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| https://en.wikipedia.org/wiki?curid=14143313 |
14143320 | 4-hydroxymandelate synthase | Class of enzymes
In enzymology, a 4-hydroxymandelate synthase (EC 1.13.11.46) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylpyruvate + O2 formula_0 4-hydroxymandelate + CO2
Thus, the two substrates of this enzyme are 4-hydroxyphenylpyruvate and oxygen, whereas its two products are 4-hydroxymandelate and carbon dioxide.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme is also called 4-hydroxyphenylpyruvate dioxygenase II.
References.
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| https://en.wikipedia.org/wiki?curid=14143320 |
14143345 | 7,8-dihydroxykynurenate 8,8a-dioxygenase | Class of enzymes
In enzymology, a 7,8-dihydroxykynurenate 8,8a-dioxygenase (EC 1.13.11.10) is an enzyme that catalyzes the chemical reaction
7,8-dihydroxykynurenate + O2 formula_0 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
Thus, the two substrates of this enzyme are 7,8-dihydroxykynurenate and O2, whereas its product is 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing). Other names in common use include 7,8-dihydroxykynurenate oxygenase, and 7,8-dihydroxykynurenate 8,8alpha-dioxygenase. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.
References.
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| https://en.wikipedia.org/wiki?curid=14143345 |
14143362 | Acetylacetone-cleaving enzyme | Class of enzymes
In enzymology, an acetylacetone-cleaving enzyme (EC 1.13.11.50) is an enzyme that catalyzes the chemical reaction
pentane-2,4-dione + O2 formula_0 acetate + 2-oxopropanal
Thus, the two substrates of this enzyme are pentane-2,4-dione and O2, whereas its two products are acetate and 2-oxopropanal.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is acetylacetone:oxygen oxidoreductase. Other names in common use include Dke1, acetylacetone dioxygenase, diketone cleaving dioxygenase, and diketone cleaving enzyme.
References.
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| https://en.wikipedia.org/wiki?curid=14143362 |
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