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14040930 | Acyl-CoA dehydrogenase (NADP+) | Class of enzymes
In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ formula_0 2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ 2-oxidoreductase. Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+).
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YXM.
References.
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| https://en.wikipedia.org/wiki?curid=14040930 |
14040950 | Acyl-CoA oxidase | InterPro Family
In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction
acyl-CoA + O2 formula_0 trans-2,3-dehydroacyl-CoA + H2O2
Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2,3-dehydroacyl-CoA and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is acyl-CoA:oxygen 2-oxidoreductase. Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1IS2, 1W07, 2DDH, 2FON, 2IX5, and 2IX6.
References.
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| https://en.wikipedia.org/wiki?curid=14040950 |
14040962 | All-trans-retinol 13,14-reductase | Class of enzymes
In enzymology, an all-trans-retinol 13,14-reductase (EC 1.3.99.23) is an enzyme, encoded by the RETSAT gene, that catalyzes the chemical reaction
all-trans-13,14-dihydroretinol + acceptor formula_0 all-trans-retinol + reduced acceptor
Thus, the two substrates of this enzyme are all-trans-13,14-dihydroretinol and acceptor, whereas its two products are all-trans-retinol and reduced acceptor. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of all-trans-retinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. Other names in common use include retinol saturase, RetSat, (13,14)-all-trans-retinol saturase, and all-trans-retinol:all-trans-13,14-dihydroretinol saturase.
The gene has also been called PPAR-alpha-regulated and starvation-induced gene protein.
References.
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Further reading.
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14040976 | Alpha-santonin 1,2-reductase | Class of enzymes
In enzymology, an alpha-santonin 1,2-reductase (EC 1.3.1.47) is an enzyme that catalyzes the chemical reaction
1,2-dihydrosantonin + NAD(P)+ formula_0 alpha-santonin + NAD(P)H + H+
The 3 substrates of this enzyme are 1,2-dihydrosantonin, NAD+, and NADP+, whereas its 4 products are alpha-santonin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase.
References.
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| https://en.wikipedia.org/wiki?curid=14040976 |
14041004 | Anthocyanidin reductase | Class of enzymes
In enzymology, an anthocyanidin reductase (EC 1.3.1.77) is an enzyme that catalyzes the chemical reaction
a flavan-3-ol + 2 NAD(P)+ formula_0 an anthocyanidin + 2 NAD(P)H + H+
The 3 substrates of this enzyme are flavan-3-ol, NAD+, and NADP+, whereas its 4 products are anthocyanidin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is flavan-3-ol:NAD(P)+ oxidoreductase. Other names in common use include AtANR, and MtANR. This enzyme participates in flavonoid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14041004 |
14041020 | Arogenate dehydrogenase | Class of enzymes
In enzymology, an arogenate dehydrogenase (EC 1.3.1.43) is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD+ formula_0 L-tyrosine + NADH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2F1K.
References.
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| https://en.wikipedia.org/wiki?curid=14041020 |
14041038 | Arogenate dehydrogenase (NAD(P)+) | Class of enzymes
In enzymology, an arogenate dehydrogenase [NAD(P)+] (EC 1.3.1.79) is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD(P)+ formula_0 L-tyrosine + NAD(P)H + CO2
The 3 substrates of this enzyme are L-arogenate, NAD+, and NADP+, whereas its 4 products are L-tyrosine, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD(P)+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, and pretyrosine dehydrogenase (ambiguous).
References.
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| https://en.wikipedia.org/wiki?curid=14041038 |
14041065 | Arogenate dehydrogenase (NADP+) | Enzyme class
In enzymology, an arogenate dehydrogenase (NADP+) (EC 1.3.1.78) is an enzyme that catalyzes the chemical reaction
L-arogenate + NADP+ formula_0 L-tyrosine + NADPH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NADP+, whereas its 3 products are L-tyrosine, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), pretyrosine dehydrogenase (ambiguous), TyrAAT1, TyrAAT2, and TyrAa.
References.
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| https://en.wikipedia.org/wiki?curid=14041065 |
14041152 | Benzoyl-CoA reductase | In enzymology, a benzoyl-CoA reductase (EC 1.3.7.8) is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O formula_0 cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate
The 4 substrates of this enzyme are benzoyl-CoA, reduced acceptor, ATP, and H2O, whereas its 4 products are cyclohexa-1,5-diene-1-carbonyl-CoA, acceptor, ADP, and phosphate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP-forming). This enzyme is also called benzoyl-CoA reductase (dearomatizing). This enzyme participates in benzoate degradation via CoA ligation. It has two cofactors: manganese, and magnesium.
References.
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| https://en.wikipedia.org/wiki?curid=14041152 |
14041162 | Beta-nitroacrylate reductase | Class of enzymes
In enzymology, a beta-nitroacrylate reductase (EC 1.3.1.16) is an enzyme that catalyzes the chemical reaction
3-nitropropanoate + NADP+ formula_0 3-nitroacrylate + NADPH + H+
Thus, the two substrates of this enzyme are 3-nitropropanoate and NADP+, whereas its 3 products are 3-nitroacrylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-nitropropanoate:NADP+ oxidoreductase.
References.
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| https://en.wikipedia.org/wiki?curid=14041162 |
14041179 | Bilirubin oxidase | In enzymology, a bilirubin oxidase, BOD or BOx, (EC 1.3.3.5) is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction
2 bilirubin + O2 formula_0 2 biliverdin + 2 H2O
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism. It is widely studied as a catalyst for oxygen reduction.
Two structures of bilirubin oxidase from the ascomycete "Myrothecium verrucaria" have been deposited in the Protein Data Bank (accession codes 3abg and 2xll).
The active site consists of four copper centers, reminiscent of laccase. These centers are classified as type I (cys, met, his, his), type II (3his), and two type III (2his). The latter two centers are arranged in a trinuclear copper cluster forming the active site for oxygen reduction. The type I copper center is the primary electron acceptor and the site for the reduction of bilirubin.
References.
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Further reading.
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| https://en.wikipedia.org/wiki?curid=14041179 |
14041200 | Biochanin-A reductase | Class of enzymes
In enzymology, a biochanin-A reductase (EC 1.3.1.46) is an enzyme that catalyzes the chemical reaction
dihydrobiochanin A + NADP+ formula_0 biochanin A + NADPH + H+
Thus, the two substrates of this enzyme are dihydrobiochanin A and NADP+, whereas its 3 products are biochanin A, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrobiochanin-A:NADP+ Delta2-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14041200 |
14041239 | Cholestenone 5alpha-reductase | Class of enzymes
In enzymology, a cholestenone 5alpha-reductase (EC 1.3.1.22) is an enzyme that catalyzes the chemical reaction
5alpha-cholestan-3-one + NADP+ formula_0 cholest-4-en-3-one + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholestan-3-one and NADP+, whereas its 3 products are cholest-4-en-3-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxo-5alpha-steroid:NADP+ Delta4-oxidoreductase. Other names in common use include testosterone Delta4-5alpha-reductase, steroid 5alpha-reductase, 3-oxosteroid Delta4-dehydrogenase, 5alpha-reductase, steroid 5alpha-hydrogenase, 3-oxosteroid 5alpha-reductase, testosterone Delta4-hydrogenase, 4-ene-3-oxosteroid 5alpha-reductase, reduced nicotinamide adenine dinucleotide, phosphate:Delta4-3-ketosteroid 5alpha-oxidoreductase, 4-ene-5alpha-reductase, Delta4-3-ketosteroid 5alpha-oxidoreductase, cholest-4-en-3-one 5alpha-reductase, and testosterone 5alpha-reductase.
References.
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| https://en.wikipedia.org/wiki?curid=14041239 |
14041257 | Cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase | Class of enzymes
In enzymology, a cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase (EC 1.3.1.29) is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydronaphthalene-1,2-diol + NAD+ formula_0 naphthalene-1,2-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydronaphthalene-1,2-diol and NAD+, whereas its 3 products are naphthalene-1,2-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase. Other names in common use include (+)-cis-naphthalene dihydrodiol dehydrogenase, naphthalene dihydrodiol dehydrogenase, and cis-dihydrodiol naphthalene dehydrogenase. This enzyme participates in 1- and 2-methylnaphthalene degradation and naphthalene and anthracene degradation.
References.
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14041274 | Cis-1,2-dihydrobenzene-1,2-diol dehydrogenase | Class of enzymes
In enzymology, a cis-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.19) is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydrobenzene-1,2-diol + NAD+ formula_0 catechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydrobenzene-1,2-diol and NAD+, whereas its 3 products are catechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase. Other names in common use include cis-benzene glycol dehydrogenase, cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine, and dinucleotide) oxidoreductase. This enzyme participates in 4 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, naphthalene and anthracene degradation, and styrene degradation.
References.
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14041286 | Cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase | Class of enzymes
In enzymology, a cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase (EC 1.3.1.67) is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)+ formula_0 4-methylcatechol + NAD(P)H + CO2
The 3 substrates of this enzyme are cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate, NAD+, and NADP+, whereas its 4 products are 4-methylcatechol, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+ oxidoreductase (decarboxylating). This enzyme participates in toluene and xylene degradation.
References.
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14041295 | Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase | Class of enzymes
In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56) is an enzyme that catalyzes the chemical reaction
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ formula_0 biphenyl-2,3-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-3-phenylcyclohexa-3,5-diene-1,2-diol and NAD+, whereas its 3 products are biphenyl-2,3-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase. This enzyme is also called 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase. This enzyme participates in biphenyl degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14041295 |
14041312 | Cis-2-enoyl-CoA reductase (NADPH) | Class of enzymes
In enzymology, a cis-2-enoyl-CoA reductase (NADPH) (EC 1.3.1.37) is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ formula_0 cis-2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are cis-2,3-dehydroacyl-CoA, NADPH, and H+.
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ cis-2-oxidoreductase. Other names in common use include NADPH-dependent cis-enoyl-CoA reductase, reductase, cis-2-enoyl coenzyme A, cis-2-enoyl-coenzyme A reductase, and cis-2-enoyl-CoA reductase (NADPH).
References.
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Further reading.
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14041325 | Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase | Class of enzymes
In enzymology, a cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase (EC 1.3.1.49) is an enzyme that catalyzes the chemical reaction
(+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ formula_0 phenanthrene-3,4-diol + NADH + H+
Thus, the two substrates of this enzyme are (+)-cis-3,4-dihydrophenanthrene-3,4-diol and NAD+, whereas its 3 products are phenanthrene-3,4-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14041325 |
14041341 | Cis-dihydroethylcatechol dehydrogenase | Class of enzymes
In enzymology, a cis-dihydroethylcatechol dehydrogenase (EC 1.3.1.66) is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydro-3-ethylcatechol + NAD+ formula_0 3-ethylcatechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydro-3-ethylcatechol and NAD+, whereas its 3 products are 3-ethylcatechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase. This enzyme participates in ethylbenzene degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14041341 |
14041356 | Coproporphyrinogen dehydrogenase | In enzymology, a coproporphyrinogen dehydrogenase (EC 1.3.99.22) is an enzyme that catalyzes the chemical reaction
coproporphyrinogen III + 2 S-adenosyl-L-methionine formula_0 protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
Thus, the two substrates of this enzyme are coproporphyrinogen III and S-adenosyl-L-methionine, whereas its 4 products are protoporphyrinogen IX, CO2, L-methionine, and 5'-deoxyadenosine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating). Other names in common use include oxygen-independent coproporphyrinogen-III oxidase, HemF, HemN, radical SAM enzyme, and coproporphyrinogen III oxidase. This enzyme participates in porphyrin and chlorophyll metabolism. HemN is the Oxygen-independent oxidase produced in E. coli. HemF is the oxygen-dependent oxidase within E. coli. Importantly, only HemN utilizes S-adenosyl Methionine (SAM). Human variants of Coproporphyrinogen oxidase are cofactor-independent.
References.
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| https://en.wikipedia.org/wiki?curid=14041356 |
14041377 | Cortisone alpha-reductase | Class of enzymes
In enzymology, a cortisone alpha-reductase (EC 1.3.1.4) is an enzyme that catalyzes the chemical reaction
4,5alpha-dihydrocortisone + NADP+ formula_0 cortisone + NADPH + H+
Thus, the two substrates of this enzyme are 4,5alpha-dihydrocortisone and NADP+, whereas its 3 products are cortisone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,5alpha-dihydrocortisone:NADP+ Delta4-oxidoreductase. Other names in common use include cortisone Delta4-5alpha-reductase, microsomal steroid reductase (5alpha), Delta4-3-ketosteroid reductase (5alpha), Delta4-3-oxosteroid-5alpha-reductase, NADPH:Delta4-3-oxosteroid-5alpha-oxidoreductase, and Delta4-5alpha-reductase.
References.
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| https://en.wikipedia.org/wiki?curid=14041377 |
14041393 | Cucurbitacin Delta23-reductase | Class of enzymes
In enzymology, a cucurbitacin Delta23-reductase (EC 1.3.1.5) is an enzyme that catalyzes the chemical reaction
23,24-dihydrocucurbitacin + NAD(P)+ formula_0 cucurbitacin + NAD(P)H + H+
The 3 substrates of this enzyme are 23,24-dihydrocucurbitacin, NAD+, and NADP+, whereas its 4 products are cucurbitacin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 23,24-dihydrocucurbitacin:NAD(P)+ Delta23-oxidoreductase. This enzyme is also called NAD(P)H: cucurbitacin B Delta23-oxidoreductase. It employs one cofactor, manganese.
References.
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| https://en.wikipedia.org/wiki?curid=14041393 |
14041405 | Cyclohexanone dehydrogenase | In enzymology, a cyclohexanone dehydrogenase (EC 1.3.99.14) is an enzyme that catalyzes a redox chemical reaction of the form
cyclohexanone + acceptor formula_0 cyclohex-2-enone + reduced acceptor
Thus, the two substrates of this enzyme are cyclohexanone and acceptor, whereas its two products are cyclohex-2-enone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:(acceptor) 2-oxidoreductase.
References.
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| https://en.wikipedia.org/wiki?curid=14041405 |
14041419 | Delta14-sterol reductase | Class of enzymes
In enzymology, a Delta14-sterol reductase (EC 1.3.1.70) is an enzyme that catalyzes the chemical reaction
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ formula_0 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol and NADP+, whereas its 3 products are 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol:NADP+ Delta14-oxidoreductase. This enzyme participates in biosynthesis of steroids.
References.
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| https://en.wikipedia.org/wiki?curid=14041419 |
14041436 | Delta24(241)-sterol reductase | Class of enzymes
In enzymology, a Delta24(241)-sterol reductase (EC 1.3.1.71) is an enzyme that catalyzes the chemical reaction
ergosterol + NADP+ formula_0 ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are ergosterol and NADP+, whereas its 3 products are ergosta-5,7,22,24(241)-tetraen-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ergosterol:NADP+ Delta24(241)-oxidoreductase. Other names in common use include sterol Delta24(28)-methylene reductase, and sterol Delta24(28)-reductase. This enzyme participates in biosynthesis of steroids.
References.
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| https://en.wikipedia.org/wiki?curid=14041436 |
14041458 | Delta24-sterol reductase | Class of enzymes
In enzymology, a Delta24-sterol reductase (EC 1.3.1.72) is an enzyme that catalyzes the chemical reaction
5alpha-cholest-7-en-3beta-ol + NADP+ formula_0 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 5alpha-cholesta-7,24-dien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sterol:NADP+ Delta24-oxidoreductase. This enzyme is also called lanosterol Delta24-reductase. This enzyme participates in biosynthesis of steroids.
References.
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| https://en.wikipedia.org/wiki?curid=14041458 |
14041477 | Dibenzothiophene dihydrodiol dehydrogenase | Class of enzymes
In enzymology, a dibenzothiophene dihydrodiol dehydrogenase (EC 1.3.1.60) is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD+ formula_0 1,2-dihydroxydibenzothiophene + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene and NAD+, whereas its 3 products are 1,2-dihydroxydibenzothiophene, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD+ oxidoreductase.
References.
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| https://en.wikipedia.org/wiki?curid=14041477 |
14041512 | Dihydropyrimidine dehydrogenase (NADP+) | Class of enzymes
In enzymology, a dihydropyrimidine dehydrogenase (NADP+) (EC 1.3.1.2) is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NADP+ formula_0 uracil + NADPH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NADP+, whereas its 3 products are uracil, NADPH, and H+.
In humans the enzyme is encoded by the "DPYD" gene. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur. It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.
Terminology.
The systematic name of this enzyme class is 5,6-dihydrouracil:NADP+ 5-oxidoreductase. Other names in common use include:
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GT8, 1GTE, 1GTH, 1H7W, and 1H7X.
Function.
The protein is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. Genetic deficiency of this enzyme results in an error in pyrimidine metabolism associated with thymine-uraciluria and an increased risk of toxicity in cancer patients receiving 5-fluorouracil chemotherapy.
Interactive pathway map.
"Click on genes, proteins and metabolites below to link to respective articles."
Fluorouracil (5-FU) Activity edit
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References.
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Further reading.
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14041529 | Dihydrouracil dehydrogenase (NAD+) | Class of enzymes
In enzymology, a dihydrouracil dehydrogenase (NAD+) (EC 1.3.1.1) is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NAD+ formula_0 uracil + NADH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NAD+, whereas its 3 products are uracil, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:NAD+ oxidoreductase. Other names in common use include dehydrogenase, dihydrouracil, dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, pyrimidine reductase, thymine reductase, uracil reductase, and dihydrouracil dehydrogenase (NAD+). This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.
References.
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{
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14041543 | Dihydrouracil oxidase | In enzymology, a dihydrouracil oxidase (EC 1.3.3.7) is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + O2 formula_0 uracil + H2O2
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and O2, whereas its two products are uracil and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:oxygen oxidoreductase. It employs one cofactor, FMN.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14041543 |
14041560 | Divinyl chlorophyllide a 8-vinyl-reductase | Class of enzymes
In enzymology, divinyl chlorophyllide "a" 8-vinyl-reductase (EC 1.3.1.75) is an enzyme that catalyzes the chemical reaction
3,8-divinylprotochlorophyllide + NADPH + H+ formula_0 protochlorophyllide + NADP+
The three substrates of this enzyme are 3,8-divinylprotochlorophyllide, NADPH, and H+; its two products are protochlorophyllide and NADP+. This enzyme can also convert alternative substrates, for example 3,8-divinyl chlorophyllide "a" and in all cases reduces a single specific vinyl group to an ethyl group.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorophyllide-"a" :NADP+ oxidoreductase. Other names in common use include 3,8-divinyl protochlorophyllide "a" 8-vinyl-reductase, [4-vinyl]chlorophyllide "a" reductase, and 4VCR. This enzyme is part of the biosynthetic pathway to chlorophylls.
References.
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| https://en.wikipedia.org/wiki?curid=14041560 |
14041571 | Enoyl-(acyl-carrier-protein) reductase (NADPH, A-specific) | Enzyme class
In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) (EC 1.3.1.39) is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ formula_0 trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are acyl-[acyl-carrier-protein] and NADP+, whereas its 3 products are trans-2,3-dehydroacyl-[acyl-carrier-protein], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific). Other names in common use include acyl-ACP dehydrogenase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine, dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl-ACp reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific).
References.
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{
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| https://en.wikipedia.org/wiki?curid=14041571 |
14041588 | Enoyl-(acyl-carrier-protein) reductase (NADPH, B-specific) | Class of enzymes
In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ formula_0 trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are acyl-[acyl-carrier-protein] and NADP+, whereas its 3 products are trans-2,3-dehydroacyl-[acyl-carrier-protein], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific). Other names in common use include acyl-ACP dehydrogenase, reductase, enoyl-[acyl carrier protein] (reduced nicotinamide, adenine dinucleotide phosphate), NADPH 2-enoyl Co A reductase, enoyl acyl-carrier-protein reductase, enoyl-ACP reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). This enzyme participates in fatty acid biosynthesis.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ULU and 2YW9.
References.
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| https://en.wikipedia.org/wiki?curid=14041588 |
14041603 | Fumarate reductase (NADH) | Type of enzyme
In enzymology, a fumarate reductase (NADH) (EC 1.3.1.6) is an enzyme that catalyzes the chemical reaction
succinate + NAD+ formula_0 fumarate + NADH + H+
Thus, the two substrates of this enzyme are succinate and NAD+, whereas its three products are fumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate:NAD+ oxidoreductase. Other names in common use include NADH-fumarate reductase, NADH-dependent fumarate reductase, and fumarate reductase (NADH).
References.
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| https://en.wikipedia.org/wiki?curid=14041603 |
14041701 | Geissoschizine dehydrogenase | Class of enzymes
In enzymology, a geissoschizine dehydrogenase (EC 1.3.1.36) is an enzyme that catalyzes the chemical reaction
geissoschizine + NADP+ formula_0 4,21-didehydrogeissoschizine + NADPH
Thus, the two substrates of this enzyme are geissoschizine and NADP+, whereas its two products are 4,21-didehydrogeissoschizine and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geissoschizine:NADP+ 4,21-oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14041701 |
14041711 | Isoquinoline 1-oxidoreductase | In enzymology, an isoquinoline 1-oxidoreductase (EC 1.3.99.16) is an enzyme that catalyzes the chemical reaction
isoquinoline + acceptor + H2O formula_0 isoquinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are isoquinoline, acceptor, and H2O, whereas its two products are isoquinolin-1(2H)-one and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating).
References.
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| https://en.wikipedia.org/wiki?curid=14041711 |
14041729 | Isovaleryl-CoA dehydrogenase | In enzymology, an isovaleryl-CoA dehydrogenase (EC 1.3.8.4) is an enzyme that catalyzes the chemical reaction
3-methylbutanoyl-CoA + acceptor formula_0 3-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 3-methylbutanoyl-CoA and acceptor, whereas its two products are 3-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, FAD.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1IVH. It was created by a group containing K.A.Tiffany, D.L.Roberts, M.Wang, R.Paschke, A.-W.A.Mohsen, J.Vockley, and J.J.P.Kim. The structure was released on May 20, 1998.
References.
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14041748 | Kynurenate-7,8-dihydrodiol dehydrogenase | Class of enzymes
In enzymology, a kynurenate-7,8-dihydrodiol dehydrogenase (EC 1.3.1.18) is an enzyme that catalyzes the chemical reaction
7,8-dihydro-7,8-dihydroxykynurenate + NAD+ formula_0 7,8-dihydroxykynurenate + NADH + H+
Thus, the two substrates of this enzyme are 7,8-dihydro-7,8-dihydroxykynurenate and NAD+, whereas its 3 products are 7,8-dihydroxykynurenate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase. Other names in common use include 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase, and 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase. This enzyme participates in tryptophan metabolism.
References.
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14041765 | L-galactonolactone oxidase | In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reaction
L-galactono-1,4-lactone + O2 formula_0 L-ascorbate + H2O2
Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase. This enzyme participates in ascorbic acid and aldaric acid metabolism. It employs one cofactor, FAD.
References.
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14041804 | Maleylacetate reductase | Class of enzymes
In enzymology, a maleylacetate reductase (EC 1.3.1.32) is an enzyme that catalyzes the chemical reaction
3-oxoadipate + NAD(P)+ formula_0 2-maleylacetate + NAD(P)H + H+
The 3 substrates of this enzyme are 3-oxoadipate, NAD+, and NADP+, whereas its 4 products are 2-maleylacetate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxoadipate:NAD(P)+ oxidoreductase. This enzyme is also called maleolylacetate reductase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, benzoate degradation via hydroxylation, and 1,4-dichlorobenzene degradation.
References.
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14041818 | Meso-tartrate dehydrogenase | Class of enzymes
In enzymology, a meso-tartrate dehydrogenase (EC 1.3.1.7) is an enzyme that catalyzes the chemical reaction
meso-tartrate + NAD+ formula_0 dihydroxyfumarate + NADH + H+
Thus, the two substrates of this enzyme are meso-tartaric acid and NAD+, whereas its 3 products are dihydroxyfumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is meso-tartrate:NAD+ oxidoreductase. This enzyme participates in glyoxylic acid and dicarboxylic acid metabolism.
References.
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14041837 | Orotate reductase (NADH) | Class of enzymes
In enzymology, an orotate reductase (NADH) (EC 1.3.1.14) is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NAD+ formula_0 orotate + NADH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NAD+, whereas its 3 products are orotate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NAD+ oxidoreductase. This enzyme is also called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism. It has 2 cofactors: FAD, and FMN.
References.
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14041851 | Orotate reductase (NADPH) | Enzyme class
In enzymology, an orotate reductase (NADPH) (EC 1.3.1.15) is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NADP+ formula_0 orotate + NADPH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NADP+, whereas its 3 products are orotate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NADP+ oxidoreductase. Other names in common use include orotate reductase, dihydroorotate dehydrogenase, dihydro-orotic dehydrogenase, L-5,6-dihydro-orotate:NAD+ oxidoreductase, and orotate reductase (NADPH). It has one cofactor, FAD.
References.
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14041866 | Phloroglucinol reductase | Class of enzymes
In enzymology, a phloroglucinol reductase (EC 1.3.1.57) is an enzyme that catalyzes the chemical reaction
dihydrophloroglucinol + NADP+ formula_0 phloroglucinol + NADPH + H+
Thus, the two substrates of this enzyme are dihydrophloroglucinol and NADP+, whereas its 3 products are phloroglucinol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrophloroglucinol:NADP+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References.
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14041879 | Phosphatidylcholine desaturase | In enzymology, a phosphatidylcholine desaturase (EC 1.14.19.22, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD+ formula_0 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH + H+
Thus, the two substrates of this enzyme are 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine and NAD+, whereas its 3 products are 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine:NAD+ Delta12-oxidoreductase. Other names in common use include oleate desaturase, linoleate synthase, oleoyl-CoA desaturase, and oleoylphosphatidylcholine desaturase.
References.
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14041899 | Phthalate 4,5-cis-dihydrodiol dehydrogenase | Class of enzymes
In enzymology, a phthalate 4,5-cis-dihydrodiol dehydrogenase (EC 1.3.1.64) is an enzyme that catalyzes the chemical reaction
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ formula_0 4,5-dihydroxyphthalate + NADH + H+
Thus, the two substrates of this enzyme are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate and NAD+, whereas its 3 products are 4,5-dihydroxyphthalate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References.
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14041933 | Almost integer | Any number that is not an integer but is very close to one
In recreational mathematics, an almost integer (or near-integer) is any number that is not an integer but is very close to one. Almost integers may be considered interesting when they arise in some context in which they are unexpected.
Almost integers relating to the golden ratio and Fibonacci numbers.
Some examples of almost integers are high powers of the golden ratio formula_0, for example:
formula_1
The fact that these powers approach integers is non-coincidental, because the golden ratio is a Pisot–Vijayaraghavan number.
The ratios of Fibonacci or Lucas numbers can also make almost integers, for instance:
The above examples can be generalized by the following sequences, which generate near-integers approaching Lucas numbers with increasing precision:
As "n" increases, the number of consecutive nines or zeros beginning at the tenths place of "a"("n") approaches infinity.
Almost integers relating to "e" and π.
Other occurrences of non-coincidental near-integers involve the three largest Heegner numbers:
where the non-coincidence can be better appreciated when expressed in the common simple form:
formula_9
formula_10
formula_11
where
formula_12
and the reason for the squares is due to certain Eisenstein series. The constant formula_13
is sometimes referred to as Ramanujan's constant.
Almost integers that involve the mathematical constants π and e have often puzzled mathematicians. An example is: formula_14
The explanation for this seemingly remarkable coincidence was given by A. Doman in September 2023, and is a result of a sum related to Jacobi theta functions as follows:
formula_15
The first term dominates since the sum of the terms for formula_16 total formula_17 The sum can therefore be truncated to
formula_18
where solving for formula_19 gives formula_20
Rewriting the approximation for formula_19 and using the approximation for formula_21 gives
formula_22
Thus, rearranging terms gives formula_23 Ironically, the crude approximation for formula_24 yields an additional order of magnitude of precision.
Another example involving these constants is: formula_25
References.
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{
"math_id": 1,
"text": "\n\\begin{align}\n\\phi^{17} & =\\frac{3571+1597\\sqrt5}{2}\\approx 3571.00028 \\\\[6pt]\n\\phi^{18} & =2889+1292\\sqrt5 \\approx 5777.999827 \\\\[6pt]\n\\phi^{19} & =\\frac{9349+4181\\sqrt5}{2}\\approx 9349.000107\n\\end{align}\n"
},
{
"math_id": 2,
"text": " \\frac{\\operatorname{Fib}(360)}{\\operatorname{Fib}(216)} \\approx 1242282009792667284144565908481.999999999999999999999999999999195 "
},
{
"math_id": 3,
"text": " \\frac{\\operatorname{Lucas}(361)}{\\operatorname{Lucas}(216)} \\approx 2010054515457065378082322433761.000000000000000000000000000000497\n"
},
{
"math_id": 4,
"text": "a(n) = \\frac{\\operatorname{Fib}(45\\times2^n)}{\\operatorname{Fib}(27\\times2^n)} \\approx \\operatorname{Lucas}(18\\times2^n)"
},
{
"math_id": 5,
"text": "a(n) = \\frac{\\operatorname{Lucas}(45\\times2^n+1)}{\\operatorname{Lucas}(27\\times2^n)} \\approx \\operatorname{Lucas}(18\\times2^n+1)"
},
{
"math_id": 6,
"text": "e^{\\pi\\sqrt{43}}\\approx 884736743.999777466"
},
{
"math_id": 7,
"text": "e^{\\pi\\sqrt{67}}\\approx 147197952743.999998662454"
},
{
"math_id": 8,
"text": "e^{\\pi\\sqrt{163}}\\approx 262537412640768743.99999999999925007"
},
{
"math_id": 9,
"text": "e^{\\pi\\sqrt{43}}=12^3(9^2-1)^3+744-(2.225\\ldots)\\times 10^{-4}"
},
{
"math_id": 10,
"text": "e^{\\pi\\sqrt{67}}=12^3(21^2-1)^3+744-(1.337\\ldots)\\times 10^{-6}"
},
{
"math_id": 11,
"text": "e^{\\pi\\sqrt{163}}=12^3(231^2-1)^3+744-(7.499\\ldots)\\times 10^{-13}"
},
{
"math_id": 12,
"text": "21=3\\times7, \\quad 231=3\\times7\\times11, \\quad 744=24\\times 31"
},
{
"math_id": 13,
"text": "e^{\\pi\\sqrt{163}}"
},
{
"math_id": 14,
"text": "e^\\pi-\\pi=19.999099979189\\ldots"
},
{
"math_id": 15,
"text": "\\sum_{k=1}^{\\infty}\\left( 8\\pi k^2 -2 \\right) e^{-\\pi k^2} = 1."
},
{
"math_id": 16,
"text": "k\\geq 2"
},
{
"math_id": 17,
"text": "\\sim 0.0003436."
},
{
"math_id": 18,
"text": "\\left( 8\\pi -2\\right) e^{-\\pi}\\approx 1,"
},
{
"math_id": 19,
"text": "e^{\\pi}"
},
{
"math_id": 20,
"text": "e^{\\pi} \\approx 8\\pi -2."
},
{
"math_id": 21,
"text": "7\\pi \\approx 22"
},
{
"math_id": 22,
"text": " e^{\\pi} \\approx \\pi + 7\\pi - 2 \\approx \\pi + 22-2 = \\pi+20."
},
{
"math_id": 23,
"text": "e^{\\pi} - \\pi \\approx 20."
},
{
"math_id": 24,
"text": "7\\pi"
},
{
"math_id": 25,
"text": "e+\\pi+e\\pi+e^\\pi+\\pi^e=59.9994590558\\ldots"
}
]
| https://en.wikipedia.org/wiki?curid=14041933 |
14041977 | Pimeloyl-CoA dehydrogenase | Class of enzymes
In enzymology, a pimeloyl-CoA dehydrogenase (EC 1.3.1.62) is an enzyme that catalyzes the chemical reaction
pimeloyl-CoA + NAD+ formula_0 6-carboxyhex-2-enoyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are pimeloyl-CoA and NAD+, whereas its 3 products are 6-carboxyhex-2-enoyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References.
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| https://en.wikipedia.org/wiki?curid=14041977 |
14042000 | Precorrin-2 dehydrogenase | Class of enzymes
In enzymology, a precorrin-2 dehydrogenase (EC 1.3.1.76) is an enzyme that catalyzes the chemical reaction
precorrin-2 + NAD+ formula_0 sirohydrochlorin + NADH + H+
The two substrates of this enzyme are precorrin-2 and NAD+; its three products are sirohydrochlorin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is precorrin-2:NAD+ oxidoreductase. Other names in common use include Met8p, SirC, and CysG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria and to Cofactor F430.
References.
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| https://en.wikipedia.org/wiki?curid=14042000 |
14042017 | Precorrin-6A reductase | Class of enzymes
In enzymology, a precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction
precorrin-6A + NADPH + H+ formula_0 precorrin-6B + NADP+
The three substrates of this enzyme are precorrin 6A, NADPH and a proton; its two products are precorrin 6B and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH=CH group of an acceptor with NAD or NADPH as donor. The systematic name of this enzyme class is precorrin-6B:NADP+ oxidoreductase. Other names in common use include precorrin-6X reductase, precorrin-6Y:NADP+ oxidoreductase and CobK. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042017 |
14042037 | Prephenate dehydrogenase | Class of enzymes
Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine.
Nomenclature.
Gene: (Saccharomyces Cerevisiae) TYR1
Shikimate pathway: Arogenate/Prephenate (ADH/PDH). Although in the shikimate pathway arogenate and prephenate dehydrogenase catalyze different reactions, they can at times be used interchangeably.
Homology.
This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria (mostly cyanobacteria) and four different kinds of plants (mostly different kinds of beans).
Bacteria organisms (examples): Acenitobacter calcoaceticus, Fischerella sp., Flavobacterium so., Comamonas testosteroni, and nostoc sp.
Plant organisms: phaseolus coccineus, phaseolus vulgaris, vicia faba, vigna radiata
Function.
Present in the shikimate pathway, in the pathway to synthesize tyrosine (a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4-hydroxyphenylpyruvate.
Reaction.
In enzymology, a prephenate dehydrogenase (EC 1.3.1.12) is an enzyme that catalyzes the chemical reaction
prephenate + NAD+ formula_0 4-hydroxyphenylpyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are prephenate and NAD+, whereas its 3 products are 4-hydroxyphenylpyruvate, CO2, and NADH.
Structure.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include hydroxyphenylpyruvate synthase, and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
Also found in haemophilus influenzae, synechocystis (bacteria), and aquifex aeolicus (plant).
However, in haemophilus influenzae, prephenate dehydrogenase is fused with the enzyme chorismate mutase. This fusion is not found in plants or animals.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2G5C and 2PV7.
References.
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| https://en.wikipedia.org/wiki?curid=14042037 |
14042053 | Prephenate dehydrogenase (NADP+) | Class of enzymes
In enzymology, a prephenate dehydrogenase (NADP+) (EC 1.3.1.13) is an enzyme that catalyzes the chemical reaction
prephenate + NADP+ formula_0 4-hydroxyphenylpyruvate + CO2 + NADPH
Thus, the two substrates of this enzyme are prephenate and NADP+, whereas its 3 products are 4-hydroxyphenylpyruvate, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include prephenate dehydrogenase, prephenate (nicotinamide adenine dinucleotide phosphate), dehydrogenase, and prephenate dehydrogenase (NADP). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042053 |
14042070 | Progesterone 5alpha-reductase | Catalyzing enzyme
In enzymology, a progesterone 5alpha-reductase (EC 1.3.1.22) is an enzyme that catalyzes the chemical reaction
5alpha-pregnan-3,20-dione + NADP+ formula_0 progesterone + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-pregnan-3,20-dione and NADP+, whereas its 3 products are progesterone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. It is a C-steroid hormone that is a 5α-pregnane substituted with a oxo groups at positions 3 and 20. It is an intermediate in the conversion of progesterone to allopregnalone and isopregnanolone, other common forms of neurosteroids. The systematic name of this enzyme class is 5alpha-pregnan-3,20-dione:NADP+ 5-oxidoreductase. Other names in common use include steroid 5-alpha-reductase, and Delta4-steroid 5alpha-reductase (progesterone).
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042070 |
14042084 | Protochlorophyllide reductase | In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide "a". They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.
There are two structurally unrelated proteins with this sort of activity, referred to as light-dependent (LPOR) and dark-operative (DPOR). The light- and NADPH-dependent reductase is part of the short-chain dehydrogenase/reductase (SDR) superfamily and is found in plants and oxygenic photosynthetic bacteria, while the ATP-dependent dark-operative version is a completely different protein, consisting of three subunits that exhibit significant sequence and quaternary structure similarity to the three subunits of nitrogenase. This enzyme may be evolutionary older; due to its bound iron-sulfur clusters is highly sensitive to free oxygen and does not function if the atmospheric oxygen concentration exceeds about 3%. It is possible that evolutionary pressure associated with the great oxidation event resulted in the development of the light-dependent system.
The light-dependent version (EC 1.3.1.33) uses NADPH:
protochlorophyllide + NADPH + H+ formula_0 chlorophyllide "a" + NADP+
While the light-independent or dark-operative version (EC 1.3.7.7) uses ATP and ferredoxin:
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
Light-dependent.
The light-dependent version has the accepted name protochlorophyllide reductase. The systematic name is chlorophyllide-"a" :NADP+ 7,8-oxidoreductase. Other names in common use include NADPH2-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide reductase, protochlorophyllide oxidoreductase, and protochlorophyllide photooxidoreductase.
LPOR is one of only three known light-dependent enzymes. The enzyme enables light-dependent protochlorophyllide reduction via direct local hydride transfer from NADPH and a longer-range proton transfer along a defined structural pathway. LPOR is a ~40kDa monomeric enzyme, for which the structure has been solved by X-ray crystallography. It is part of the SDR superfamily, which includes alcohol dehydrogenase, and consists of a Rossman-fold NADPH-binding site and a substrate-specific C-terminal segment region. The protochlorophyllide substrate is thought to bind to a cavity near the nicotinamide end of the bound NADPH. LPOR is primarily found in plants and oxygenic photosynthetic bacteria, as well as in some algae.
Light-independent.
The light-independent version has the accepted name of ferredoxin:protochlorophyllide reductase (ATP-dependent). Systematically it is known as ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase. Other names in common use include light-independent protochlorophyllide reductase and dark-operative protochlorophyllide reductase (DPOR).
DPOR is a nitrogenase homologue and adopts an almost identical overall architecture arrangement to both nitrogenase as well as the downstream chlorophyllide a reductase (COR). The enzyme consists of a catalytic heterotetramer and two transiently-bound ATPase dimers (right). Similar to nitrogenase, the reduction mechanism relies on an electron transfer from the iron-sulfur cluster of the ATPase domain, through a secondary cluster on the catalytic heterotetramer and finally to the protochlorophyllide-bound active site (which, distinct from nitrogenase, does not contain FeMoco). The reduction requires significantly less input than the nitrogenase reaction, requiring only a 2-electron reduction and 4 ATP equivalents, and as such may require an auto-inhibitory mechanism to avoid over-activity.
DPOR can alternatively take as its substrate the compound with a second vinyl group (instead of an ethyl group) in the structure, in which case the reaction is
3,8-divinylprotochlorophyllide + reduced ferredoxin + 2 ATP + 2 H2O formula_0 3,8-divinylchlorophyllide "a" + oxidized ferredoxin + 2 ADP + 2 phosphate
This enzyme is present in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms.
References.
<templatestyles src="Reflist/styles.css" />
at the U.S. National Library of Medicine Medical Subject Headings (MeSH) | [
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| https://en.wikipedia.org/wiki?curid=14042084 |
14042100 | Pyrroloquinoline-quinone synthase | In enzymology, a pyrroloquinoline-quinone synthase (EC 1.3.3.11) is an enzyme that catalyzes the chemical reaction
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O2 formula_0 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline- 2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
The two substrates of this enzyme are 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate, and O2, whereas its 3 products are 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, H2O2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinol ine-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing). This enzyme is also called PqqC.
References.
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| https://en.wikipedia.org/wiki?curid=14042100 |
14042111 | Quinaldate 4-oxidoreductase | In enzymology, a quinaldate 4-oxidoreductase (EC 1.3.99.18) is an enzyme that catalyzes the chemical reaction
quinaldate + acceptor + H2O formula_0 kynurenate + reduced acceptor
The 3 substrates of this enzyme are quinaldate, acceptor, and H2O, whereas its two products are kynurenate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating). This enzyme is also called quinaldic acid 4-oxidoreductase.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
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| https://en.wikipedia.org/wiki?curid=14042111 |
14042122 | Quinoline 2-oxidoreductase | In enzymology, a quinoline 2-oxidoreductase (EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction
quinoline + acceptor + H2O formula_0 quinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are quinoline, acceptor, and H2O, whereas its two products are quinolin-1(2H)-one and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline:acceptor 2-oxidoreductase (hydroxylating).
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3Q.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042122 |
14042140 | Quinoline-4-carboxylate 2-oxidoreductase | In enzymology, a quinoline-4-carboxylate 2-oxidoreductase (EC 1.3.99.19) is an enzyme that catalyzes the chemical reaction
quinoline-4-carboxylate + acceptor + H2O formula_0 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor
The 3 substrates of this enzyme are quinoline-4-carboxylate, acceptor, and H2O, whereas its two products are 2-oxo-1,2-dihydroquinoline-4-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating). Other names in common use include quinaldic acid 4-oxidoreductase, and quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating).
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042140 |
14042157 | Secologanin synthase | In enzymology, a secologanin synthase (EC 1.14.19.62, was wrongly classified as EC 1.3.3.9 in the past) is an enzyme that catalyzes the chemical reaction
loganin + NADPH + H+ + O2 formula_0 secologanin + NADP+ + 2 H2O
The 4 substrates of this enzyme are loganin, NADPH, H+, and O2, whereas its 3 products are secologanin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is loganin:oxygen oxidoreductase (ring-cleaving). This enzyme participates in indole and ipecac alkaloid biosynthesis.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042157 |
14042172 | Terephthalate 1,2-cis-dihydrodiol dehydrogenase | In enzymology, a terephthalate 1,2-cis-dihydrodiol dehydrogenase (EC 1.3.1.61) is an enzyme that catalyzes the chemical reaction:
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD+ formula_0 3,4-dihydroxybenzoate + CO2 + NADH
Thus, the two substrates of this enzyme are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate and NAD+, whereas its 3 products are 3,4-dihydroxybenzoate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in 2,4-dichlorobenzoate degradation.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042172 |
14042195 | Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase | Class of enzymes
In enzymology, a trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.20) is an enzyme that catalyzes the chemical reaction
trans-1,2-dihydrobenzene-1,2-diol + NADP+ formula_0 catechol + NADPH + H+
Thus, the two substrates of this enzyme are trans-1,2-dihydrobenzene-1,2-diol and NADP+, whereas its three products are catechol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase. This enzyme is also called dihydrodiol dehydrogenase. This enzyme participates in metabolism of xenobiotics by cytochrome p450.
Structural studies.
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1RY0, 1RY8, 1S1P, 1S1R, 1S2A, 1S2C, 1XF0, 1ZQ5, 2F38, 2HDJ, 2IPJ, 2O48, 2O4U, and 2POQ.
References.
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| https://en.wikipedia.org/wiki?curid=14042195 |
14042214 | Trans-2-enoyl-CoA reductase (NAD+) | Class of enzymes
In enzymology, a trans-2-enoyl-CoA reductase (NAD+) (EC 1.3.1.44) is an enzyme that catalyzes the chemical reaction
trans-2,3-dehydroacyl-CoA + NADH + H+ formula_0 acyl-CoA + NAD+
Thus, the three substrates of this enzyme are trans-didehydroacyl-CoA, NADH, and H+, whereas its two products are acyl-CoA and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NAD+ trans-2-oxidoreductase. This enzyme is also called trans-2-enoyl-CoA reductase (NAD+). This enzyme participates in butanoate metabolism.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042214 |
14042229 | Trans-2-enoyl-CoA reductase (NADPH) | Class of enzymes
In enzymology, a trans-2-enoyl-CoA reductase (NADPH) (EC 1.3.1.38) is an enzyme that catalyzes the chemical reaction
trans-2,3-dehydroacyl-CoA + NADPH + H+ formula_0 acyl-CoA + NADP+
Thus, the three substrates of this enzyme are trans-2,3-dehydroacyl-CoA, NADPH, and H+, whereas its two products are acyl-CoA and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ trans-2-oxidoreductase. Other names in common use include NADPH-dependent trans-2-enoyl-CoA reductase, reductase, trans-enoyl coenzyme A, and trans-2-enoyl-CoA reductase (NADPH). This enzyme participates in fatty acid elongation in mitochondria and polyunsaturated fatty acid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14042229 |
14042243 | Tryptophan alpha,beta-oxidase | In enzymology, a tryptophan alpha,beta-oxidase (EC 1.3.3.10) is an enzyme that catalyzes the chemical reaction
L-tryptophan + O2 formula_0 alpha,beta-didehydrotryptophan + H2O2
Thus, the two substrates of this enzyme are L-tryptophan and O2, whereas its two products are alpha,beta-didehydrotryptophan and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-tryptophan:oxygen alpha,beta-oxidoreductase. Other names in common use include L-tryptophan 2',3'-oxidase, and L-tryptophan alpha,beta-dehydrogenase. It employs one cofactor, heme.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042243 |
14042262 | Xanthommatin reductase | Class of enzymes
In enzymology, a xanthommatin reductase (EC 1.3.1.41) is an enzyme that catalyzes the chemical reaction
5,12-dihydroxanthommatin + NAD+ formula_0 xanthommatin + NADH + H+
Thus, the two substrates of this enzyme are 5,12-dihydroxanthommatin and NAD+, whereas its three products are xanthommatin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,12-dihydroxanthommatin:NAD+ oxidoreductase.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14042262 |
14042283 | Zeatin reductase | Class of enzymes
In enzymology, a zeatin reductase (EC 1.3.1.69) is an enzyme that catalyzes the chemical reaction
dihydrozeatin + NADP+ formula_0 zeatin + NADPH + H+
Thus, the two substrates of this enzyme are dihydrozeatin and NADP+, whereas its 3 products are zeatin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrozeatin:NADP+ oxidoreductase.
References.
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14043383 | Chlorate reductase | In enzymology, a chlorate reductase (EC 1.97.1.1) is an enzyme that catalyzes the chemical reaction
AH2 + chlorate formula_0 A + H2O + chlorite
Thus, the two substrates of this enzyme are a reduced electron acceptor (denoted AH2) and chlorate, whereas its 3 products are an oxidized electron acceptor (denoted A), water, and chlorite. It is closely related to the enzyme perchlorate reductase which reduces both chlorate and perchlorate.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorite:acceptor oxidoreductase. This enzyme is also called chlorate reductase C.
References.
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14043399 | (Formate-C-acetyltransferase)-activating enzyme | Class of enzymes
In enzymology, a [formate-C-acetyltransferase]-activating enzyme (EC 1.97.1.4) is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine formula_0 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
The 3 substrates of this enzyme are S-adenosyl-L-methionine, dihydroflavodoxin, and formate C-acetyltransferase-glycine, whereas its 4 products are 5'-deoxyadenosine, L-methionine, flavodoxin semiquinone, and formate C-acetyltransferase-glycin-2-yl radical.
This radical SAM enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is [formate C-acetyltransferase]-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving). Other names in common use include PFL activase, PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), formate acetyltransferase activating enzyme, formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving).
References.
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14043415 | Pyrogallol hydroxytransferase | In enzymology, a pyrogallol hydroxytransferase (EC 1.97.1.2) is an enzyme that catalyzes the chemical reaction
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene formula_0 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene
Thus, the two substrates of this enzyme are 1,2,3,5-tetrahydroxybenzene and 1,2,3-trihydroxybenzene (pyrogallol), whereas its two products are 1,3,5-trihydroxybenzene (phloroglucinol) and 1,2,3,5-tetrahydroxybenzene.
This enzyme participates in benzoic acid degradation via CoA ligation.
Nomenclature.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene hydroxytransferase. Other names in common use include 1,2,3,5-tetrahydroxybenzene hydroxyltransferase, 1,2,3,5-tetrahydroxybenzene:pyrogallol transhydroxylase, 1,2,3,5-tetrahydroxybenzene-pyrogallol hydroxyltransferase (transhydroxylase), pyrogallol hydroxyltransferase, 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene hydroxyltransferase.
References.
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14043431 | Selenate reductase | In enzymology, a selenate reductase (EC 1.97.1.9) is an enzyme that catalyzes the chemical reaction
selenite + H2O + acceptor formula_0 selenate + reduced acceptor
The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.
References.
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14043455 | Tetrachloroethene reductive dehalogenase | In enzymology, a tetrachloroethene reductive dehalogenase (EC 1.97.1.8) is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family.
trichloroethene + chloride + acceptor formula_0 tetrachloroethene + reduced acceptor
The 3 substrates of this enzyme are trichloroethene, chloride, and acceptor, whereas its two products are tetrachloroethene and reduced acceptor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is acceptor:trichloroethene oxidoreductase (chlorinating). This enzyme is also called tetrachloroethene reductase. This enzyme participates in tetrachloroethene degradation.
Note that the physiologically relevant reaction actually occurs in the reverse direction from that shown above. In other words, in the bacterial species where this enzyme is found, tetrachloroethene is reductively dechlorinated to trichloroethene and chloride.
This enzyme is one member of a family of enzymes including trichloroethene dehalogenase and vinyl chloride dehalogenase. The other members of this family do not have their own EC numbers at present.
Reductive dehalogenases are key enzymes for anaerobic respiratory process, termed organohalide respiration.
References.
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Further reading.
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14043645 | Beta-cyclopiazonate dehydrogenase | Beta-cyclopiazonate dehydrogenase (EC 1.21.99.1) is an enzyme that catalyzes the chemical reaction
beta-cyclopiazonate + acceptor formula_0 alpha-cyclopiazonate + reduced acceptor
Thus, the two substrates of this enzyme are beta-cyclopiazonate and an acceptor, whereas its two products are alpha-cyclopiazonate and a reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with other acceptors. The systematic name of this enzyme class is beta-cyclopiazonate:acceptor oxidoreductase (cyclizing). Other names in common use include beta-cyclopiazonate oxidocyclase, beta-cyclopiazonic oxidocyclase, and beta-cyclopiazonate:(acceptor) oxidoreductase (cyclizing). It employs one cofactor, FAD.
References.
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14043657 | Betaine reductase | Enzyme
Betaine reductase (EC 1.21.4.4) is an enzyme that catalyzes the chemical reaction
acetyl phosphate + trimethylamine + thioredoxin disulfide formula_0 N,N,N-trimethylglycine + phosphate + thioredoxin
The 3 substrates of this enzyme are acetyl phosphate, trimethylamine, and thioredoxin disulfide, whereas its 3 products are N,N,N-trimethylglycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming).
References.
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14043668 | Columbamine oxidase | Class of enzymes
In enzymology, a columbamine oxidase (EC 1.21.3.2) is an enzyme that catalyzes the chemical reaction
2 columbamine + O2 formula_0 2 berberine + 2 H2O
Thus, the two substrates of this enzyme are columbamine and O2, whereas its two products are berberine and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is columbamine:oxygen oxidoreductase (cyclizing). This enzyme is also called berberine synthase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, iron.
References.
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14043689 | D-proline reductase (dithiol) | In enzymology, a D-proline reductase (dithiol) (EC 1.21.4.1) is an enzyme that catalyzes the chemical reaction
5-aminopentanoate + lipoate formula_0 D-proline + dihydrolipoate
Thus, the two substrates of this enzyme are 5-aminopentanoate and lipoate, whereas its two products are D-proline and dihydrolipoate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is 5-aminopentanoate:lipoate oxidoreductase (cyclizing). This enzyme participates in arginine and proline metabolism. It employs one cofactor, pyruvate.
References.
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14043705 | Glycine reductase | In enzymology, a glycine reductase (EC 1.21.4.2) is an enzyme that catalyzes the chemical reaction
acetyl phosphate + NH3 + thioredoxin disulfide + H2O formula_0 glycine + phosphate + thioredoxin
The 4 substrates of this enzyme are acetyl phosphate, NH3, thioredoxin disulfide, and H2O, whereas its 3 products are glycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming).
References.
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14043714 | Isopenicillin N synthase | Isopenicillin N synthase (IPNS) is a non-heme iron protein belonging to the 2-oxoglutarate (2OG)-dependent dioxygenases oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(-α-aminoadipoyl)--cysteinyl--valine (-ACV).
"N"-[(5"S")-5-amino-5-carboxypentanoyl]--cysteinyl--valine + O2 formula_0 isopenicillin N + 2 H2O
This reaction is a key step in the biosynthesis of penicillin and cephalosporin antibiotics.
The active sites of most isopenicillin N synthases contain an iron ion.
This enzyme is also called isopenicillin N synthetase.
Mechanism.
A Fe(II) metal ion in the active site of the enzyme is coordinated by at least two histidine residues, an aspartate residue, a glutamine residue, and two water molecules in the absence of a bound substrate. Just two histidine residues and one aspartic acid residue are entirely conserved. Therefore, it is highly significant that these two histidine residues, His214 and His270, and one aspartic acid residue, Asp216, are precisely the ones essential for activity. When ACV binds the active site, Gln330 and one water molecule are replaced by the ACV thiolate.
The linear tripeptide δ-(-α-aminoadipoyl)--cysteinyl--valine (-ACV) must first be assembled from its component amino acids by N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (ACV synthase). This allows for the binding of the substrate ACV to the deprotonated thiol group of the cysteine residue. This ligation of the thiolate to the iron center anchors the ACV within the active site.
The ligation of ACV results in a decrease in the FeII/FeIII redox potential, which facilitates the reduction of dioxygen to superoxide. Formation of a highly covalent RS-FeIII bond lowers the activation barrier to dioxygen binding, thereby initiating the reaction cycle. An intramolecular hydrogen atom transfer from C-3 of the cysteine residue (BDE= 93 kcal/mol) to the distal superoxo oxygen takes place, thereby converting the FeIII back to the FeII oxidation state. A thioaldehyde and a hydroperoxy ligand (OOH) are produced in this process. The hydroperoxy ligand deprotonates the amide which then closes the β-lactam ring by a nucleophilic attack at the thioaldehyde carbon.
This causes the hydrogen atom at the C-3 of the valine residue to come closer to the iron(IV) oxo ligand which is highly electrophilic. A second hydrogen transfer occurs, most likely producing an isopropyl radical which closes the thiazolidine ring by attacking the thiolate sulfur atom.
Role in Antibiotic Formation.
Following the IPNS pathway, further enzymes are responsible for the epimerization of isopenicillin N to penicillin N, the derivitazation to other penicillins, and the ring expansion that eventually leads to the various cephalosporins.
This shows how IPNS occupies an early and key role in the biosynthetic pathway of all of the penicillins and cephalosporins, which are different types of β-lactam antibiotics. This class of antibiotics is the most widely used. They act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls, which is especially important in Gram-positive organisms.
There are several types of penicillins that can be used to treat different kinds of bacterial infections. They will not work for infections caused by viruses, such as colds or the flu.
Structural studies.
As of late 2007, 26 structures have been solved for this class of enzymes, with PDB accession codes 1ODM, 1UZW, 1W03, 1W04, 1W05, 1W06, 1W3V, 1W3X, 2BJS, 2BU9, 2IVI, 2IVJ, 2JB4, 1QJE, 1ODN, 1HB1, 1HB2, 1HB3, 1HB4, 1QIQ, 1QJF, 1BK0, 1BLZ, 1OBN, 1OC1, 1IPS
References.
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Further reading.
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14043728 | Reticuline oxidase | In enzymology, a reticuline oxidase (EC 1.21.3.3) is an enzyme that catalyzes the chemical reaction
(S)-reticuline + O2 formula_0 (S)-scoulerine + H2O2
Thus, the two substrates of this enzyme are (S)-reticuline and O2, whereas its two products are (S)-scoulerine and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming). Other names in common use include BBE, berberine bridge enzyme, berberine-bridge-forming enzyme, and tetrahydroprotoberberine synthase. This enzyme participates in alkaloid biosynthesis i.
References.
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14043741 | Sarcosine reductase | In enzymology, a sarcosine reductase (EC 1.21.4.3) is an enzyme that catalyzes the chemical reaction
acetyl phosphate + methylamine + thioredoxin disulfide formula_0 N-methylglycine + phosphate + thioredoxin
The 3 substrates of this enzyme are acetyl phosphate, methylamine, and thioredoxin disulfide, whereas its 3 products are N-methylglycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxydoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate methilamine:thioredoxin disulfide oxydoreductase (M-methylglycine-forming).
References.
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Further reading.
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14043759 | Sulochrin oxidase ((−)-bisdechlorogeodin-forming) | In enzymology, a sulochrin oxidase [(−)-bisdechlorogeodin-forming] (EC 1.21.3.5) is an enzyme that catalyzes the chemical reaction
2 sulochrin + O2 formula_0 2 (−)-bisdechlorogeodin + 2 H2O
Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (−)-bisdechlorogeodin and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (−)-specific). This enzyme is also called sulochrin oxidase.
References.
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14043780 | Sulochrin oxidase ((+)-bisdechlorogeodin-forming) | In enzymology, a sulochrin oxidase [(+)-bisdechlorogeodin-forming] (EC 1.21.3.4) is an enzyme that catalyzes the chemical reaction
2 sulochrin + O2 formula_0 2 (+)-bisdechlorogeodin + 2 H2O
Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (+)-bisdechlorogeodin and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (+)-specific). This enzyme is also called sulochrin oxidase.
References.
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14044158 | 2,4-dichlorophenol 6-monooxygenase | Class of enzymes
In enzymology, a 2,4-dichlorophenol 6-monooxygenase (EC 1.14.13.20) is an enzyme that catalyzes the chemical reaction
2,4-dichlorophenol + NADPH + H+ + O2 formula_0 3,5-dichlorocatechol + NADP+ + H2O
The 4 substrates of this enzyme are 2,4-dichlorophenol, NADPH, H+, and O2, whereas its 3 products are 3,5-dichlorocatechol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2,4-dichlorophenol,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include 2,4-dichlorophenol hydroxylase, and 2,4-dichlorophenol monooxygenase. This enzyme participates in 1,4-dichlorobenzene degradation. It employs one cofactor, FAD.
References.
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14044177 | 24-hydroxycholesterol 7alpha-hydroxylase | Class of enzymes
In enzymology, a 24-hydroxycholesterol 7alpha-hydroxylase (EC 1.14.13.99) is an enzyme that catalyzes the chemical reaction
(24R)-cholest-5-ene-3beta,24-diol + NADPH + H+ + O2 formula_0 (24R)-cholest-5-ene-3beta,7alpha,24-triol + NADP+ + H2O
The 4 substrates of this enzyme are (24R)-cholest-5-ene-3beta,24-diol, NADPH, H+, and O2, whereas its 3 products are (24R)-cholest-5-ene-3beta,7alpha,24-triol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (24R)-cholest-5-ene-3beta,24-diol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). Other names in common use include 24-hydroxycholesterol 7alpha-monooxygenase, CYP39A1, and CYP39A1 oxysterol 7alpha-hydroxylase.
References.
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14044193 | 2,6-dihydroxypyridine 3-monooxygenase | Class of enzymes
In enzymology, a 2,6-dihydroxypyridine 3-monooxygenase (EC 1.14.13.10) is an enzyme that catalyzes the chemical reaction
2,6-dihydroxypyridine + NADH + H+ + O2 formula_0 2,3,6-trihydroxypyridine + NAD+ + H2O
The 4 substrates of this enzyme are 2,6-dihydroxypyridine, NADH, H+, and O2, whereas its 3 products are 2,3,6-trihydroxypyridine, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called 2,6-dihydroxypyridine oxidase. It has 2 cofactors: FAD, and Flavoprotein.
References.
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14044209 | 27-hydroxycholesterol 7alpha-monooxygenase | Class of enzymes
In enzymology, a 27-hydroxycholesterol 7alpha-monooxygenase (EC 1.14.13.60) is an enzyme that catalyzes the chemical reaction
27-hydroxycholesterol + NADPH + H+ + O2 formula_0 7alpha,27-dihydroxycholesterol + NADP+ + H2O
The 4 substrates of this enzyme are 27-hydroxycholesterol, NADPH, H+, and O2, whereas its 3 products are 7alpha,27-dihydroxycholesterol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 27-hydroxycholesterol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). This enzyme is also called 27-hydroxycholesterol 7alpha-hydroxylase. It employs one cofactor, heme-thiolate(P-450).
References.
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14044229 | 2-aminobenzenesulfonate 2,3-dioxygenase | Class of enzymes
In enzymology, a 2-aminobenzenesulfonate 2,3-dioxygenase (EC 1.14.12.14) is an enzyme that catalyzes the chemical reaction
2-aminobenzenesulfonate + NADH + H+ + O2 formula_0 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
The 4 substrates of this enzyme are 2-aminobenzenesulfonate, NADH, H+, and O2, whereas its 3 products are 2,3-dihydroxybenzenesulfonate, NH3, and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming). This enzyme is also called 2-aminosulfobenzene 2,3-dioxygenase. This enzyme participates in benzoate degradation via hydroxylation.
References.
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14044245 | 2-chlorobenzoate 1,2-dioxygenase | Class of enzymes
In enzymology, a 2-chlorobenzoate 1,2-dioxygenase (EC 1.14.12.13) is an enzyme that catalyzes the chemical reaction
2-chlorobenzoate + NADH + H+ + O2 formula_0 catechol + chloride + NAD+ + CO2
The 4 substrates of this enzyme are 2-chlorobenzoate, NADH, H+, and O2, whereas its 4 products are catechol, chloride, NAD+, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 2-chlorobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, dechlorinating, decarboxylating). This enzyme is also called 2-halobenzoate 1,2-dioxygenase. This enzyme participates in benzoate degradation via coa ligation. It employs one cofactor, iron.
References.
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14044264 | 2'-deoxymugineic-acid 2'-dioxygenase | Class of enzymes
In enzymology, a 2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) is an enzyme that catalyzes the chemical reaction
2'-deoxymugineic acid + 2-oxoglutarate + O2 formula_0 mugineic acid + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxymugineic acid, 2-oxoglutarate, and O2, whereas its 3 products are mugineic acid, (a compound related to azetidine-2-carboxylic acid) succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is 2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating). This enzyme is also called IDS3.
References.
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14044279 | 2-hydroxybiphenyl 3-monooxygenase | Class of enzymes
In enzymology, a 2-hydroxybiphenyl 3-monooxygenase (EC 1.14.13.44) is an enzyme that catalyzes the chemical reaction
2-hydroxybiphenyl + NADH + H+ + O2 formula_0 2,3-dihydroxybiphenyl + NAD+ + H2O
The 4 substrates of this enzyme are 2-hydroxybiphenyl, NADH, H+, and O2, whereas its 3 products are 2,3-dihydroxybiphenyl, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-hydroxybiphenyl,NADH:oxygen oxidoreductase (3-hydroxylating).
References.
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| https://en.wikipedia.org/wiki?curid=14044279 |
14044301 | 2-hydroxycyclohexanone 2-monooxygenase | Class of enzymes
In enzymology, a 2-hydroxycyclohexanone 2-monooxygenase (EC 1.14.13.66) is an enzyme that catalyzes the chemical reaction
2-hydroxycyclohexan-1-one + NADPH + H+ + O2 formula_0 6-hydroxyhexan-6-olide + NADP+ + H2O
The 4 substrates of this enzyme are 2-hydroxycyclohexan-1-one, NADPH, H+, and O2, whereas its 3 products are 6-hydroxyhexan-6-olide, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-hydroxycyclohexan-1-one,NADPH:oxygen 2-oxidoreductase (1,2-lactonizing).
References.
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| https://en.wikipedia.org/wiki?curid=14044301 |
14044329 | 2-hydroxypyridine 5-monooxygenase | Class of enzymes
In enzymology, a 2-hydroxypyridine 5-monooxygenase (EC 1.14.99.26) is an enzyme that catalyzes the chemical reaction
2-hydroxypyridine + AH2 + O2 formula_0 2,5-dihydroxypyridine + A + H2O
The 3 substrates of this enzyme are 2-hydroxypyridine, an electron acceptor AH2, and O2, whereas its 3 products are 2,5-dihydroxypyridine, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 2-hydroxypyridine,hydrogen-donor:oxygen oxidoreductase (5-hydroxylating). This enzyme is also called 2-hydroxypyridine oxygenase.
References.
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| https://en.wikipedia.org/wiki?curid=14044329 |
14044347 | 2-hydroxyquinoline 5,6-dioxygenase | Class of enzymes
In enzymology, a 2-hydroxyquinoline 5,6-dioxygenase (EC 1.14.12.16) is an enzyme that catalyzes the chemical reaction
quinolin-2-ol + NADH + H+ + O2 formula_0 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+
The 4 substrates of this enzyme are quinolin-2-ol, NADH, H+, and O2, whereas its two products are 2,5,6-trihydroxy-5,6-dihydroquinoline and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating). Other names in common use include 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase, quinolin-2-ol 5,6-dioxygenase, and quinolin-2(1H)-one 5,6-dioxygenase.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14044347 |
14044360 | 2-hydroxyquinoline 8-monooxygenase | Class of enzymes
In enzymology, a 2-hydroxyquinoline 8-monooxygenase (EC 1.14.13.61) is an enzyme that catalyzes the chemical reaction
quinolin-2-ol + NADH + H+ + O2 formula_0 quinolin-2,8-diol + NAD+ + H2O
The 4 substrates of this enzyme are quinolin-2-ol, NADH, H+, and O2, whereas its 3 products are quinolin-2,8-diol, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating). This enzyme is also called 2-oxo-1,2-dihydroquinoline 8-monooxygenase. It employs one cofactor, iron.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1Z01, 1Z02, and 1Z03.
References.
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| https://en.wikipedia.org/wiki?curid=14044360 |
14044367 | 2-nitrophenol 2-monooxygenase | Class of enzymes
In enzymology, a 2-nitrophenol 2-monooxygenase (EC 1.14.13.31) is an enzyme that catalyzes the chemical reaction
2-nitrophenol + NADPH + H+ + O2 formula_0 catechol + nitrite + NADP+ + H2O
The 4 substrates of this enzyme are 2-nitrophenol, NADPH, H+, and O2, whereas its 4 products are catechol, nitrite, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-nitrophenol,NADPH:oxygen 2-oxidoreductase (2-hydroxylating, nitrite-forming). Other names in common use include 2-nitrophenol oxygenase, and nitrophenol oxygenase.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14044367 |
14044388 | 3,9-dihydroxypterocarpan 6a-monooxygenase | Class of enzymes
In enzymology, a 3,9-dihydroxypterocarpan 6a-monooxygenase (EC 1.14.13.28) is an enzyme that catalyzes the chemical reaction
(6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + H+ + O2 formula_0 (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP+ + H2O
The 4 substrates of this enzyme are (6aR,11aR)-3,9-dihydroxypterocarpan, NADPH, H+, and O2, whereas its 3 products are (6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (6aR,11aR)-3,9-dihydroxypterocarpan,NADPH:oxygen oxidoreductase (6a-hydroxylating). Other names in common use include 3,9-dihydroxypterocarpan 6a-hydroxylase, and 3,9-dihydroxypterocarpan 6alpha-monooxygenase (erroneous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14044388 |
14044405 | 3-hydroxy-2-methylpyridinecarboxylate dioxygenase | Class of enzymes
In enzymology, a 3-hydroxy-2-methylpyridinecarboxylate dioxygenase (EC 1.14.12.4) is an enzyme that catalyzes the chemical reaction
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 formula_0 2-(acetamidomethylene)succinate + NAD(P)+
The 5 substrates of this enzyme are 3-hydroxy-2-methylpyridine-5-carboxylate, NADH, NADPH, H+, and O2, whereas its 3 products are 2-(acetamidomethylene)succinate, NAD+, and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing). Other names in common use include methylhydroxypyridinecarboxylate oxidase, 2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase, methylhydroxypyridine carboxylate dioxygenase, and 3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14044405 |
14044420 | 3-hydroxybenzoate 2-monooxygenase | Class of enzymes
In enzymology, a 3-hydroxybenzoate 2-monooxygenase (EC 1.14.99.23) is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + AH2 + O2 formula_0 2,3-dihydroxybenzoate + A + H2O
The 3 substrates of this enzyme are 3-hydroxybenzoate, an electron acceptor AH2, and O2, whereas its 3 products are 2,3-dihydroxybenzoate, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 3-hydroxybenzoate,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 3-hydroxybenzoate 2-hydroxylase, and 3-HBA-2-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation.
References.
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{
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| https://en.wikipedia.org/wiki?curid=14044420 |
14044434 | 3-hydroxybenzoate 4-monooxygenase | Class of enzymes
In enzymology, a 3-hydroxybenzoate 4-monooxygenase (EC 1.14.13.23) is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + NADPH + H+ + O2 formula_0 3,4-dihydroxybenzoate + NADP+ + H2O
The 4 substrates of this enzyme are 3-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are 3,4-dihydroxybenzoate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). This enzyme is also called 3-hydroxybenzoate 4-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2DKH and 2DKI.
References.
<templatestyles src="Reflist/styles.css" /> | [
{
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| https://en.wikipedia.org/wiki?curid=14044434 |
14044456 | 3-hydroxybenzoate 6-monooxygenase | Class of enzymes
In enzymology, a 3-hydroxybenzoate 6-monooxygenase (EC 1.14.13.24) is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + NADH + H+ + O2 formula_0 2,5-dihydroxybenzoate + NAD+ + H2O
The 4 substrates of this enzyme are 3-hydroxybenzoate, NADH, H+, and O2, whereas its 3 products are 2,5-dihydroxybenzoate, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include 3-hydroxybenzoate 6-hydroxylase, m-hydroxybenzoate 6-hydroxylase, and 3-hydroxybenzoic acid-6-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation. 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=14044456 |
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