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14044469 | 3-hydroxyphenylacetate 6-hydroxylase | Class of enzymes
In enzymology, a 3-hydroxyphenylacetate 6-hydroxylase (EC 1.14.13.63) is an enzyme that catalyzes the chemical reaction
3-hydroxyphenylacetate + NAD(P)H + H+ + O2 formula_0 2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 3-hydroxyphenylacetate, NADH, NADPH, H+, and O2, whereas its 4 products are 2,5-dihydroxyphenylacetate, NAD+, 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-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called 3-hydroxyphenylacetate 6-monooxygenase. This enzyme participates in styrene degradation. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044469 |
14044488 | 3-phenylpropanoate dioxygenase | Class of enzymes
In enzymology, a 3-phenylpropanoate dioxygenase (EC 1.14.12.19) is an enzyme that catalyzes the chemical reaction
3-phenylpropanoate + NADH + H+ + O2 formula_0 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+
The 4 substrates of this enzyme are 3-phenylpropanoate, NADH, H+, and O2, whereas its two products are 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate 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 3-phenylpropanoate,NADH:oxygen oxidoreductase (2,3-hydroxylating). Other names in common use include HcaA1A2CD, Hca dioxygenase, and 3-phenylpropionate dioxygenase.
References.
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| https://en.wikipedia.org/wiki?curid=14044488 |
14044502 | 4-aminobenzoate 1-monooxygenase | Class of enzymes
In enzymology, a 4-aminobenzoate 1-monooxygenase (EC 1.14.13.27) is an enzyme that catalyzes the chemical reaction
4-aminobenzoate + NAD(P)H + 2 H+ + O2 formula_0 4-hydroxyaniline + NAD(P)+ + H2O + CO2
The 5 substrates of this enzyme are 4-aminobenzoate, NADH, NADPH, H+, and O2, whereas its 5 products are 4-hydroxyaniline, NAD+, NADP+, H2O, 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 one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-aminobenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating). Other names in common use include 4-aminobenzoate hydroxylase, and 4-aminobenzoate monooxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044502 |
14044524 | 4-chlorophenylacetate 3,4-dioxygenase | Class of enzymes
In enzymology, a 4-chlorophenylacetate 3,4-dioxygenase (EC 1.14.12.9) is an enzyme that catalyzes the chemical reaction
4-chlorophenylacetate + NADH + H+ + O2 formula_0 3,4-dihydroxyphenylacetate + chloride + NAD+
The 4 substrates of this enzyme are 4-chlorophenylacetate, NADH, H+, and O2, whereas its 3 products are 3,4-dihydroxyphenylacetate, chloride, 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 4-chlorophenylacetate,NADH:oxygen oxidoreductase (3,4-hydroxylating, dechlorinating). It employs one cofactor, iron.
References.
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14044541 | 4-hydroxyacetophenone monooxygenase | Class of enzymes
In enzymology, a 4-hydroxyacetophenone monooxygenase (EC 1.14.13.84) is an enzyme that catalyzes the chemical reaction:
(4-hydroxyphenyl)ethan-1-one + NADPH + H+ + O2 formula_0 O-acetylhydroquinone + NADP+ + H2O
The 4 substrates of this enzyme are (4-hydroxyphenyl)ethan-1-one, NADPH, H+, and O2, whereas its 3 products are hydroquinone acetate ester, 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 (4-hydroxyphenyl)ethan-1-one,NADPH:oxygen oxidoreductase (ester-forming). This enzyme is also called HAPMO. This enzyme participates in bisphenol a degradation.
References.
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| https://en.wikipedia.org/wiki?curid=14044541 |
14044556 | 4-hydroxybenzoate 1-hydroxylase | Class of enzymes
In enzymology, a 4-hydroxybenzoate 1-hydroxylase (EC 1.14.13.64) is an enzyme that catalyzes the chemical reaction
4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 formula_0 hydroquinone + NAD(P)+ + H2O + CO2
The 5 substrates of this enzyme are 4-hydroxybenzoate, NADH, NADPH, H+, and O2, whereas its 5 products are hydroquinone, NAD+, NADP+, H2O, 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 one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating). This enzyme is also called 4-hydroxybenzoate 1-monooxygenase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044556 |
14044584 | 4-hydroxybenzoate 3-monooxygenase (NAD(P)H) | Class of enzymes
In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction
4-hydroxybenzoate + NAD(P)H + H+ + O2 formula_0 3,4-dihydroxybenzoate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 4-hydroxybenzoate, NADH, NADPH, H+, and O2, whereas its 4 products are 3,4-dihydroxybenzoate, NAD+, 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 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine, dinucleotide (phosphate)), 4-hydroxybenzoate-3-hydroxylase, and 4-hydroxybenzoate 3-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044584 |
14044598 | 4-hydroxyphenylacetaldehyde oxime monooxygenase | Class of enzymes
In enzymology, a 4-hydroxyphenylacetaldehyde oxime monooxygenase (EC 1.14.13.68) is an enzyme that catalyzes the chemical reaction
(Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H+ + O2 formula_0 (S)-4-hydroxymandelonitrile + NADP+ + 2 H2O
The 4 substrates of this enzyme are (Z)-4-hydroxyphenylacetaldehyde oxime, NADPH, H+, and O2, whereas its 3 products are (S)-4-hydroxymandelonitrile, 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 (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. Other names in common use include 4-hydroxybenzeneacetaldehyde oxime monooxygenase, cytochrome P450II-dependent monooxygenase, NADPH-cytochrome P450 reductase (CYP71E1), CYP71E1, and 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. This enzyme participates in tyrosine metabolism.
References.
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14044612 | 4-hydroxyphenylacetate 1-monooxygenase | Class of enzymes
In enzymology, a 4-hydroxyphenylacetate 1-monooxygenase (EC 1.14.13.18) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate + NAD(P)H + H+ + O2 formula_0 homogentisate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 4-hydroxyphenylacetate, NADH, NADPH, H+, and O2, whereas its 4 products are homogentisate, NAD+, 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 4-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating). Other names in common use include 4-hydroxyphenylacetate 1-hydroxylase, 4-hydroxyphenylacetic 1-hydroxylase, and 4-HPA 1-hydroxylase. This enzyme participates in tyrosine metabolism.. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044612 |
14044631 | 4-Hydroxyphenylacetate 3-monooxygenase | Class of enzymes
4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.14.9) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate + FADH2 + O2 formula_0 3,4-dihydroxyphenylacetate + FAD + H2O
This reaction is the first step in a pathway found in enteric bacteria such as Escherichia coli and soil bacteria such as Pseudomonas putida which degrades 4-hydroxyphenylacetate (4-HPA), allowing these bacteria to use 4-HPA and other aromatic compounds found in mammalian digestive tracts or in soil as a carbon source. While most known flavin monooxygenases use NADH or NADPH as substrates (and use the flavins FAD or FMN as prosthetic groups ), this enzyme is part of a two-component system, in which a flavin oxidoreductase partner (EC 1.5.1.37) regenerates FADH2 by oxidizing NADH to NAD+. hpaB and hpaC, the 4-HPA oxygenase and reductase partner proteins (respectively) of "E. coli" strain W, were the first two-component flavin monoxygenase system identified. While known examples of this enzyme share a common catalytic mechanism and likely evolutionary origin, they differ with respect to regulation and ability to substitute FMNH2 for FADH2 as a substrate.
Structure.
This enzyme is a tetramer which forms as a dimer of dimers. Sequence alignments of the Thermus thermophilus and "E. coli" hpaB enzymes show structural similarity to each other and to the oxygenase components of other bacterial two-component monooxygenases for compounds such as phenol and chlorophenol. Each monomer of this protein consists of an N-terminal alpha-helical domain, a middle beta barrel domain, and a C-terminal "tail" helix. FADH2 is bound by a groove between these domains; this binding event causes a loop in the middle domain to change position, preforming a binding site for 4-HPA. At this point, multiple residues act to stabilize catalytic intermediates by hydrogen-bonding to the peroxide bound to FAD, as well as to the hydroxyl group of 4-HPA's phenol moiety (stabilizing its dienone transition state - see Mechanism). The loop which moves to form the 4-HPA binding site when FADH2 binds provides catalytic specificity by hydrogen-bonding to 4-HPA's carboxylic acid moiety.
Mechanism.
While many flavin-dependent monooxygenases retain FMN or FAD in their active sites throughout their catalytic cycle, this enzyme binds FADH2 at the start of its catalytic cycle and releases FAD at the end. After FADH2 binds, dioxygen attacks it at the C4a carbon, leading to a C4a-hydroperoxyflavin intermediate. 4-HPA then binds, and a conformational change sequesters the enzyme's active site from solution, preventing the oxygen from escaping as toxic hydrogen peroxide. 4-HPA is then hydroxylated via a dienone intermediate and released as 3,4-DHPA; with the peroxide bond broken, C4a-hydroxyflavin releases the remaining oxygen atom by eliminating water and is released from the enzyme as FAD.
Biological Function.
To cope with the wide variety of phenolic compounds found in nature, bacterial pathways for degradation of aromatic compounds generally begin by channeling these diverse substrates towards a few common intermediates, which are then further degraded. Pathways for catabolizing aromatic compounds generally begin by adding two hydroxyl groups to the benzene ring, most often on adjacent carbons. This product then undergoes ring cleavage to produce a linear molecule which is ultimately degraded to intermediates of central metabolism, such as succinate, pyruvate, and carbon dioxide. In the case of 4-hydroxyphenylacetate, which only needs one hydroxyl group to be added, a monooxygenase is required.
Among common "E. coli" laboratory strains, the 4-HPA degradation pathway is not found in the commonly used K-12 strain, but it does appear in strains B, C, and W (the strain in which most research into the pathway has been done). Only strains containing this pathway are able to survive by metabolizing 4-HPA as the sole carbon source, showing that this pathway is required for catabolism of this compound, and likely for similar phenolic compounds as well.
Evolution.
In addition to the exclusively FADH2-dependent monooxygenase found in species such as "E. coli" and "T. thermophilus", a version of the enzyme which can use either reduced FAD or reduced FMN has been described in Acinetobacter baumannii. Although these enzymes catalyze similar reactions and share a similar acyl-CoA dehydrogenase fold, the FMN-dependent enzyme is allosterically regulated by 4-HPA while the FADH2-dependent enzyme is likely regulated by a simpler kinetic mechanism, in which low concentrations of 4-HPA lead the enzyme to bind and sequester FADH2 as part of the normal catalytic cycle, causing the free concentration of FADH2 to drop until the flavin oxidoreductase's reaction is indirectly inhibited as well. Along with other differences in regulation and substrate binding despite a shared fundamental catalytic mechanism, this has led to speculation that these enzymes collectively represent an example of convergent evolution.
Potential Applications.
In addition to 4-HPA, the enzyme has been reported to have activity on a number of other phenolic substrates. Metabolic engineers have demonstrated that microbes expressing the "E. coli" enzyme can catalyze reactions such as hydroxylation of tyrosine to L-dopa and hydroxylation of the pharmacologically interesting phenylpropanoids umbelliferone and resveratrol. However, these approaches are not currently used commercially.
References.
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| https://en.wikipedia.org/wiki?curid=14044631 |
14044646 | 4-hydroxyquinoline 3-monooxygenase | Class of enzymes
In enzymology, a 4-hydroxyquinoline 3-monooxygenase (EC 1.14.13.62) is an enzyme that catalyzes the chemical reaction
quinolin-4-ol + NADH + H+ + O2 formula_0 quinolin-3,4-diol + NAD+ + H2O
The 4 substrates of this enzyme are quinolin-4-ol, NADH, H+, and O2, whereas its 3 products are quinolin-3,4-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-4(1H)-one,NADH:oxygen oxidoreductase (3-oxygenating). This enzyme is also called quinolin-4(1H)-one 3-monooxygenase.
References.
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| https://en.wikipedia.org/wiki?curid=14044646 |
14044663 | 4-methoxybenzoate monooxygenase (O-demethylating) | Class of enzymes
In enzymology, a 4-methoxybenzoate monooxygenase (O-demethylating) (EC 1.14.99.15) is an enzyme that catalyzes the chemical reaction
4-methoxybenzoate + AH2 + O2 formula_0 4-hydroxybenzoate + formaldehyde + A + H2O
The 3 substrates of this enzyme are 4-methoxybenzoate, an electron acceptor AH2, and O2, whereas its 4 products are 4-hydroxybenzoate, formaldehyde, 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 4-methoxybenzoate,hydrogen-donor:oxygen oxidoreductase (O-demethylating). Other names in common use include 4-methoxybenzoate 4-monooxygenase (O-demethylating), 4-methoxybenzoate O-demethylase, p-anisic O-demethylase, and piperonylate-4-O-demethylase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References.
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14044677 | 4'-methoxyisoflavone 2'-hydroxylase | Class of enzymes
In enzymology, a 4'-methoxyisoflavone 2'-hydroxylase (EC 1.14.14.89, Formerly EC 1.14.13.53) is an enzyme that catalyzes the chemical reaction
formononetin + NADPH + H+ + O2 formula_0 2'-hydroxyformononetin + NADP+ + H2O
The 4 substrates of this enzyme are formononetin, NADPH, H+, and O2, whereas its 3 products are 2'-hydroxyformononetin, 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 formononetin,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase (ambiguous), and isoflavone 2'-hydroxylase (ambiguous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References.
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| https://en.wikipedia.org/wiki?curid=14044677 |
14044690 | 4-nitrophenol 2-monooxygenase | Class of enzymes
In enzymology, a 4-nitrophenol 2-monooxygenase (EC 1.14.13.29) is an enzyme that catalyzes the chemical reaction
4-nitrophenol + NADH + H+ + O2 formula_0 4-nitrocatechol + NAD+ + H2O
The 4 substrates of this enzyme are 4-nitrophenol, NADH, H+, and O2, whereas its 3 products are 4-nitrocatechol, 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 4-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 4-nitrophenol hydroxylase, and 4-nitrophenol-2-hydroxylase. This enzyme participates in gamma-hexachlorocyclohexane degradation. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14044690 |
14044706 | 4-sulfobenzoate 3,4-dioxygenase | Class of enzymes
In enzymology, a 4-sulfobenzoate 3,4-dioxygenase (EC 1.14.12.8) is an enzyme that catalyzes the chemical reaction
4-sulfobenzoate + NADH + H+ + O2 formula_0 3,4-dihydroxybenzoate + sulfite + NAD+
The 4 substrates of this enzyme are 4-sulfobenzoate, NADH, H+, and O2, whereas its 3 products are 3,4-dihydroxybenzoate, sulfite, 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 4-sulfobenzoate,NADH:oxygen oxidoreductase (3,4-hydroxylating, sulfite-forming). Other names in common use include 4-sulfobenzoate dioxygenase, and 4-sulfobenzoate 3,4-dioxygenase system. This enzyme participates in 2,4-dichlorobenzoate degradation. It has 3 cofactors: iron, FMN, and Iron-sulfur.
References.
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14044722 | 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase | Class of enzymes
In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction
5beta-cholestane-3alpha,7alpha-diol + NADPH + H+ + O2 formula_0 5beta-cholestane-3alpha,7alpha,12alpha-triol + NADP+ + H2O
The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha-diol, NADPH, H+, and O2, whereas its 3 products are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADP+, and H2O.
Nomenclature.
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 5beta-cholestane-3alpha,7alpha-diol,NADPH:oxygen oxidoreductase (12alpha-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha-diol 12alpha-monooxygenase, sterol 12alpha-hydroxylase (ambiguous), CYP8B1, and cytochrome P450 8B1.
References.
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Further reading.
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14044733 | 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase | Class of enzymes
In enzymology, a 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase (EC 1.14.13.36) is an enzyme that catalyzes the chemical reaction
trans-5-O-(4-coumaroyl)-D-quinate + NADPH + H+ + O2 formula_0 trans-5-O-caffeoyl-D-quinate + NADP+ + H2O
The 4 substrates of this enzyme are trans-5-O-(4-coumaroyl)-D-quinate, NADPH, H+, and O2, whereas its 3 products are trans-5-O-caffeoyl-D-quinate, 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 trans-5-O-(4-coumaroyl)-D-quinate,NADPH:oxygen oxidoreductase (3'-hydroxylating). Other names in common use include 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase, and coumaroylquinate(coumaroylshikimate) 3'-monooxygenase. This enzyme participates in phenylpropanoid biosynthesis.
References.
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14044746 | 5-pyridoxate dioxygenase | Class of enzymes
In enzymology, a 5-pyridoxate dioxygenase (EC 1.14.12.5) is an enzyme that catalyzes the chemical reaction
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + H+ + O2 formula_0 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+
The 4 substrates of this enzyme are 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate, NADPH, H+, and O2, whereas its two products are 2-(acetamidomethylene)-3-(hydroxymethyl)succinate 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 o oxygen into the other donor. The systematic name of this enzyme class is 5-pyridoxate,NADPH:oxygen oxidoreductase (decyclizing). This enzyme is also called 5-pyridoxate oxidase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and Flavoprotein.
References.
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14044755 | 6β-Hydroxyhyoscyamine epoxidase | Class of enzymes
In enzymology, a 6β-hydroxyhyoscyamine epoxidase (EC 1.14.11.14) is an enzyme that catalyzes the chemical reaction
(6"S")-6-hydroxyhyoscyamine + 2-oxoglutarate + O2 formula_0 scopolamine + succinate + CO2 + H2O
The 3 substrates of this enzyme are (6"S")-6-hydroxyhyoscyamine, 2-oxoglutarate, and O2, whereas its 4 products are scopolamine, succinate, CO2, 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 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. This enzyme participates in alkaloid biosynthesis ii. It has two cofactors: iron and ascorbate.
Nomenclature.
The systematic name of this enzyme class is (6"S")-6-hydroxyhyoscyamine,2-oxoglutarate oxidoreductase (epoxide-forming). This enzyme is also called hydroxyhyoscyamine dioxygenase.
References.
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14044767 | 6-oxocineole dehydrogenase | Class of enzymes
In enzymology, a 6-oxocineole dehydrogenase (EC 1.14.13.51) is an enzyme that catalyzes the chemical reaction
6-oxocineole + NADPH + H+ + O2 formula_0 1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one + NADP+ + H2O
The 4 substrates of this enzyme are 6-oxocineole, NADPH, H+, and O2, whereas its 3 products are 1,6,6-trimethyl-2,7-dioxabicyclo[3.2.2]nonan-3-one, 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 6-oxocineole,NADPH:oxygen oxidoreductase. This enzyme is also called 6-oxocineole oxygenase. This enzyme participates in terpenoid biosynthesis.
References.
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14044785 | 7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase | Class of enzymes
7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase (EC 1.14.14.139, previously EC 1.14.13.95) is an enzyme that catalyzes the chemical reaction:
7alpha-hydroxycholest-4-en-3-one + NADPH + H+ + O2 formula_0 7alpha,12alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O
The 4 substrates of this enzyme are 7alpha-hydroxycholest-4-en-3-one (7 alpha-hydroxy-4-cholesten-3-one, NADPH, H+, and O2. Its products are 7alpha,12alpha-dihydroxycholest-4-en-3-one, NADP+, and H2O.
Since 2015, the enzyme has been classified with EC 1.14.14.139 with the systematic name of 5β-cholestan-3α,7α-diol 12α-hydroxylase. Other names that have been used include 7alpha-hydroxycholest-4-en-3-one,NADPH:oxygen oxidoreductase (12alpha-hydroxylating), 7alpha-hydroxy-4-cholesten-3-one 12alpha-monooxygenase, CYP12, sterol 12alpha-hydroxylase (ambiguous), and HCO 12alpha-hydroxylase.
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 of oxygen into the other donor. It was purified and characterized from rabbit liver microsomes in 1992 and was cloned and sequenced in 1996. Its structure was 39% similar to human prostacyclin synthase (CYP8) and 31% similar to cholesterol 7 alpha-hydroxylase (CYP7).
This enzymatic activity is now known to be performed by the product of the "CYP8B1" gene. This step leads to the formation of the bile acid cholic acid. Cholic acid is a 3,7,12 tri-hydroxy bile acid and is one of the major bile acids in humans and many other animals. Activity of this enzyme determines the balance between cholic and chenodeoxycholic acids in humans.
References.
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14044796 | 7-deoxyloganin 7-hydroxylase | Class of enzymes
In enzymology, a 7-deoxyloganin 7-hydroxylase (EC 1.14.13.74) is an enzyme that catalyzes the chemical reaction
7-deoxyloganin + NADPH + H+ + O2 formula_0 loganin + NADP+ + H2O
The 4 substrates of this enzyme are 7-deoxyloganin, NADPH, H+, and O2, whereas its 3 products are loganin, 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 7-deoxyloganin,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). This enzyme participates in indole and ipecac alkaloid biosynthesis.
References.
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14044806 | 8-dimethylallylnaringenin 2'-hydroxylase | Class of enzymes
In enzymology, a 8-dimethylallylnaringenin 2'-hydroxylase (EC 1.14.13.103) is an enzyme that catalyzes the chemical reaction
sophoraflavanone B + NADPH + H+ + O2 formula_0 leachianone G + NADP+ + H2O
The 4 substrates of this enzyme are sophoraflavanone B, NADPH, H+, and O2, whereas its 3 products are leachianone G, 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 sophoraflavanone-B,NADPH:oxygen oxidoreductase (2'-hydroxylating). This enzyme is also called 8-DMAN 2'-hydroxylase.
References.
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14044819 | (+)-abscisic acid 8'-hydroxylase | Class of enzymes
In enzymology, a (+)-abscisic acid 8'-hydroxylase (EC 1.14.13.93) is an enzyme that catalyzes the chemical reaction
(+)-abscisate + NADPH + H+ + O2 formula_0 8'-hydroxyabscisate + NADP+ + H2O
The four substrates of this enzyme are (+)-abscisate, NADPH, H+, and O2, whereas its three products are 8'-hydroxy-abscisate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, to be specific 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 of oxygen into the other donor. This enzyme participates in carotenoid biosynthesis.
Nomenclature.
The systematic name of this enzyme class is abscisate,NADPH:oxygen oxidoreductase (8'-hydroxylating). Other names in common use include
References.
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14044828 | Acyl-(acyl-carrier-protein) desaturase | Class of enzymes
In enzymology, an acyl-[acyl-carrier-protein] desaturase (EC 1.14.19.2) is an enzyme that catalyzes the chemical reaction
stearoyl-[acyl-carrier-protein] + reduced acceptor + O2 formula_0 oleoyl-[acyl-carrier-protein] + acceptor + 2 H2O
The systematic name of this enzyme class is acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase. Other names in common use include stearyl acyl carrier protein desaturase, and stearyl-ACP desaturase. This enzyme participates in polyunsaturated fatty acid biosynthesis. It employs one cofactor, ferredoxin.
Reaction.
The 3 substrates of this enzyme are stearoyl-(acyl-carrier-protein), reduced acceptor, and O2, whereas its 3 products are oleoyl-(acyl-carrier-protein), acceptor, and H2O.
The precise mechanism of this class of enzymes is not known, however recent studies using the kinetic isotope effect suggest that the rate limiting step is the removal of a hydrogen from the carbon nearest the carboxylic acid group. The diiron cluster moves through to a peroxo intermediate which can then dehydrate the short-lived alcohol intermediate, liberating water. There are a variety of specific enzymes within this class that attack using this mechanism, but do so at different points along the carbon chain of their respective fatty acids
Biological Function.
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 oxidation of a pair of donors resulting in the formation of H2O.
This family of enzymes is found only in the plastids of higher plant cells, unlike other desaturases such as acyl-lipid desaturases and acyl-CoA desaturases. The regiospecific role of stearoyl-ACP desaturase is to initialise multiple desaturations by acyl-lipid desaturases. Oleic acid is formed from this reaction is transported to either the thylakoid or cytoplasm to complete desaturation.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1OQ4, 1OQ7, 1OQ9, 1OQB, and 1ZA0. 2XZ0 and 2XZ1 show the dramatic change in conformation of the enzyme when bound (2XZ1) and unbound (2XZ0). As a dimer, the fatty acid chain binds to a hydrophobic pocket at the interface of the two dimers. This central channel is mirrored by binding sites for the electron donors on either side.
The stabilisation of the diiron-oxo element required to catalyse the reaction has been of particular interest. Crystallographic studies suggest that the iron groups are held in place by the desaturase using aspartate and glutamate. A structure of aspartate-X-X-histidine was found to be a common motif in several plant species. This desaturase family can be further divided by the consensus motif used to hold the iron clusters in place. Of particular note are the "soluble" desaturases, which use carboxylic acid groups, whereas it is possible for some variants to use histidines instead. The histidine rich desaturases tend to be integral membrane proteins.
Structural studies strongly suggest that the animal form of this enzyme (Stearoyl-acyl-carrier-protein desaturase) is evolutionarily divergent from the forms found in plants and fungi. This is to be expected as the roles of the enzymes are different in both. For example, in insects, the desaturase is critical in the formation of ceramide, and for complex signalling molecules (pheremones), while in fungi, the function of the enzyme, and concentration of unsaturated lipids is regulated in response to function of growth temperature by controlling membrane fluidity in cells.
Potential Industrial Relevance.
This enzyme class plays a critical role in the biosynthesis of unsaturated fatty acids in plants, and are very specific to their substrates. A common theme in recent research has been to identify uncommon desaturases in various plants and isolate their genetic code. In particular, this can then be inserted into model cells (such as "Escherichia coli") and up-regulated through metabolic engineering to skew the composition of oils produced by the model cells.
This becomes a particularly lucrative endeavour if it becomes possible to successfully synthesise so-called Omega-3 fatty acids or other nutraceutical products from basic saturated fatty acids, and extract them from their hosts.
References.
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14044841 | Albendazole monooxygenase | Class of enzymes
In enzymology, an albendazole monooxygenase (EC 1.14.13.32) is an enzyme that catalyzes the chemical reaction
albendazole + NADPH + H+ + O2 formula_0 albendazole S-oxide + NADP+ + H2O
The four substrates of this enzyme are albendazole, NADPH, H+, and O2, whereas its three products are albendazole S-oxide, NADP+, and H2O.
This enzyme is coded by the gene for CYP3A4 and 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 of oxygen into the other donor. The systematic name of this enzyme class is albendazole,NADPH:oxygen oxidoreductase (sulfoxide-forming). Other names in common use include albendazole oxidase, and albendazole sulfoxidase. It employs one cofactor, FAD.
References.
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14044852 | Alkanal monooxygenase (FMN-linked) | In enzymology, an alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) is an enzyme that catalyzes the chemical reaction
RCHO + reduced FMN + O2 formula_0 RCOOH + FMN + H2O + hnu
The 3 substrates of this enzyme are RCHO, reduced FMN, and O2, whereas its 4 products are RCOOH, FMN, H2O, and hn.
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 reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing). Other names in common use include bacterial luciferase, aldehyde monooxygenase, luciferase, and Vibrio fischeri luciferase.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1BRL, 1BSL, 1LUC, and 1XKJ.
References.
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14044868 | Alkane 1-monooxygenase | Enzyme
In enzymology, an alkane 1-monooxygenase (EC 1.14.15.3) is an enzyme that catalyzes the chemical reactions
an alkane + reduced rubredoxin + O2 formula_0 a primary alcohol + oxidized rubredoxin + H2O.
Alkanes of 6 to 22 carbons have been observed as substrates. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with oxygen as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkane, reduced-rubredoxin:oxygen 1-oxidoreductase. Other names in common use include alkane 1-hydroxylase, omega-hydroxylase, fatty acid omega-hydroxylase, alkane monooxygenase, 1-hydroxylase, AlkB, and alkane hydroxylase. It contains a diiron non-heme active site.
Recently two crystal structures of the enzyme have appeared that provide much more information about the structure of the enzyme. Both structures show an unusual diiron active site where the two iron ions are separated by more than 5 angstroms. Neither structure shows evidence for a ligand that would bridge the two iron ions.
References.
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14044880 | Alkanesulfonate monooxygenase | In enzymology, an alkanesulfonate monooxygenase (EC 1.14.14.5) is an enzyme that catalyzes the chemical reaction
an alkanesulfonate (R-CH2-SO3H) + FMNH2 + O2 formula_0 an aldehyde (R-CHO) + FMN + sulfite + H2O
The 3 substrates of this enzyme are alkanesulfonate (R-CH2-SO3H), FMNH2, and O2, whereas its 4 products are aldehyde, FMN, sulfite, 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 reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkanesulfonate, reduced-FMN:oxygen oxidoreductase. Other names in common use include SsuD, and sulfate starvation-induced protein 6.
References.
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14044892 | Alkene monooxygenase | Class of enzymes
In enzymology, an alkene monooxygenase (EC 1.14.13.69) is an enzyme that catalyzes the chemical reaction
propene + NADH + H+ + O2 formula_0 1,2-epoxypropane + NAD+ + H2O
The 4 substrates of this enzyme are propene, NADH, H+, and O2, whereas its 3 products are 1,2-epoxypropane, 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 alkene,NADH:oxygen oxidoreductase. This enzyme is also called alkene epoxygenase. This enzyme participates in tetrachloroethene degradation.
References.
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14044909 | Aminocyclopropanecarboxylate oxidase | In enzymology, an aminocyclopropanecarboxylate oxidase (EC 1.14.17.4) is an enzyme that catalyzes the chemical reaction
1-aminocyclopropane-1-carboxylate + ascorbate + O2 formula_0 ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
The 3 substrates of this enzyme are 1-aminocyclopropane-1-carboxylate, ascorbate, and O2, whereas its 5 products are ethylene, cyanide, dehydroascorbate, CO2, 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 reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming). Other names in common use include ACC oxidase, and ethylene-forming enzyme.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1W9Y and 1WA6.
Reaction Mechanism.
Mechanistic and structural studies support binding of ACC and oxygen to an iron center located in the active site of ACC oxidase. The ring-opening of bound ACC is believed to result in the elimination of ethylene together with an unstable intermediate, cyanoformate ion, which then decomposes to cyanide ion and carbon dioxide. Cyanide ion is a known deactivating agent for iron-containing enzymes, but the cyanoformate ion intermediate is believed to play a vital role to carry potentially toxic cyanide away from the active site of ACC oxidase. Cyanoformate was recently identified in condensed media as a tetraphenylphosphonium salt with a weak carbon-carbon bond.
References.
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14044923 | Androst-4-ene-3,17-dione monooxygenase | In enzymology, an androst-4-ene-3,17-dione monooxygenase (EC 1.14.99.12) is an enzyme that catalyzes the chemical reaction
androst-4-ene-3,17-dione + AH2 + O2 formula_0 3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone + A + H2O
The 3 substrates of this enzyme are androst-4-ene-3,17-dione, an electron acceptor AH2, and O2, whereas its 3 products are 3-oxo-13,17-secoandrost-4-ene-17,13alpha-lactone, 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 androst-4-ene-3,17-dione-hydrogen-donor:oxygen oxidorcockeductase (13-hydroxylating, lactonizing). Other names in common use include androstene-3,17-dione hydroxylase, androst-4-ene-3,17-dione 17-oxidoreductase, androst-4-ene-3,17-dione hydroxylase, androstenedione monooxygenase, and 4-androstene-3,17-dione monooxygenase. This enzyme participates in androgen and estrogen metabolism.
References.
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14044938 | Anhydrotetracycline monooxygenase | Class of enzymes
In enzymology, an anhydrotetracycline monooxygenase (EC 1.14.13.38) is an enzyme that catalyzes the chemical reaction
anhydrotetracycline + NADPH + H+ + O2 formula_0 12-dehydrotetracycline + NADP+ + H2O
The 4 substrates of this enzyme are anhydrotetracycline, NADPH, H+, and O2, whereas its 3 products are 12-dehydrotetracycline, 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 anhydrotetracycline,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include ATC oxygenase, and anhydrotetracycline oxygenase. This enzyme participates in tetracycline biosynthesis and biosynthesis of type ii polyketide products.
References.
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14044948 | Anthranilate 1,2-dioxygenase (deaminating, decarboxylating) | Class of enzymes
In enzymology, an anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) is an enzyme that catalyzes the chemical reaction
anthranilate + NAD(P)H + 2 H+ + O2 formula_0 catechol + CO2 + NAD(P)+ + NH3
The 5 substrates of this enzyme are anthranilate, NADH, NADPH, H+, and O2, whereas its 5 products are catechol, CO2, NAD+, NADP+, and NH3.
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 anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating, deaminating, decarboxylating). Other names in common use include anthranilate hydroxylase, anthranilic hydroxylase, and anthranilic acid hydroxylase. This enzyme participates in 3 metabolic pathways: benzoate degradation via hydroxylation, carbazole degradation, and nitrogen metabolism. It employs one cofactor, iron.
References.
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14044962 | Anthranilate 3-monooxygenase | Enzyme
In enzymology, an anthranilate 3-monooxygenase (EC 1.14.16.3) is an enzyme that catalyzes the chemical reaction
anthranilate + tetrahydrobiopterin + O2 formula_0 3-hydroxyanthranilate + dihydrobiopterin + H2O
The 3 substrates of this enzyme are anthranilate, tetrahydrobiopterin, and O2, whereas its 3 products are 3-hydroxyanthranilate, dihydrobiopterin, 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 reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is anthranilate,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating). Other names in common use include anthranilate 3-hydroxylase, anthranilate hydroxylase, anthranilic hydroxylase, and anthranilic acid hydroxylase. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.
References.
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14044980 | Anthranilate 3-monooxygenase (deaminating) | Enzyme class
In enzymology, an anthranilate 3-monooxygenase (deaminating) (EC 1.14.13.35) is an enzyme that catalyzes the chemical reaction
anthranilate + NADPH + H+ + O2 formula_0 2,3-dihydroxybenzoate + NADP+ + NH3
The 4 substrates of this enzyme are anthranilate, NADPH, H+, and O2, whereas its 3 products are 2,3-dihydroxybenzoate, NADP+, and NH3.
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 anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating). Other names in common use include anthranilate hydroxylase, anthranilate 2,3-dioxygenase (deaminating), anthranilate hydroxylase (deaminating), anthranilic hydroxylase, and anthranilate 2,3-hydroxylase (deaminating). This enzyme participates in 3 metabolic pathways: benzoate degradation via hydroxylation, carbazole degradation, and nitrogen metabolism.
References.
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14044996 | Anthraniloyl-CoA monooxygenase | Class of enzymes
In enzymology, an anthraniloyl-CoA monooxygenase (EC 1.14.13.40) is an enzyme that catalyzes the chemical reaction
2-aminobenzoyl-CoA + 2 NAD(P)H + 2 H+ + O2 formula_0 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
The 5 substrates of this enzyme are 2-aminobenzoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are 2-amino-5-oxocyclohex-1-enecarboxyl-CoA, H2O, 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 one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing). Other names in common use include anthraniloyl coenzyme A reductase, and 2-aminobenzoyl-CoA monooxygenase/reductase. This enzyme participates in carbazole degradation. It employs one cofactor, FAD.
References.
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14045028 | Benzoate 1,2-dioxygenase | Class of enzymes
In enzymology, a benzoate 1,2-dioxygenase (EC 1.14.12.10) is an enzyme that catalyzes the chemical reaction
benzoate + NADH + H+ + O2 formula_0 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
The 4 substrates of this enzyme are benzoate, NADH, H+, and O2, whereas its two products are 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate 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 benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include benzoate hydroxylase, benzoate hydroxylase, benzoic hydroxylase, benzoate dioxygenase, benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, and decarboxylating) [incorrect]. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: FAD, Iron, and Sulfur.
References.
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14045041 | Benzoate 4-monooxygenase | Class of enzymes
In enzymology, a benzoate 4-monooxygenase (EC 1.14.14.92, Formerly EC 1.14.13.12) is an enzyme that catalyzes the chemical reaction
benzoate + NADPH + H+ + O2 formula_0 4-hydroxybenzoate + NADP+ + H2O
The 4 substrates of this enzyme are benzoate, NADPH, H+, and O2, whereas its 3 products are 4-hydroxybenzoate, 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 benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use include benzoic acid 4-hydroxylase, benzoate 4-hydroxylase, benzoic 4-hydroxylase, benzoate-p-hydroxylase, and p-hydroxybenzoate hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: iron, Tetrahydrobiopterin, and Tetrahydropteridine.
References.
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14045055 | Benzoyl-CoA 3-monooxygenase | Class of enzymes
In enzymology, a benzoyl-CoA 3-monooxygenase (EC 1.14.13.58) is an enzyme that catalyzes the chemical reaction:
benzoyl-CoA + NADPH + H+ + O2 formula_0 3-hydroxybenzoyl-CoA + NADP+ + H2O
The 4 substrates of this enzyme are benzoyl-CoA, NADPH, H+, and O2, whereas its 3 products are 3-hydroxybenzoyl-CoA, 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 benzoyl-CoA,NADPH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called benzoyl-CoA 3-hydroxylase.
The enzyme is found in Pseudomonas bacteria.
References.
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14045069 | Berbamunine synthase | In enzymology, a berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the chemical reaction
(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 formula_0 berbamunine + NADP+ + 2 H2O
The 5 substrates of this enzyme are (S)-N-methylcoclaurine, (R)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are berbamunine, 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 the other dehydrogenated. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling). This enzyme is also called (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). This enzyme participates in alkaloid biosynthesis i.
References.
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14045085 | Biphenyl 2,3-dioxygenase | Class of enzymes
In enzymology, a biphenyl 2,3-dioxygenase (EC 1.14.12.18) is an enzyme that catalyzes the chemical reaction
biphenyl + NADH + H+ + O2 formula_0 (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
The 4 substrates of this enzyme are biphenyl, NADH, H+, and O2, whereas its two products are (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol 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 biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating). This enzyme is also called biphenyl dioxygenase. This enzyme participates in biphenyl degradation.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ULI and 1ULJ.
References.
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14045124 | Camphor 1,2-monooxygenase | Class of enzymes
In enzymology, a camphor 1,2-monooxygenase (EC 1.14.15.2) is an enzyme that catalyzes the chemical reaction
(+)-bornane-2,5-dione + reduced rubredoxin + O2 formula_0 5-oxo-1,2-campholide + oxidized rubredoxin + H2O
The 3 substrates of this enzyme are (+)-bornane-2,5-dione, reduced rubredoxin, and O2, whereas its 3 products are 5-oxo-1,2-campholide, oxidized rubredoxin, 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 reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,2-lactonizing). Other names in common use include 2,5-diketocamphane lactonizing enzyme, camphor ketolactonase I, oxygenase, camphor 1,2-mono, and ketolactonase I. It employs one cofactor, iron.
References.
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14045145 | Camphor 5-monooxygenase | In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction
(+)-camphor + putidaredoxin + O2 formula_0 (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
The 3 substrates of this enzyme are (+)-camphor, putidaredoxin, and O2, whereas its 3 products are (+)-exo-5-hydroxycamphor, oxidized putidaredoxin, 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 reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced putidaredoxin:oxygen oxidoreductase (5-hydroxylating). Other names in common use include camphor 5-exo-methylene hydroxylase, 2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, camphor 5-exo-hydroxylase, camphor 5-exohydroxylase, camphor hydroxylase, d-camphor monooxygenase, methylene hydroxylase, methylene monooxygenase, D-camphor-exo-hydroxylase, and camphor methylene hydroxylase. It employs one cofactor, heme.
Structural studies.
As of late 2007, 58 structures have been solved for this class of enzymes, with PDB accession codes 1AKD, 1C8J, 1CP4, 1GEB, 1GEK, 1GEM, 1GJM, 1IWI, 1IWJ, 1IWK, 1J51, 1K2O, 1LWL, 1MPW, 1NOO, 1O76, 1P2Y, 1P7R, 1PHA, 1PHB, 1PHC, 1PHD, 1PHE, 1PHF, 1PHG, 1QMQ, 1RE9, 1RF9, 1T85, 1T86, 1T87, 1T88, 1YRC, 1YRD, 2A1M, 2A1N, 2A1O, 2CP4, 2CPP, 2FE6, 2FER, 2FEU, 2FRZ, 2GQX, 2GR6, 2H7Q, 2H7R, 2H7S, 3CP4, 3CPP, 4CP4, 4CPP, 5CP4, 5CPP, 6CP4, 6CPP, 7CPP, and 8CPP.
Examples.
Cytochrome P450 camphor 5-monooxygenase is a bacterial enzyme originally from "Pseudomonas putida", which catalyzes a critical step in the metabolism of camphor. In 1987, Cytochrome P450cam was the first cytochrome P450 three-dimensional protein structure solved by X-ray crystallography.
It is a heterotrimeric protein derived from the products of three genes: a cytochrome P450 enzyme (encoded by the CamC gene from the CYP family CYP101), a Putidaredoxin (encoded by the CamB gene) complexed with cofactors 2Fe-2S, a NADH-dependent Putidaredoxin reductase (encoded by the CamA gene).
References.
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Further reading.
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14045159 | Carotene 7,8-desaturase | Oxidoreductases enzyme
In enzymology, a carotene 7,8-desaturase (EC 1.14.99.30) is an enzyme that catalyzes the chemical reaction
neurosporene + AH2 + O2 formula_0 lycopene + A + 2 H2O
The 3 substrates of this enzyme are neurosporene, an electron acceptor AH2, and O2, whereas its 3 products are lycopene, 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 derived from O miscellaneous. The systematic name of this enzyme class is carotene, hydrogen-donor:oxygen oxidoreductase. This enzyme is also called zeta-carotene desaturase. This enzyme participates in carotenoid biosynthesis - general.
References.
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14045176 | Cholestanetriol 26-monooxygenase | Class of enzymes
In enzymology, a cholestanetriol 26-monooxygenase (EC 1.14.13.15) is an enzyme that catalyzes the chemical reaction
5beta-cholestane-3alpha,7alpha,12alpha-triol + NADPH + H+ + O2 formula_0 (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NADP+ + H2O
The 4 substrates of this enzyme are 5beta-cholestane-3alpha,7alpha,12alpha-triol, NADPH, H+, and O2, whereas its 3 products are (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol, 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 5beta-cholestane-3alpha,7alpha,12alpha-triol,NADPH:oxygen oxidoreductase (26-hydroxylating). Other names in common use include 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase, cholestanetriol 26-hydroxylase, sterol 27-hydroxylase, sterol 26-hydroxylase, cholesterol 27-hydroxylase, CYP27A, CYP27A1, and cytochrome P450 27A1'. This enzyme participates in bile acid biosynthesis and ppar signaling pathway.
References.
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14045189 | Cholesterol 24-hydroxylase | Protein family
Cholesterol 24-hydroxylase (EC 1.14.13.98), also commonly known as cholesterol 24S-hydroxylase, cholesterol 24-monooxygenase, CYP46, or CYP46A1, is an enzyme that catalyzes the conversion of cholesterol to 24S-hydroxycholesterol. It is responsible for the majority of cholesterol turnover in the human central nervous system. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating).
This enzyme is a member of the cytochrome P450 (CYP) superfamily of enzymes. Like many other CYP enzymes that act on cholesterol, cholesterol-24 hydroxylase is a monooxygenase that hydroxylates the side-chain of cholesterol.
Because 24S-hydroxycholesterol is more polar than cholesterol, it can more easily pass the blood–brain barrier to exit the brain and pass into the bloodstream, where it can then travel to the liver to be further degraded. This enzyme has also been found at low quantities in the retina, where it performs the same function to a lesser degree.
Genetic cloning of the encoding gene ("CYP46A1") was first accomplished in 1999 and an extensive "E. coli" expression and purification system was later developed in 2003.
Molecular structure.
The enzymatic structure of the human cholesterol-24 hydroxylase was determined via crystallography at the Stanford Synchrotron Radiation Lightsource, and was shown to be a 57kDa (500 residue) monomeric heme-containing protein bound to the endoplasmic reticulum in neurons.
Cholesterol-24 hydroxylase is similar in structure to many other cytochrome P450s, possessing, for example, the conserved stretch of 23 hydrophobic residues in the N-terminus that make up a transmembrane-anchoring domain (residues 3-27). Even so, the cholesterol-24 hydroxylase C-terminus has a unique proline-rich region of 5 repeated proline residues, a structural motif absent in all other related cytochrome p450 enzymes. While the exact function of these proline residues remain highly speculative, it has been shown that the deletion of this region results in a two-fold decrease in the enzyme’s catalytic efficiency.
Binding of cholesterol results in an enzymatic conformational change and a subsequent induced fit of the active site around the cholesterol molecule, anchoring the hydroxylation site (C-24, C-25) near the catalytic center of the enzyme (5.7Å from the iron core of the heme molecule to allow oxyferryl intermediates to perform the cholesterol hydroxylation). A loop region, known as the B'-C loop, has a series of 5 residues (residues 116-120) unique to cholesterol-24 hydroxylase that contribute to the positioning of the cholesterol molecule within the active site. A single cholesterol molecule takes up the entirety of the active site, with the aliphatic tail of the cholesterol held in place by interactions with the following hydrophobic residues: Phe-121, Val-126, Ile-301, Ala-302, Ala-367, Thr-475. The active site is accessed via a single entrance created by two helices (B' and F) and the β1-sheet.
There are no known allosteric regulatory sites.
Enzyme mechanism.
Cholesterol-24 hydroxylase catalyzes the following reaction:
cholesterol + NADPH + H+ + O2 formula_0 (24S)-24-hydroxycholesterol + NADP+ + H2O
The 4 substrates of this enzyme are cholesterol, NADPH, H+, and O2, and its 3 products are 24S-hydroxycholesterol, NADP+, and H2O.
Like all other cytochrome P450s, cholesterol-24 hydroxylase utilizes an oxyferryl intermediate to hydroxylate cholesterol. The oxyferryl radical takes the hydrogen from carbon-24 to create an alkyl radical intermediate. The cholesterol alkyl radical then combines with the activated oxygen on the heme to create 24S-hydroxycholesterol.
Function.
Cholesterol-24 hydroxylase contributes to brain cholesterol homeostasis by hydroxylating cholesterol at carbon-24 to 24S-hydroxycholesterol to allow for elimination of cholesterol from the brain to the liver. Only around 6–7 mg of cholesterol, however, are hydroxylated by this enzyme on a daily basis, suggesting the existence of alternative functions – presently unknown. "In vitro" experiments have shown that it is also capable of further metabolizing 24S-hydroxycholesterol into 24,25- and 24,27-dihydroxycholesterols.
Cholesterol-24 hydroxylase has a variety of possible substrates, including: elongated steroid chains, cholesterol derivatives, and a variety of drug candidates. As such, it is also likely that it plays a role in lipid metabolism in the brain beyond cholesterol breakdown.
Because 24S-hydroxycholesterol (main product of this enzyme) is a major activator of oxysterol liver X receptors (LXR), it is possible that cholesterol-24 hydroxylase may play an indirect regulatory role in the metabolism of lipids in the liver. 24S-hydroxycholesterol also regulates the rate of cholesterol synthesis in the brain, with high levels of 24S-hydroxycholesterol shown to reduce mRNA levels of the following cholesterol synthesis enzymes: HMG CoA reductase, squalene synthase, and FPP synthase.
Clinical significance.
Variable expression of cholesterol-24 hydroxylase has been linked to the onset of Alzheimer's disease (AD) in humans. Studies have shown that in AD patients, there is significant decreased expression of cholesterol-24 hydroxylase in neurons. As a result, there is a marked increase of cholesterol in the brain tissue, consistent with the trend observed in AD patients. Neuron degradation in AD has often been attributed to the imbalance in cholesterol homeostasis, and many scientists hypothesize that the lowered expression of cholesterol-24 hydroxylase may be the main cause of this imbalance.
On the other hand, while there is decreased expression in the neurons, there is a contrasting increase of expression in the AD patients' astrocytes, where there is a consequent build-up of the product, 24S-hydroxycholesterol. Recent studies have shown that the increased levels of 24S-hydroxycholesterol in astrocytes may lead to a loss of glial glutamate transporters (EAAT2) and the consequent loss of the glutamate uptake function in the brain, another common symptom observed in AD patients.
Still, the link between expression levels of cholesterol-24 hydroxylase and Alzheimer's Disease remain disputable. While some studies have shown that polymorphisms in the encoding gene for cholesterol-24 hydroxylase have an established positive correlation with AD onset, other publications did not find such an association.
Increased expression of cholesterol-24 hydroxylase has also been observed in patients of traumatic brain injury, leading to decreased levels of cholesterol in the plasma membrane. This is hypothesized to be the brain’s typical response to injury.
Cholesterol-24 hydroxylase is easily inhibited by many drugs due to its broad substrate specificity. It has been shown to metabolize bufuralol, progesterone, dextromethorphan, methoxyresorufin, cortisol, diclofenac, phenacetin, and testosterone. The ability for inhibition by various xenobiotics makes this enzyme a prime candidate for drug therapy for AD or other brain injuries.
References.
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14045198 | Cholesterol 25-hydroxylase | Class of enzymes
In enzymology, a cholesterol 25-hydroxylase (EC 1.14.99.38) is an enzyme that catalyzes the chemical reaction
cholesterol + AH2 + O2 formula_0 25-hydroxycholesterol + A + H2O
The 3 substrates of this enzyme are cholesterol, an electron acceptor AH2, and O2, whereas its 3 products are 25-hydroxycholesterol (25HC), 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 cholesterol, hydrogen-donor:oxygen oxidoreductase (25-hydroxylating). This enzyme is also called cholesterol 25-monooxygenase.
Transcripts for this enzyme have been identified in macrophages from the testis.
CH25H is an interferon-stimulated gene, and its primary product 25HC may have broad-spectrum antiviral activity, demonstrated in mice against HIV, ebola, Nipah virus, Rift Valley Fever virus, and SARS-CoV-2. Specifically, 25HC blocks membrane fusion between the cell and virus, and may "implicate membrane-modifying oxysterols as potential antiviral therapeutics.” Recently, upregulation of CH25H has been shown to play a role in effectively restricting infection of lung epithelial cells with SARS-Cov-2 through its enzymatic product, 25HC, which depletes accessible membrane cholesterol so that the virus is unable to achieve fusion with the cell membrane necessary for entry and infection.
It has been proposed, based on experimental research in both mice and human cell culture, that 25HC is a potent senolytic. Further research needs to elaborate on this research and reveal its true significance to aging.
References.
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Further reading.
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14045209 | Cholesterol 7alpha-monooxygenase | Enzyme
In enzymology, a cholesterol 7alpha-monooxygenase (EC 1.14.13.17) is an enzyme that catalyzes the chemical reaction
cholesterol + NADPH + H+ + O2 formula_0 7alpha-hydroxycholesterol + NADP+ + H2O
The 4 substrates of this enzyme are cholesterol, NADPH, H+, and O2, whereas its 3 products are 7-alpha-hydroxycholesterol, 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 cholesterol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). Other names in common use include cholesterol 7alpha-hydroxylase, and CYP7A1. This enzyme participates in bile acid biosynthesis and ppar signaling pathway. It employs one cofactor, heme.
References.
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14045227 | Choline monooxygenase | Class of enzymes
In enzymology, a choline monooxygenase (EC 1.14.15.7) is an enzyme that catalyzes the chemical reaction
choline + O2 + 2 reduced ferredoxin + 2 H+ formula_0 betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
The 4 substrates of this enzyme are choline, O2, reduced ferredoxin, and H+, whereas its 3 products are betaine aldehyde hydrate, H2O, and oxidized ferredoxin.
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 reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is choline, reduced-ferredoxin:oxygen oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism.
References.
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14045243 | CMP-N-acetylneuraminate monooxygenase | Class of enzymes
In enzymology, a CMP-N-acetylneuraminate monooxygenase (EC 1.14.18.2) is an enzyme that catalyzes the chemical reaction
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+ formula_0 CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
The 4 substrates of this enzyme are CMP-N-acetylneuraminate, ferrocytochrome b5, O2, and H+, whereas its 3 products are CMP-N-glycoloylneuraminate, ferricytochrome b5, 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 another compound as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is CMP-N-acetylneuraminate,ferrocytochrome-b5:oxygen oxidoreductase (N-acetyl-hydroxylating). Other names in common use include CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, cytidine monophosphoacetylneuraminate monooxygenase, N-acetylneuraminic monooxygenase, and cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. This enzyme participates in aminosugars metabolism.
References.
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14045253 | Corticosterone 18-monooxygenase | Class of enzymes
In enzymology, a corticosterone 18-monooxygenase (EC 1.14.15.5) is an enzyme that catalyzes the chemical reaction
corticosterone + reduced adrenal ferredoxin + O2 formula_0 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
The 3 substrates of this enzyme are corticosterone, reduced adrenal ferredoxin, and O2, whereas its 3 products are 18-hydroxycorticosterone, oxidized adrenal ferredoxin, 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 reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase (18-hydroxylating). Other names in common use include corticosterone 18-hydroxylase, and corticosterone methyl oxidase. This enzyme participates in c21-steroid hormone metabolism.
References.
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14045295 | Cyclopentanone monooxygenase | Class of enzymes
In enzymology, a cyclopentanone monooxygenase (EC 1.14.13.16) is an enzyme that catalyzes the chemical reaction
cyclopentanone + NADPH + H+ + O2 formula_0 5-valerolactone + NADP+ + H2O
The 4 substrates of this enzyme are cyclopentanone, NADPH, H+, and O2, whereas its 3 products are 5-valerolactone, 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 cyclopentanone,NADPH:oxygen oxidoreductase (5-hydroxylating, lactonizing). This enzyme is also called cyclopentanone oxygenase.
References.
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14045305 | Deacetoxycephalosporin-C hydroxylase | Class of enzymes
In enzymology, a deacetoxycephalosporin-C hydroxylase (EC 1.14.11.26) is an enzyme that catalyzes the chemical reaction
deacetoxycephalosporin C + 2-oxoglutarate + O2 formula_0 deacetylcephalosporin C + succinate + CO2
The 3 substrates of this enzyme are deacetoxycephalosporin C, 2-oxoglutarate, and O2, whereas its 3 products are deacetylcephalosporin C, 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 deacetoxycephalosporin-C,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include deacetylcephalosporin C synthase, 3'-methylcephem hydroxylase, DACS, DAOC hydroxylase, and deacetoxycephalosporin C hydroxylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14045305 |
14045351 | Desacetoxyvindoline 4-hydroxylase | In enzymology, a desacetoxyvindoline 4-hydroxylase (EC 1.14.11.20) is an enzyme that catalyzes the chemical reaction
desacetoxyvindoline + 2-oxoglutarate + O2 formula_0 deacetylvindoline + succinate + CO2
The 3 substrates of this enzyme are desacetoxyvindoline, 2-oxoglutarate, and O2, whereas its 3 products are deacetylvindoline, 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 desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4beta-hydroxylating). Other names in common use include desacetoxyvindoline 4-hydroxylase, desacetyoxyvindoline-17-hydroxylase, D17H, desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase, and (4beta-hydroxylating). This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14045351 |
14045369 | Delta12-fatty acid dehydrogenase | In enzymology, a Delta12-fatty acid dehydrogenase (EC 1.14.99.33) is an enzyme that catalyzes the chemical reaction
linoleate + 2AH + O2 formula_0 crepenynate + 2A + H2O
where AH is either NADH or NADPH.
The 3 substrates of this enzyme are linoleate, 2AH, and O2, whereas its 3 products are crepenynate, 2A, 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.
This enzyme participates in linoleic acid metabolism.
Nomenclature.
The systematic name of this enzyme class is linoleate, hydrogen-donor:oxygen oxidoreductase (Delta12-unsaturating). Other names in common use include
References.
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Further reading.
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| https://en.wikipedia.org/wiki?curid=14045369 |
14045382 | Deoxyhypusine monooxygenase | In enzymology, a deoxyhypusine monooxygenase (EC 1.14.99.29) is an enzyme that catalyzes the chemical reaction
protein "N"6-(4-aminobutyl)--lysine + AH2 + O2 formula_0 protein "N"6-[("R")-4-amino-2-hydroxybutyl]--lysine + A + H2O
The 3 substrates of this enzyme are a protein-bound "N"6-(4-aminobutyl)--lysine, an electron acceptor AH2, and O2, and its 3 products are protein-bound "N"6-[("R")-4-amino-2-hydroxybutyl]--lysine, 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 deoxyhypusine,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating). Other names in common use include deoxyhypusine hydroxylase, and deoxyhypusine dioxygenase.
Mammalian proteins.
The HUGO symbol for human gene and protein is DOHH, the full name is deoxyhypusine hydroxylase, and there are orthologs in other mammals. The orthologs have the same symbol, except for rodents, there the symbol is Dohh. The difference in case is just a meaningless historical artifact.
References.
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| https://en.wikipedia.org/wiki?curid=14045382 |
14045398 | Deoxysarpagine hydroxylase | Class of enzymes
In enzymology, a deoxysarpagine hydroxylase (EC 1.14.13.91) is an enzyme that catalyzes the chemical reaction
10-deoxysarpagine + NADPH + H+ + O2 formula_0 sarpagine + NADP+ + H2O
The 4 substrates of this enzyme are 10-deoxysarpagine, NADPH, H+, and O2, whereas its 3 products are sarpagine, 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 of oxygen into the other donor. The systematic name of this enzyme class is 10-deoxysarpagine,NADPH:oxygen oxidoreductase (10-hydroxylating). This enzyme is also called DOSH.
References.
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| https://en.wikipedia.org/wiki?curid=14045398 |
14045406 | Dihydrochelirubine 12-monooxygenase | Class of enzymes
In enzymology, a dihydrochelirubine 12-monooxygenase (EC 1.14.13.57) is an enzyme that catalyzes the chemical reaction
dihydrochelirubine + NADPH + H+ + O2 formula_0 12-hydroxydihydrochelirubine + NADP+ + H2O
The 4 substrates of this enzyme are dihydrochelirubine, NADPH, H+, and O2, whereas its 3 products are 12-hydroxydihydrochelirubine, 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 dihydrochelirubine,NADPH:oxygen oxidoreductase (12-hydroxylating). This enzyme is also called dihydrochelirubine 12-hydroxylase. This enzyme participates in alkaloid biosynthesis i.
References.
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| https://en.wikipedia.org/wiki?curid=14045406 |
14045418 | Dihydrosanguinarine 10-monooxygenase | Class of enzymes
In enzymology, a dihydrosanguinarine 10-monooxygenase (EC 1.14.13.56) is an enzyme that catalyzes the chemical reaction
dihydrosanguinarine + NADPH + H+ + O2 formula_0 10-hydroxydihydrosanguinarine + NADP+ + H2O
The 4 substrates of this enzyme are dihydrosanguinarine, NADPH, H+, and O2, whereas its 3 products are 10-hydroxydihydrosanguinarine, 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 dihydrosanguinarine,NADPH:oxygen oxidoreductase (10-hydroxylating). This enzyme is also called dihydrosanguinarine 10-hydroxylase. This enzyme participates in alkaloid biosynthesis i.
References.
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| https://en.wikipedia.org/wiki?curid=14045418 |
14045447 | Ecdysone 20-monooxygenase | Enzyme
Ecdysone 20-monooxygenase (EC 1.14.99.22) is an enzyme that catalyzes the chemical reaction
ecdysone + AH2 + O2 formula_0 20-hydroxyecdysone + A + H2O
The three substrates of this enzyme are ecdysone, an electron acceptor AH2, and O2, whereas its three products are 20-hydroxyecdysone, 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 ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating). Like other genes in the ecdysone synthesis pathway, it belongs to Cytochrome P450 Halloween genes, with the nickname "shade", other names in common use include alpha-ecdysone C-20 hydroxylase, and ecdysone 20-hydroxylase.
References.
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| https://en.wikipedia.org/wiki?curid=14045447 |
14045456 | Estradiol 6beta-monooxygenase | In enzymology, an estradiol 6beta-monooxygenase (EC 1.14.99.11) is an enzyme that catalyzes the chemical reaction
estradiol-17beta + AH2 + O2 formula_0 6beta-hydroxyestradiol-17beta + A + H2O
The 3 substrates of this enzyme are estradiol-17beta, an electron acceptor AH2, and O2, whereas its 3 products are 6beta-hydroxyestradiol-17beta, 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 estradiol-17beta,hydrogen-donor:oxygen oxidoreductase (6beta-hydroxylating). This enzyme is also called estradiol 6beta-hydroxylase. This enzyme participates in androgen and estrogen metabolism.
References.
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| https://en.wikipedia.org/wiki?curid=14045456 |
14045474 | Flavanone 3-dioxygenase | Class of enzymes
In enzymology, a flavanone 3-dioxygenase (EC 1.14.11.9) is an enzyme that catalyzes the chemical reaction
a flavanone + 2-oxoglutarate + O2 formula_0 a dihydroflavonol + succinate + CO2
The 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 3 products are dihydroflavonol, 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 flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include naringenin 3-hydroxylase, flavanone 3-hydroxylase, flavanone 3beta-hydroxylase, flavanone synthase I, (2S)-flavanone 3-hydroxylase, and naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme participates in flavonoid biosynthesis. It has 2 cofactors: iron, and Ascorbate.
References.
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| https://en.wikipedia.org/wiki?curid=14045474 |
14045483 | Flavone synthase | In enzymology, a flavone synthase (EC 1.14.11.22) is an enzyme that catalyzes the chemical reaction
a flavanone + 2-oxoglutarate + O2 formula_0 a flavone + succinate + CO2 + H2O
The 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 4 products are flavone, succinate, CO2, 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 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating). This enzyme participates in flavonoid biosynthesis and isoflavonoid biosynthesis.
References.
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14045493 | Flavonoid 3'-monooxygenase | Class of enzymes
In enzymology, a flavonoid 3'-monooxygenase (EC 1.14.14.82, was wrongly classified as EC 1.14.13.21 in the past) is an enzyme that catalyzes the chemical reaction
a flavonoid + NADPH + H+ + O2 formula_0 a 3'-hydroxyflavonoid + NADP+ + H2O
The 4 substrates of this enzyme are flavonoid, NADPH, H+, and O2, whereas its 3 products are 3'-hydroxyflavonoid, 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 of oxygen into the other donor. The systematic name of this enzyme class is flavonoid,NADPH:oxygen oxidoreductase (3'-hydroxylating). Other names in common use include flavonoid 3'-hydroxylase, flavonoid 3-hydroxylase (erroneous), NADPH:flavonoid-3'-hydroxylase, and flavonoid 3-monooxygenase (erroneous). This enzyme participates in flavonoid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14045493 |
14045504 | Flavonol synthase | In enzymology, a flavonol synthase (EC 1.14.11.23) is an enzyme that catalyzes the following chemical reaction :
dihydroflavonol + 2-oxoglutarate + O2 formula_0 a flavonol + succinate + CO2 + H2O
The 3 substrates of this enzyme are dihydroflavonol, 2-oxoglutarate, and O2, whereas its 4 products are flavonol, succinate, CO2, 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 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. The systematic name of this enzyme class is dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in flavonoid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14045504 |
14045517 | Gamma-butyrobetaine dioxygenase | Protein-coding gene in the species Homo sapiens
Gamma-butyrobetaine dioxygenase (also known as BBOX, GBBH or γ-butyrobetaine hydroxylase) is an enzyme that in humans is encoded by the "BBOX1" gene. Gamma-butyrobetaine dioxygenase catalyses the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthesis pathway. Carnitine is essential for the transport of activated fatty acids across the mitochondrial membrane during mitochondrial beta oxidation. In humans, gamma-butyrobetaine dioxygenase can be found in the kidney (high), liver (moderate), and brain (very low). "BBOX1" has recently been identified as a potential cancer gene based on a large-scale microarray data analysis.
Reaction.
Gamma-butyrobetaine dioxygenase belongs to the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily. It catalyses the following reaction:
4-trimethylammoniobutanoate (γ-butyrobetaine) + 2-oxoglutarate + O2 formula_0 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine) + succinate + CO2
The three substrates of this enzyme are 4-trimethylammoniobutanoate (γ-butyrobetaine), 2-oxoglutarate, and O2, whereas its three products are 3-hydroxy-4-trimethylammoniobutanoate (L-carnitine), succinate, and carbon dioxide.
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 of oxygen into each donor. This enzyme participates in lysine degradation. Iron is a cofactor for gamma-butyrobetaine dioxygenase. Similar to many other 2OG oxygenases, the activity of gamma-butyrobetaine dioxygenase can be stimulated by reducing agents such as ascorbate and glutathione. The catalytic activity of gamma-butyrobetaine dioxygenase can be stimulated with different metal ions, especially potassium ions.
Both the "apo" (PDB id: 3N6W) and the "holo" (PDB id: 3O2G) structures of gamma-butyrobetaine dioxygenase have been solved, demonstrating an induced fit mechanism may contribute to the catalytic activity of gamma-butyrobetaine dioxygenase.
Gamma-butyrobetaine dioxygenase is promiscuous in substrate selectivity and it processes a number of modified substrates, including the natural catalytic products L-carnitine and D-carnitine, forming 3-dehydrocarnitine and trimethylaminoacetone. Gamma-butyrobetaine dioxygenase also catalyses the oxidation of mildronate to form multiple products including malonic acid semialdehyde, dimethylamine, formaldehyde and (1-methylimidazolidin-4-yl)acetic acid, which is proposed to be formed via a Stevens rearrangement mechanism. Gamma-butyrobetaine dioxygenase is unique among other human 2OG oxygenases that it catalyses both hydroxylation (e.g.: L-carnitine), demethylation (e.g.: formaldehyde) and C-C bond formation (e.g.: (1-methylimidazolidin-4-yl)acetic acid).
Inhibition.
Gamma-butyrobetaine dioxygenase is an inhibition target for 3-(2,2,2-trimethylhydraziniumyl)propionate (mildronate, also known as THP, MET-88, Meldonium or Quarterine). Mildronate is offered, clinically, to non-U.S. markets, in treatment of angina and myocardial infarction. Some studies suggested that mildronate may also be beneficial for the treatment of neurological disorder, diabetes, and seizures and alcohol intoxication. Mildronate is currently manufactured and marketed by Grindeks, a pharmaceutical company based in Latvia. To date, at least five clinical trial reports were published in peer-reviewed journals documenting the efficacy and safety of mildronate on the treatments of angina, stroke and chronic heart failure. However, there have been no randomized clinical trials to support the use of mildronate to treat any cardiovascular disease.
Mildronate has a similar structure to the natural substrate gamma-butyrobetaine, with a NH group replacing the CH2 of gamma-butyrobetaine at the C-4 position. A crystal structure of mldronate in complex with gamma-butyrobetaine dioxygenase was published, and it suggests mildronate bind to gamma-butyrobetaine dioxygenase in exactly the same way as gamma-butyrobetaine (PDB id: 3MS5). To date, most enzyme inhibitors for human 2OG oxygenases bind to the cosubstrate 2OG binding site; mildronate is a rare example of a non-peptidyl substrate mimic inhibitor. Although initial reports suggested mildronate is a non-competitive and non-hydroxylatable analogue of gamma-butyrobetaine, further studies have identified mildronate is indeed a substrate for gamma-butyrobetaine dioxygenase.
Similar to other 2OG oxygenases, gamma-butyrobetaine dioxygenase can be inhibited by 2OG mimics and aromatic inhibitors such as pyridine 2,4-dicarboxylate. Other reported gamma-butyrobetaine dioxygenase inhibitors include cyclopropyl-substituted gamma-butyrobetaines and 3-(2,2-dimethylcyclopropyl)propanoic acid, which is a mechanism-based enzyme inhibitor.
Assay.
Several "in vitro" biochemical assays have been applied to monitor the catalytic activity of gamma-butyrobetaine dioxygenase. Early methods have mainly focused on the use of radiolabeled compounds, including 14C-labelled gamma-butyrobetaine and 14C-labelled 2OG. Enzyme-coupled method have also been applied to detect carnitine formation, by using the enzyme carnitine acetyltransferase and 14C-labelled acetyl-coenzyme A to give labelled acetylcarnitine for detection. Using this method, it is possible to detect carnitine concentration down to the pico-molar range. Other analytical methods including mass spectrometry and NMR have also been applied, and they are in particularly useful for the study of the coupling ratio between 2OG oxidation and substrate formation, and for the characterisation of unknown enzymatic products. However, these methods are often not suitable for high-throughput screening and require expensive instrumentation. A potentially high-throughput fluorescence-based assay has also been proposed by using a fluorinated-gamma-butyrobetaine analog. The fluoride ions released as a result of gamma-butyrobetaine dioxygenase catalyses can be detected by using chemosensors such as protected fluorescein.
References.
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Further reading.
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14045530 | Gibberellin 2beta-dioxygenase | In enzymology, a gibberellin 2beta-dioxygenase (EC 1.14.11.13) is an enzyme that catalyzes the chemical reaction
gibberellin 1 + 2-oxoglutarate + O2 formula_0 2beta-hydroxygibberellin 1 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 1, 2-oxoglutarate, and O2, whereas its 3 products are 2beta-hydroxygibberellin 1, 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 (gibberellin-1),2-oxoglutarate:oxygen oxidoreductase (2beta-hydroxylating). This enzyme is also called gibberellin 2beta-hydroxylase. This enzyme participates in diterpenoid biosynthesis.
References.
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14045542 | Gibberellin 3beta-dioxygenase | In enzymology, a gibberellin 3beta-dioxygenase (EC 1.14.11.15) is an enzyme that catalyzes the chemical reaction
gibberellin 20 + 2-oxoglutarate + O2 formula_0 gibberellin 1 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 20, 2-oxoglutarate, and O2, whereas its 3 products are gibberellin 1, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as the oxidant. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and one atom of oxygen is incorporated into each donor. The systematic name of this enzyme class is (gibberellin-20), 2-oxoglutarate: oxygen oxidoreductase (3beta-hydroxylating). Other names in common use include gibberellin 3beta-hydroxylase, (gibberrellin-20), 2-oxoglutarate: oxygen oxidoreductase and (3beta-hydroxylating). This enzyme participates in diterpenoid biosynthesis. It has 2 cofactors: iron and Ascorbate.
References.
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| https://en.wikipedia.org/wiki?curid=14045542 |
14045554 | Gibberellin-44 dioxygenase | In enzymology, a gibberellin-44 dioxygenase (EC 1.14.11.12) is an enzyme that catalyzes the chemical reaction
gibberellin 44 + 2-oxoglutarate + O2 formula_0 gibberellin 19 + succinate + CO2
The 3 substrates of this enzyme are gibberellin 44, 2-oxoglutarate, and O2, whereas its 3 products are gibberellin 19, 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 (gibberellin-44),2-oxoglutarate:oxygen oxidoreductase. Other names in common use include oxygenase, gibberellin A44 oxidase, and (gibberellin-44), 2-oxoglutarate:oxygen oxidoreductase. This enzyme participates in diterpenoid biosynthesis. It employs one cofactor, iron.
References.
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14045571 | Glyceollin synthase | Class of enzymes
In enzymology, glyceollin synthase is an enzyme that catalyzes the last committed step in glyceollin biosynthesis. This enzyme has been classified as a cytochrome dependent monooxygenase. It uses cyclization of prenyl residue to convert glyceollidins (I and II) into glyceollins (I - III).
This enzyme catalyzes the following chemical reaction:
2-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADPH + H+ + O2 formula_0 glyceollin + NADP+ + 2 H2O
The five substrates of this enzyme are 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADPH, H+, and O2, whereas its three products are glyceollin, 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-(or 4-)dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan,NADPH:oxygen oxidoreductase (cyclizing). This enzyme participates in isoflavonoid biosynthesis.
References.
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14045585 | Alkylglycerol monooxygenase | Class of enzymes
Alkylglycerol monooxygenase (AGMO) (EC 1.14.16.5) is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7.
In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.
The reaction catalyzed by alkylglycerol monooxygenase:
The unstable intermediate product 1-hydroxyalkyl-sn-glycerol rearranges into the fatty aldehyde and the free glycerol derivative. The fatty aldehyde is then further oxidized to the corresponding acid by fatty aldehyde dehydrogenase.
Alkylglycerol monooxygenase is a membrane-bound mixed-function oxidase and harbours a fatty acid hydroxylase motif. The iron is believed to be coordinated by a diiron center composed of eight histidines, which can be found in all enzymes containing this motif.
Nomenclature.
The systematic name for this enzyme is 1-alkyl-sn-glycerol,tetrahydrobiopterin:oxygen oxidoreductase. Other names in use are glyceryl-ether monooxygenase, glyceryl-ether cleaving enzyme, glyceryl ether oxygenase, glyceryl etherase, and O-alkylglycerol monooxygenase.
References.
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Further reading.
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14045596 | Hydroxyphenylacetonitrile 2-monooxygenase | Class of enzymes
In enzymology, a hydroxyphenylacetonitrile 2-monooxygenase (EC 1.14.13.42) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetonitrile + NADPH + H+ + O2 formula_0 4-hydroxymandelonitrile + NADP+ + H2O
The 4 substrates of this enzyme are 4-hydroxyphenylacetonitrile, NADPH, H+, and O2, whereas its 3 products are 4-hydroxymandelonitrile, 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 4-hydroxyphenylacetonitrile,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 4-hydroxyphenylacetonitrile monooxygenase, and 4-hydroxyphenylacetonitrile hydroxylase. It employs one cofactor, heme.
References.
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| https://en.wikipedia.org/wiki?curid=14045596 |
14045605 | Hyoscyamine (6S)-dioxygenase | In enzymology, a hyoscyamine (6S)-dioxygenase (EC 1.14.11.11) is an enzyme that catalyzes the chemical reaction
L-hyoscyamine + 2-oxoglutarate + O2 formula_0 (6S)-hydroxyhyoscyamine + succinate + CO2
The 3 substrates of this enzyme are L-hyoscyamine, 2-oxoglutarate, and O2, whereas its 3 products are (6S)-hydroxyhyoscyamine, 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 L-hyoscyamine,2-oxoglutarate:oxygen oxidoreductase ((6S)-hydroxylating). Other names in common use include hyoscyamine 6beta-hydroxylase, hyoscyamine 6beta-dioxygenase, and hyoscyamine 6-hydroxylase. This enzyme participates in alkaloid biosynthesis ii. It has 2 cofactors: iron, and Ascorbate.
References.
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| https://en.wikipedia.org/wiki?curid=14045605 |
14045613 | Imidazoleacetate 4-monooxygenase | Class of enzymes
In enzymology, an imidazoleacetate 4-monooxygenase (EC 1.14.13.5) is an enzyme that catalyzes the chemical reaction
4-imidazoleacetate + NADH + H+ + O2 formula_0 5-hydroxy-4-imidazoleacetate + NAD+ + H2O
The 4 substrates of this enzyme are 4-imidazoleacetate, NADH, H+, and O2, whereas its 3 products are 5-hydroxy-4-imidazoleacetate, 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 4-imidazoleacetate,NADH:oxygen oxidoreductase (5-hydroxylating). Other names in common use include imidazoleacetic hydroxylase, imidazoleacetate hydroxylase, and imidazoleacetic monooxygenase. This enzyme participates in histidine metabolism. It employs one cofactor, FAD.
References.
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| https://en.wikipedia.org/wiki?curid=14045613 |
14045619 | Isoflavone 2'-hydroxylase | In enzymology, an isoflavone 2'-hydroxylase (EC 1.14.14.90, Formerly EC 1.14.13.89) is an enzyme that catalyzes the chemical reaction
an isoflavone + NADPH + H+ + O2 formula_0 a 2'-hydroxyisoflavone + NADP+ + H2O
The 4 substrates of this enzyme are isoflavone, NADPH, H+, and O2, whereas its 3 products are 2'-hydroxyisoflavone, 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 isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase, CYP81E1, and CYP Ge-3. This enzyme participates in isoflavonoid biosynthesis.
References.
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| https://en.wikipedia.org/wiki?curid=14045619 |
14045632 | Isoflavone 3'-hydroxylase | In enzymology, an isoflavone 3'-hydroxylase (EC 1.14.14.88, Formerly EC 1.14.13.52) is an enzyme that catalyzes the chemical reaction
formononetin + NADPH + H+ + O2 formula_0 calycosin + NADP+ + H2O
The 4 substrates of this enzyme are formononetin, NADPH, H+, and O2, whereas its 3 products are calycosin, 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 formononetin,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called isoflavone 3'-monooxygenase. This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References.
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| https://en.wikipedia.org/wiki?curid=14045632 |
14045649 | Juglone 3-monooxygenase | In enzymology, juglone 3-monooxygenase (EC 1.14.99.27) is an enzyme that catalyzes the chemical reaction
5-hydroxy-1,4-naphthoquinone + AH2 + O2 formula_0 3,5-dihydroxy-1,4-naphthoquinone + A + H2O
The 3 substrates of this enzyme are 5-hydroxy-1,4-naphthoquinone, AH2, and O2, whereas its 3 products are 3,5-dihydroxy-1,4-naphthoquinone, 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 derived from O miscellaneous. The systematic name of this enzyme class is 5-hydroxy-1,4-naphthoquinone,hydrogen-donor:oxygen oxidoreductase (3-hydroxylating). Other names in common use include juglone hydroxylase, naphthoquinone hydroxylase, and naphthoquinone-hydroxylase.
References.
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| https://en.wikipedia.org/wiki?curid=14045649 |
14045673 | Kynurenine 7,8-hydroxylase | In enzymology, a kynurenine 7,8-hydroxylase (EC 1.14.99.2) is an enzyme that catalyzes the chemical reaction
kynurenate + AH2 + O2 formula_0 7,8-dihydro-7,8-dihydroxykynurenate + A
The 3 substrates of this enzyme are kynurenate, an electron acceptor AH2, and O2, whereas its two products are 7,8-dihydro-7,8-dihydroxykynurenate and the reduction product A.
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 kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating). Other names in common use include kynurenic acid hydroxylase, kynurenic hydroxylase, and kynurenate 7,8-hydroxylase. This enzyme participates in tryptophan metabolism.
References.
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| https://en.wikipedia.org/wiki?curid=14045673 |
14045697 | Latia-luciferin monooxygenase (demethylating) | In enzymology, a Latia-luciferin monooxygenase (demethylating) (EC 1.14.99.21) is an enzyme that catalyzes the chemical reaction
Latia luciferin + AH2 + 2 O2 formula_0 oxidized Latia luciferin + CO2 + formate + A + H2O + hnu
The 3 substrates of this enzyme are Latia luciferin, an electron acceptor AH2, and O2, whereas its 6 products are oxidized Latia luciferin, CO2, formate, the reduction product A, H2O, and hn.
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 Latia-luciferin,hydrogen-donor:oxygen oxidoreductase (demethylating). Other names in common use include luciferase (Latia luciferin), and Latia luciferin monooxygenase (demethylating). It has 2 cofactors: FAD, and Flavoprotein.
References.
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| https://en.wikipedia.org/wiki?curid=14045697 |
14045706 | Leucocyanidin oxygenase | In enzymology, a leucocyanidin oxygenase (EC 1.14.11.19) is an enzyme that catalyzes the chemical reaction
leucocyanidin + 2-oxoglutarate + O2 formula_0 cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O
The 3 substrates of this enzyme are leucocyanidin, 2-oxoglutarate, and O2, whereas its 5 products are cis-dihydroquercetin, trans-dihydroquercetin, succinate, CO2, 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 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is leucocyanidin,2-oxoglutarate:oxygen oxidoreductase. This enzyme is also called leucoanthocyanidin dioxygenase (LDOX) or anthocyanidin synthase (ANS). This enzyme participates in flavonoid biosynthesis.
In a broader way, leucocyanidin oxygenase uses flavan-3,4-diols (leucoanthocyanidins) to produce 3-hydroxyanthocyanidins. The gene encoding the enzyme (PpLDOX) has been identified in peach and expression has been studied in "Vitis vinifera".
Structural studies.
As of late 2007, only one structure, in "Arabidopsis thaliana", has been solved for this class of enzymes, with the PDB accession code 2BRT.
References.
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Further reading.
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14045716 | Leukotriene-B4 20-monooxygenase | Class of enzymes
In enzymology, a leukotriene-B4 20-monooxygenase (EC 1.14.13.30) is an enzyme that catalyzes the chemical reaction
(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 formula_0 (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O
The 4 substrates of this enzyme are (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate, NADPH, H+, and O2, whereas its 4 products are (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-, tetraenoate, 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 (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,N ADPH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include leukotriene-B4 20-hydroxylase, leucotriene-B4 omega-hydroxylase, LTB4 20-hydroxylase, and LTB4 omega-hydroxylase. This enzyme participates in arachidonic acid metabolism. It employs one cofactor, heme.
References.
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14045724 | Leukotriene-E4 20-monooxygenase | Class of enzymes
In enzymology, a leukotriene-E4 20-monooxygenase (EC 1.14.13.34) is an enzyme that catalyzes the chemical reaction
(7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14- tetraenoate + NADPH + H+ + O2 formula_0 20-hydroxyleukotriene E4 + NADP+ + H2O
The 5 substrates of this enzyme are (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-, tetraenoate, NADPH, H+, and O2, whereas its 3 products are 20-hydroxyleukotriene E4, 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 (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14-te traenoate,NADPH:oxygen oxidoreductase (20-hydroxylating). This enzyme is also called leukotriene-E4 omega-hydroxylase. This enzyme participates in arachidonic acid metabolism.
References.
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14045729 | Licodione synthase | Class of enzymes
In enzymology, a licodione synthase (EC 1.14.13.87) is an enzyme that catalyzes the chemical reaction
liquiritigenin + NADPH + H+ + O2 formula_0 licodione + NADP+ + H2O
The 4 substrates of this enzyme are liquiritigenin, NADPH, H+, and O2, whereas its 3 products are licodione, 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 liquiritigenin,NADPH:oxygen oxidoreductase (licodione-forming).
References.
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14045738 | Linalool 8-monooxygenase | In enzymology, a linalool 8-monooxygenase (EC 1.14.14.84, Formerly EC 1.14.13.151) is an enzyme that catalyzes the chemical reaction
3,7-dimethylocta-1,6-dien-3-ol + AH2 + O2 formula_0 (E)-3,7-dimethylocta-1,6-dien-3,8-diol + A + H2O
The 3 substrates of this enzyme are 3,7-dimethylocta-1,6-dien-3-ol, an electron acceptor AH2, and O2, whereas its 3 products are (E)-3,7-dimethylocta-1,6-diene-3,8-diol, 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 3,7-dimethylocta-1,6-dien-3-ol,hydrogen-donor:oxygen oxidoreductase (8-hydroxylating). It employs one cofactor, heme.
References.
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14045748 | Linoleoyl-CoA desaturase | Class of enzymes
Linoleoyl-CoA desaturase (also Delta 6 desaturase, EC 1.14.19.3) is an enzyme that converts between types of fatty acids, which are essential nutrients in the human body. The enzyme mainly catalyzes the chemical reaction
linoleoyl-CoA + AH2 + O2 formula_0 gamma-linolenoyl-CoA + A + 2 H2O
The three substrates of this enzyme are linoleoyl-CoA, an electron acceptor AH2, and O2, whereas its three products are gamma-linolenoyl-CoA, 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 derived from O2 with oxidation of a pair of donors resulting in the reduction of O to two molecules of water. The systematic name of this enzyme class is linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase. Other names in common use include acyl-CoA 6-desaturase, Delta6-desaturase (D6D or Δ-6-desaturase), Delta6-fatty acyl-CoA desaturase, Delta6-acyl CoA desaturase, fatty acid Delta6-desaturase, fatty acid 6-desaturase, linoleate desaturase, linoleic desaturase, linoleic acid desaturase, linoleoyl CoA desaturase, linoleoyl-coenzyme A desaturase, and long-chain fatty acid Delta6-desaturase. This enzyme participates in linoleic acid metabolism. It employs one cofactor, iron.
The enzyme is molecularly identical across all living things. It is present in animals, plants, fungi, and cyanobacteria.
D6D is one of the three fatty acid desaturases present in humans along with Δ-5 and Δ-9, named so because it was thought to desaturate bond between carbons 6 and 7, counting from carboxyl group (with the carboxyl group carbon numbered one). The number 6 in the name of the enzyme has nothing to do with omega-6 fatty acids. In humans, D6D is encoded by the FADS2 gene.
Function.
D6D is a desaturase enzyme, i.e. it introduces a double bond in a specific position of long-chain fatty acids. D6D is necessary to synthesize longer chain omega-3 and omega-6 fatty acids. In humans, it is used principally for the conversions of cis-linoleic acid to gamma-linolenic acid (GLA), and palmitic acid to sapienic acid. It also converts alpha-linolenic acid (ALA) to stearidonic acid and tetracosatetraenoic acid to tetracosapentaenoic acid, intermediate steps in the synthesis of ALA to EPA and of EPA to DHA, respectively.
Separately from its function in synthesizing EPA and DHA, D6D plays a contributory role in fatty acid re-esterification, required for the return of unoxidized free fatty acids into white adipose tissue as triglycerides.
Agonists and inhibiting factors.
D6D is upregulated by estrogen, low levels of omega-3s, and moderate food restriction (up to 300%) .
D6D activity slows with age, suggested by reductions in GLA and subsequent metabolites. Other inhibiting factors include alcohol, radiation, and diabetes .
The conversion rate of ALA into DHA is vulnerable to suppression by dietary fatty acids. ALA intake greater than 1% and total polyunsaturated intake above 3% were found to drastically limit synthesis of EPA and DHA.
Clinical significance.
D6D deficiency can result in deficiencies in DHA, and in GLA and its metabolites dihomo-gamma-linolenic acid (DGLA) and prostaglandin E1 (PGE1). It is implicated in abnormal sperm production due to deficiency in DHA and atopic dermatitis due to deficiencies in GLA and PGE1.
"Toxoplasma gondii".
Felines lack D6D activity in their guts and accumulate systemic linoleic acid. This increase in linoleic acid in cats has an influence in causing the sexual cycle of "T. gondii" to be restricted to felines, with linoleic acid stimulating "T. gondii" sexual reproduction.
References.
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14045752 | Lithocholate 6beta-hydroxylase | Class of enzymes
In enzymology, a lithocholate 6beta-hydroxylase (EC 1.14.13.94) is an enzyme that catalyzes the chemical reaction
lithocholate + NADPH + H+ + O2 formula_0 6beta-hydroxylithocholate + NADP+ + H2O
The 4 substrates of this enzyme are lithocholate, NADPH, H+, and O2, whereas its 3 products are 6beta-hydroxylithocholate, 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 lithocholate,NADPH:oxygen oxidoreductase (6beta-hydroxylating). Other names in common use include lithocholate 6beta-monooxygenase, CYP3A10, 6beta-hydroxylase, and cytochrome P450 3A10/lithocholic acid 6beta-hydroxylase.
References.
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14045763 | L-lysine 6-monooxygenase (NADPH) | Class of enzymes
In enzymology, a L-lysine 6-monooxygenase (NADPH) (EC 1.14.13.59) is an enzyme that catalyzes the chemical reaction
L-lysine + NADPH + H+ + O2 formula_0 N6-hydroxy-L-lysine + NADP+ + H2O
The 4 substrates of this enzyme are L-lysine, NADPH, H+, and O2, whereas its 3 products are N6-hydroxy-L-lysine, 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 L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called lysine N6-hydroxylase. This enzyme participates in lysine degradation.
References.
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14045776 | Mandelate 4-monooxygenase | Class of enzymes
In enzymology, a mandelate 4-monooxygenase (EC 1.14.16.6) is an enzyme that catalyzes the chemical reaction
(S)-2-hydroxy-2-phenylacetate + tetrahydrobiopterin + O2 formula_0 (S)-4-hydroxymandelate + dihydrobiopterin + H2O
The 3 substrates of this enzyme are (S)-2-hydroxy-2-phenylacetate, tetrahydrobiopterin, and O2, whereas its 3 products are (S)-4-hydroxymandelate, dihydrobiopterin, 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 reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating). Other names in common use include L-mandelate 4-hydroxylase, and mandelic acid 4-hydroxylase. It employs one cofactor, iron.
References.
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14045787 | Melilotate 3-monooxygenase | Class of enzymes
In enzymology, a melilotate 3-monooxygenase (EC 1.14.13.4) is an enzyme that catalyzes the chemical reaction
3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 formula_0 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
The 4 substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate, NADH, H+, and O2, whereas its 3 products are 3-(2,3-dihydroxyphenyl)propanoate, 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-(2-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 2-hydroxyphenylpropionate hydroxylase, melilotate hydroxylase, 2-hydroxyphenylpropionic hydroxylase, and melilotic hydroxylase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, FAD.
References.
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14045797 | (−)-menthol monooxygenase | Class of enzymes
In enzymology, a (−)-menthol monooxygenase (EC 1.14.13.46) is an enzyme that catalyzes the chemical reaction
(−)-menthol + NADPH + H+ + O2 formula_0 p-menthane-3,8-diol + NADP+ + H2O
The 4 substrates of this enzyme are (−)-menthol, NADPH, H+, and O2, whereas its 3 products are p-menthane-3,8-diol, 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 (−)-menthol,NADPH:oxygen oxidoreductase (8-hydroxylating). This enzyme is also called l-menthol monooxygenase.
Uses.
Use of (−)-menthol monooxygenase has been explored by several companies including Procter & Gamble for cleaning products.
References.
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14045800 | Methyltetrahydroprotoberberine 14-monooxygenase | Class of enzymes
In enzymology, a methyltetrahydroprotoberberine 14-monooxygenase (EC 1.14.13.37) is an enzyme that catalyzes the chemical reaction
(S)-N-methylcanadine + NADPH + H+ + O2 formula_0 allocryptopine + NADP+ + H2O
The 4 substrates of this enzyme are (S)-N-methylcanadine, NADPH, H+, and O2, whereas its 3 products are allocryptopine, 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 (S)-N-methylcanadine,NADPH:oxygen oxidoreductase (14-hydroxylating). Other names in common use include methyltetrahydroprotoberberine 14-hydroxylase, (S)-cis-N-methyltetrahydroberberine 14-monooxygenase, and (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, heme.
References.
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14045808 | Monoprenyl isoflavone epoxidase | Class of enzymes
In enzymology, a monoprenyl isoflavone epoxidase (EC 1.14.99.34) is an enzyme that catalyzes the chemical reaction
7-O-methylluteone + NADPH + H+ + O2 formula_0 dihydrofurano derivatives + NADP+ + H2O
The 4 substrates of this enzyme are 7-O-methylluteone, NADPH, H+, and O2, whereas its 3 products are dihydrofurano pyranoisoflavone derivative, 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 derive from O miscellaneous. The systematic name of this enzyme class is 7-O-methylluteone,NADPH:O2 oxidoreductase. Other names in common use include monoprenyl isoflavone monooxygenase, and 7-O-methylluteone:O2 oxidoreductase.
References.
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| https://en.wikipedia.org/wiki?curid=14045808 |
14045816 | Myristoyl-CoA 11-(E) desaturase | In enzymology, a myristoyl-CoA 11-(E) desaturase (EC 1.14.99.31) is an enzyme that catalyzes the chemical reaction
myristoyl-CoA + NAD(P)H + H+ + O2 formula_0 (E)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
The 5 substrates of this enzyme are myristoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are (E)-11-tetradecenoyl-CoA, NAD+, 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 O miscellaneous. The systematic name of this enzyme class is n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(E) desaturating].
References.
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14045826 | Myristoyl-CoA 11-(Z) desaturase | In enzymology, a myristoyl-CoA 11-(Z) desaturase (EC 1.14.99.32) is an enzyme that catalyzes the chemical reaction
myristoyl-CoA + NAD(P)H + H+ + O2 formula_0 (Z)-11-tetradecenoyl-CoA + NAD(P)+ + 2 H2O
The 5 substrates of this enzyme are myristoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are (Z)-11-tetradecenoyl-CoA, NAD+, 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 derive from O miscellaneous. The systematic name of this enzyme class is n-tetradecanoyl-CoA,NAD(P)H:O2 oxidoreductase [11-(Z) desaturating]. This enzyme is also called n-tetradecanoyl-CoA,NADPH:O2 oxidoreductase [11-(Z) desaturating].
References.
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| https://en.wikipedia.org/wiki?curid=14045826 |
14045836 | Naphthalene 1,2-dioxygenase | Class of enzymes
In enzymology, a naphthalene 1,2-dioxygenase (EC 1.14.12.12) is an enzyme that catalyzes the chemical reaction
naphthalene + NADH + H+ + O2 formula_0 (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
The 4 substrates of this enzyme are naphthalene, NADH, H+, and O2, whereas its two products are (1R,2S)-1,2-dihydronaphthalene-1,2-diol 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 naphthalene,NADH:oxygen oxidoreductase (1,2-hydroxylating). Other names in common use include naphthalene dioxygenase, and naphthalene oxygenase. This enzyme participates in 4 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, fluorene degradation, and ethylbenzene degradation. It employs one cofactor, iron.
Structural studies.
As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes 1EG9, 1NDO, 1O7G, 1O7H, 1O7M, 1O7N, 1O7P, 1O7W, 1UUV, 1UUW, 2B1X, 2B24, 2HMJ, 2HMK, 2HML, 2HMM, 2HMN, and 2HMO.
References.
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14045844 | Nitric oxide dioxygenase | Nitric oxide dioxygenase (EC 1.14.12.17) is an enzyme that catalyzes the conversion of nitric oxide (NO) to nitrate (NO)
. The net reaction for the reaction catalyzed by nitric oxide dioxygenase is shown below:
Nitric oxide is a ubiquitous small molecule that is integrated in a wide variety of physiological processes including smooth muscle vasodilation, platelet disaggregation, neurotransmission, and immune response to bacterial infection. Overproduction of this signaling molecule can be lethal to cells by poisoning cellular energy production. The most sensitive targets of NO are aconitase, an enzyme that catalyzes the isomerization of citrate to isocitrate in the citric acid cycle, and cytochrome oxidase, the last enzyme in the respiratory electron transport chain of mitochondria. Additionally NO, with its lone radical on the nitrogen atom, is implicated in a number of secondary mechanisms of toxicity, including catalase inhibition (resulting in hydrogen peroxide toxicity), Fe-S center iron liberation, and the formation of dinitosyl-iron complexes.
Due to the potential lethality of NO, cells benefitted greatly from the evolution of an enzyme capable of catalyzing the conversion of toxic NO to nitrate.
A 'nitric oxide dioxygenase' is an enzyme that is capable of carrying out this reaction. NO dioxygenase belongs to the family of oxidoreductases, more specifically those acting on paired donors, with O2 as oxidant and with incorporation of two atoms of oxygen into the other donor.
Reaction mechanism.
The mechanism of action has still not been entirely deduced, however, the leading theory suggests that the conversion is carried out through a series of redox reactions involving iron centers as shown in the series of half reactions below:
Another theory developed more recently (2009) suggests that a NO dioxygenase activity could also proceed through phenolic nitration via a putative heme-peroxynitrite intermediate.
The most well studied NO dioxygenase is flavohemoglobin (flavoHb), shown to the right:
Studies have shown that flavohemoglobins are induced by NO, nitrite, nitrate, and NO-releasing agents in various bacteria and fungi. Additionally, flavoHbs have been shown to protect bacteria, yeast, and Dictyostelium discoideum against growth inhibition and damage mediated via NO.
Discovery.
Nitric oxide dioxygenase was discovered, and first reported in 1998, as an inducible O2-dependent enzymatic activity that protected bacteria against nitric oxide toxicity. The enzyme was identified with the "E. coli" flavohemoglobin.
More recently, another protein has been identified as a NO dioxygenase - rhodobacter sphaeroides haem protein (SHP), a novel cytochrome with NO dioxygenase activity. Although the biological function of SHP has yet to be identified, SHP has been shown, that with oxygen bound, it can react rapidly with nitric oxide to form nitrate.
Structure and molecular function.
The flavohemoglobin protein contains two domains: an oxidoreductase FAD-binding domain, and a "b"-type heme-containing "globin" domain and optionally an oxidoreductase NAD-binding domain. The reductase domain supplies an electron to the heme iron to achieve a high rate of catalytic NO dioxygenation.
In addition to numerous flavohemoglobins, many distantly related members of the hemoglobin superfamily including the muscle myoglobin, the non-symbiotic plant hemoglobin and symbiotic plant leghemoglobin, the neuronal neuroglobin, and the mammalian cytoplasmic cytoglobin appear to function as nitric oxide dioxygenases (NODs), although the cellular electron donor(s) for many globins have yet to be defined. Electron donors may include ascorbate, cytochrome b5 or ferredoxin reductase. The catalytic NO dioxygenation can be written in its simplest form:
NO + O2 + e− formula_0 NO3−
Catalysis is very efficient. The reported bimolecular NO dioxygenation rate constants range from 2 x 107 M−1s−1 for cytoglobin to 3 x 109 M−1s−1 for flavohemoglobin, and turnover rates range from 1 to 700 s−1. Structure, O2 binding, and reduction of globins appear optimized for a NO dioxygenase function.
Physiological function.
Historically, nitric oxide dioxygenase (around 1.8 billion years ago) served to provide the modern day analogue of hemoglobin/myoglobin function for oxygen storage and transport. Gardner et al. (1998) suggested that the first hemoglobin/myoglobin probably functioned as an enzyme utilizing bound ‘activated’ oxygen gas to dioxygenate NO in microbes.
The wide diversity of multicellular organisms benefitting from the oxygen storage and transport functions of myoglobin/hemoglobin appeared much later (approximately 0.5 billion years ago).
NODs are now known to serve two important physiological functions in diverse life forms: they prevent NO toxicity (otherwise known as "nitrosative stress") and regulate NO signalling. NODs belong to the larger family of well-established free radical and reactive oxygen detoxifying enzymes that includes superoxide dismutase, catalase, and peroxidase.
Distribution in nature.
NODs, as well as many hemoglobins that function as NODs, are distributed to most life forms including bacteria, fungi, protists, worms, plants and animals. In fact, nitric oxide dioxygenation appears to be a primal function for members of the hemoglobin superfamily. Moreover, it is becoming increasingly evident that the NOD function of globins is much more common than the paradigmatic O2 transport-storage function of red cell hemoglobin which was first investigated and reported over a century earlier by Felix Hoppe-Seyler and others. Other proteins that may act as NODs include mammalian microsomal cytochrome P450(s) and a novel O2-binding cytochrome "b" from "Rhodobacter sphaeroides".
Technologies.
Inhibitors of the NODs are being developed for application as microbial antibiotics, anti-tumor agents and modulators of NO signalling. The most prominent class of inhibitor of NO dioxygenase to date is imidazole antibiotics. Imidazoles have been shown to coordinate with the heme iron atom of microbial flavohemoglobin, impair ferric heme reduction, produce uncompetitive inhibition with respect to O2 and NO, and inhibit NO metabolism by yeasts and bacteria. Specifically, imidazoles bearing bulky aromatic substituents have been shown to have potential for selective and high-affinity inhibition of NO dioxygenase function by coordinating the catalytic heme iron and "fitting" within the large hydrophobic distal heme pocket. As a result, imidazole engineering has been suggested as a means to specifically inhibit NO dioxygenases.
In addition, genetically modified plants with heterologous flavohemoglobin-NODs are being developed to limit NO toxicity created by metabolism of nitrogen fertilizers by soil microbes and as a means towards plant self-fertilization through absorption of environmental NO.
Recently a lentiviral vector that allows for expression of "E. coli" flavoHb in mammalian cells has been described. This approach demonstrated that flavoHb is indeed enzymatically active within human and murine cells and potently blocks exogenous and endogenous sources of nitrosative stress. This technology was then extended to interrogate the role of NO synthesis in the highly tumorigenic cancer stem cells (CSCs) from human glioblastoma (brain tumor) samples. Expression of flavoHb within xenografted tumors led to depletion of NO generated by iNOS/NOS2. The phenotypic result was loss of tumorigenicity of the CSCs and improved mouse survival. These experiments demonstrate that flavoHb can be employed for "in vivo" studies of nitric oxide biology and suggest that therapeutic NO-depletion may be achieved via heterologous expression of bacterial flavoHbs.
References.
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14045853 | N-methylcoclaurine 3'-monooxygenase | Class of enzymes
In enzymology, a N-methylcoclaurine 3'-monooxygenase (EC 1.14.13.71) is an enzyme that catalyzes the chemical reaction
(S)-N-methylcoclaurine + NADPH + H+ + O2 formula_0 (S)-3'-hydroxy-N-methylcoclaurine + NADP+ + H2O
The 4 substrates of this enzyme are (S)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are (S)-3'-hydroxy-N-methylcoclaurine, 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 of oxygen into the other donor. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called N-methylcoclaurine 3'-hydroxylase and CYP80B1.
References.
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14045860 | Orcinol 2-monooxygenase | Class of enzymes
In enzymology, an orcinol 2-monooxygenase (EC 1.14.13.6) is an enzyme that catalyzes the chemical reaction
orcinol + NADH + H+ + O2 formula_0 2,3,5-trihydroxytoluene + NAD+ + H2O
The 4 substrates of this enzyme are orcinol, NADH, H+, and O2, whereas its 3 products are 2,3,5-trihydroxytoluene, 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 orcinol,NADH:oxygen oxidoreductase (2-hydroxylating). This enzyme is also called orcinol hydroxylase. It employs one cofactor, FAD.
References.
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14045874 | Peptide-aspartate beta-dioxygenase | In enzymology, a peptide-aspartate beta-dioxygenase (EC 1.14.11.16), a member of the alpha-ketoglutarate-dependent hydroxylases superfamily, is an enzyme that catalyzes the chemical reaction
peptide-L-aspartate + 2-oxoglutarate + O2 formula_0 peptide-3-hydroxy-L-aspartate + succinate + CO2
The 3 substrates of this enzyme are peptide-L-aspartate, 2-oxoglutarate, and O2, whereas its 3 products are peptide-3-hydroxy-L-aspartate, succinate, and CO2.
It employs one cofactor, iron.
Nomenclature.
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 peptide-L-aspartate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). Other names in common use include aspartate beta-hydroxylase, and aspartylpeptide beta-dioxygenase.
References.
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Further reading section.
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| https://en.wikipedia.org/wiki?curid=14045874 |
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