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https://en.wikipedia.org/wiki/Bilirubin%20oxidase | In enzymology, a bilirubin oxidase, BOD or BOx, () is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction
2 bilirubin + O2 2 biliverdin + 2 H2O
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism. It is widely studied as a catalyst for oxygen reduction.
Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank (accession codes and ).
The active site consists of four copper centers, reminiscent of laccase. These centers are classified as type I (cys, met, his, his), type II (3his), and two type III (2his).
Further reading
References
EC 1.3.3
Copper enzymes |
https://en.wikipedia.org/wiki/Biochanin-A%20reductase | In enzymology, a biochanin-A reductase () is an enzyme that catalyzes the chemical reaction
dihydrobiochanin A + NADP+ biochanin A + NADPH + H+
Thus, the two substrates of this enzyme are dihydrobiochanin A and NADP+, whereas its 3 products are biochanin A, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrobiochanin-A:NADP+ Delta2-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Cholestenone%205alpha-reductase | In enzymology, a cholestenone 5alpha-reductase () is an enzyme that catalyzes the chemical reaction
5alpha-cholestan-3-one + NADP+ cholest-4-en-3-one + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholestan-3-one and NADP+, whereas its 3 products are cholest-4-en-3-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxo-5alpha-steroid:NADP+ Delta4-oxidoreductase. Other names in common use include testosterone Delta4-5alpha-reductase, steroid 5alpha-reductase, 3-oxosteroid Delta4-dehydrogenase, 5alpha-reductase, steroid 5alpha-hydrogenase, 3-oxosteroid 5alpha-reductase, testosterone Delta4-hydrogenase, 4-ene-3-oxosteroid 5alpha-reductase, reduced nicotinamide adenine dinucleotide, phosphate:Delta4-3-ketosteroid 5alpha-oxidoreductase, 4-ene-5alpha-reductase, Delta4-3-ketosteroid 5alpha-oxidoreductase, cholest-4-en-3-one 5alpha-reductase, and testosterone 5alpha-reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydro-1%2C2-dihydroxynaphthalene%20dehydrogenase | In enzymology, a cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydronaphthalene-1,2-diol + NAD+ naphthalene-1,2-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydronaphthalene-1,2-diol and NAD+, whereas its 3 products are naphthalene-1,2-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydronaphthalene-1,2-diol:NAD+ 1,2-oxidoreductase. Other names in common use include (+)-cis-naphthalene dihydrodiol dehydrogenase, naphthalene dihydrodiol dehydrogenase, and cis-dihydrodiol naphthalene dehydrogenase. This enzyme participates in 1- and 2-methylnaphthalene degradation and naphthalene and anthracene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydrobenzene-1%2C2-diol%20dehydrogenase | In enzymology, a cis-1,2-dihydrobenzene-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydrobenzene-1,2-diol + NAD+ catechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydrobenzene-1,2-diol and NAD+, whereas its 3 products are catechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydrobenzene-1,2-diol:NAD+ oxidoreductase. Other names in common use include cis-benzene glycol dehydrogenase, cis-1,2-dihydrocyclohexa-3,5-diene (nicotinamide adenine, and dinucleotide) oxidoreductase. This enzyme participates in 4 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, naphthalene and anthracene degradation, and styrene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-1%2C2-dihydroxy-4-methylcyclohexa-3%2C5-diene-1-carboxylate%20dehydrogenase | In enzymology, a cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + NAD(P)+ 4-methylcatechol + NAD(P)H + CO2
The 3 substrates of this enzyme are cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate, NAD+, and NADP+, whereas its 4 products are 4-methylcatechol, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate:NAD(P)+ oxidoreductase (decarboxylating). This enzyme participates in toluene and xylene degradation.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-2%2C3-dihydrobiphenyl-2%2C3-diol%20dehydrogenase | In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+ biphenyl-2,3-diol + NADH + H+
Thus, the two substrates of this enzyme are cis-3-phenylcyclohexa-3,5-diene-1,2-diol and NAD+, whereas its 3 products are biphenyl-2,3-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3-phenylcyclohexa-3,5-diene-1,2-diol:NAD+ oxidoreductase. This enzyme is also called 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase. This enzyme participates in biphenyl degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-2-enoyl-CoA%20reductase%20%28NADPH%29 | In enzymology, a cis-2-enoyl-CoA reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ cis-2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are cis-2,3-dehydroacyl-CoA, NADPH, and H+.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ cis-2-oxidoreductase. Other names in common use include NADPH-dependent cis-enoyl-CoA reductase, reductase, cis-2-enoyl coenzyme A, cis-2-enoyl-coenzyme A reductase, and cis-2-enoyl-CoA reductase (NADPH).
References
Further reading
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-3%2C4-dihydrophenanthrene-3%2C4-diol%20dehydrogenase | In enzymology, a cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD+ phenanthrene-3,4-diol + NADH + H+
Thus, the two substrates of this enzyme are (+)-cis-3,4-dihydrophenanthrene-3,4-diol and NAD+, whereas its 3 products are phenanthrene-3,4-diol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (+)-cis-3,4-dihydrophenanthrene-3,4-diol:NAD+ 3,4-oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cis-dihydroethylcatechol%20dehydrogenase | In enzymology, a cis-dihydroethylcatechol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydro-3-ethylcatechol + NAD+ 3-ethylcatechol + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydro-3-ethylcatechol and NAD+, whereas its 3 products are 3-ethylcatechol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydro-3-ethylcatechol:NAD+ oxidoreductase. This enzyme participates in ethylbenzene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coproporphyrinogen%20dehydrogenase | In enzymology, a coproporphyrinogen dehydrogenase () is an enzyme that catalyzes the chemical reaction
coproporphyrinogen III + 2 S-adenosyl-L-methionine protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
Thus, the two substrates of this enzyme are coproporphyrinogen III and S-adenosyl-L-methionine, whereas its 4 products are protoporphyrinogen IX, CO2, L-methionine, and 5'-deoxyadenosine.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating). Other names in common use include oxygen-independent coproporphyrinogen-III oxidase, HemF, HemN, radical SAM enzyme, and coproporphyrinogen III oxidase. This enzyme participates in porphyrin and chlorophyll metabolism. HemN is the Oxygen-independent oxidase produced in E. coli. HemF is the oxygen-dependent oxidase within E. coli. Importantly, only HemN utilizes S-adenosyl Methionine (SAM). Human variants of Coproporphyrinogen oxidase are cofactor-independent.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cortisone%20alpha-reductase | In enzymology, a cortisone alpha-reductase () is an enzyme that catalyzes the chemical reaction
4,5alpha-dihydrocortisone + NADP+ cortisone + NADPH + H+
Thus, the two substrates of this enzyme are 4,5alpha-dihydrocortisone and NADP+, whereas its 3 products are cortisone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,5alpha-dihydrocortisone:NADP+ Delta4-oxidoreductase. Other names in common use include cortisone Delta4-5alpha-reductase, microsomal steroid reductase (5alpha), Delta4-3-ketosteroid reductase (5alpha), Delta4-3-oxosteroid-5alpha-reductase, NADPH:Delta4-3-oxosteroid-5alpha-oxidoreductase, and Delta4-5alpha-reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cucurbitacin%20Delta23-reductase | In enzymology, a cucurbitacin Delta23-reductase () is an enzyme that catalyzes the chemical reaction
23,24-dihydrocucurbitacin + NAD(P)+ cucurbitacin + NAD(P)H + H+
The 3 substrates of this enzyme are 23,24-dihydrocucurbitacin, NAD+, and NADP+, whereas its 4 products are cucurbitacin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 23,24-dihydrocucurbitacin:NAD(P)+ Delta23-oxidoreductase. This enzyme is also called NAD(P)H: cucurbitacin B Delta23-oxidoreductase. It employs one cofactor, manganese.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexanone%20dehydrogenase | In enzymology, a cyclohexanone dehydrogenase () is an enzyme that catalyzes a chemical reaction
cyclohexanone + acceptor cyclohex-2-enone + reduced acceptor
Thus, the two substrates of this enzyme are cyclohexanone and acceptor, whereas its two products are cyclohex-2-enone and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:(acceptor) 2-oxidoreductase.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta14-sterol%20reductase | In enzymology, a Delta14-sterol reductase () is an enzyme that catalyzes the chemical reaction
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol and NADP+, whereas its 3 products are 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol:NADP+ Delta14-oxidoreductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta24%28241%29-sterol%20reductase | In enzymology, a Delta24(241)-sterol reductase () is an enzyme that catalyzes the chemical reaction
ergosterol + NADP+ ergosta-5,7,22,24(241)-tetraen-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are ergosterol and NADP+, whereas its 3 products are ergosta-5,7,22,24(241)-tetraen-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ergosterol:NADP+ Delta24(241)-oxidoreductase. Other names in common use include sterol Delta24(28)-methylene reductase, and sterol Delta24(28)-reductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Delta24-sterol%20reductase | In enzymology, a Delta24-sterol reductase () is an enzyme that catalyzes the chemical reaction
5alpha-cholest-7-en-3beta-ol + NADP+ 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-cholest-7-en-3beta-ol and NADP+, whereas its 3 products are 5alpha-cholesta-7,24-dien-3beta-ol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sterol:NADP+ Delta24-oxidoreductase. This enzyme is also called lanosterol Delta24-reductase. This enzyme participates in biosynthesis of steroids.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dibenzothiophene%20dihydrodiol%20dehydrogenase | In enzymology, a dibenzothiophene dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD+ 1,2-dihydroxydibenzothiophene + NADH + H+
Thus, the two substrates of this enzyme are cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene and NAD+, whereas its 3 products are 1,2-dihydroxydibenzothiophene, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene:NAD+ oxidoreductase.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydropyrimidine%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a dihydropyrimidine dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NADP+ uracil + NADPH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NADP+, whereas its 3 products are uracil, NADPH, and H+.
In humans the enzyme is encoded by the DPYD gene. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur. It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.
Terminology
The systematic name of this enzyme class is 5,6-dihydrouracil:NADP+ 5-oxidoreductase. Other names in common use include:
dihydrothymine dehydrogenase
dihydrouracil dehydrogenase (NADP+)
4,5-dihydrothymine: oxidoreductase
DPD
DHPDH
dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide, phosphate)
DHU dehydrogenase
hydropyrimidine dehydrogenase
dihydropyrimidine dehydrogenase (NADP+)
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Function
The protein is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. Genetic deficiency of this enzyme results in an error in pyrimidine metabolism associated with thymine-uraciluria and an increased risk of toxicity in cancer patients receivin |
https://en.wikipedia.org/wiki/Dihydrouracil%20dehydrogenase%20%28NAD%2B%29 | In enzymology, a dihydrouracil dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + NAD+ uracil + NADH + H+
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NAD+, whereas its 3 products are uracil, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:NAD+ oxidoreductase. Other names in common use include dehydrogenase, dihydrouracil, dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, pyrimidine reductase, thymine reductase, uracil reductase, and dihydrouracil dehydrogenase (NAD+). This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrouracil%20oxidase | In enzymology, a dihydrouracil oxidase () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + O2 uracil + H2O2
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and O2, whereas its two products are uracil and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:oxygen oxidoreductase. It employs one cofactor, FMN.
References
EC 1.3.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Divinyl%20chlorophyllide%20a%208-vinyl-reductase | In enzymology, divinyl chlorophyllide a 8-vinyl-reductase () is an enzyme that catalyzes the chemical reaction
3,8-divinylprotochlorophyllide + NADPH + H+ protochlorophyllide + NADP+
The three substrates of this enzyme are 3,8-divinylprotochlorophyllide, NADPH, and H+; its two products are protochlorophyllide and NADP+. This enzyme can also convert alternative substrates, for example 3,8-divinyl chlorophyllide a and in all cases reduces a single specific vinyl group to an ethyl group.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorophyllide-a :NADP+ oxidoreductase. Other names in common use include 3,8-divinyl protochlorophyllide a 8-vinyl-reductase, [4-vinyl]chlorophyllide a reductase, and 4VCR. This enzyme is part of the biosynthetic pathway to chlorophylls.
See also
Biosynthesis of chlorophylls
References
</ref>
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Enoyl-%28acyl-carrier-protein%29%20reductase%20%28NADPH%2C%20A-specific%29 | In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, whereas its 3 products are [[trans-2,3-dehydroacyl-[acyl-carrier-protein]]], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific). Other names in common use include acyl-ACP dehydrogenase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine, dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl-ACp reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific).
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Enoyl-%28acyl-carrier-protein%29%20reductase%20%28NADPH%2C%20B-specific%29 | In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + NADP+ trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, whereas its 3 products are [[trans-2,3-dehydroacyl-[acyl-carrier-protein]]], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific). Other names in common use include acyl-ACP dehydrogenase, reductase, enoyl-[acyl carrier protein] (reduced nicotinamide, adenine dinucleotide phosphate), NADPH 2-enoyl Co A reductase, enoyl acyl-carrier-protein reductase, enoyl-ACP reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Fumarate%20reductase%20%28NADH%29 | In enzymology, a fumarate reductase (NADH) () is an enzyme that catalyzes the chemical reaction
succinate + NAD+ fumarate + NADH + H+
Thus, the two substrates of this enzyme are succinate and NAD+, whereas its three products are fumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate:NAD+ oxidoreductase. Other names in common use include NADH-fumarate reductase, NADH-dependent fumarate reductase, and fumarate reductase (NADH).
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Geissoschizine%20dehydrogenase | In enzymology, a geissoschizine dehydrogenase () is an enzyme that catalyzes the chemical reaction
geissoschizine + NADP+ 4,21-didehydrogeissoschizine + NADPH
Thus, the two substrates of this enzyme are geissoschizine and NADP+, whereas its two products are 4,21-didehydrogeissoschizine and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geissoschizine:NADP+ 4,21-oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoquinoline%201-oxidoreductase | In enzymology, an isoquinoline 1-oxidoreductase () is an enzyme that catalyzes the chemical reaction
isoquinoline + acceptor + H2O isoquinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are isoquinoline, acceptor, and H2O, whereas its two products are isoquinolin-1(2H)-one and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating).
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isovaleryl-CoA%20dehydrogenase | In enzymology, an isovaleryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-methylbutanoyl-CoA + acceptor 3-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 3-methylbutanoyl-CoA and acceptor, whereas its two products are 3-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, FAD.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . It was created by a group containing K.A.Tiffany, D.L.Roberts, M.Wang, R.Paschke, A.-W.A.Mohsen, J.Vockley, and J.J.P.Kim. The structure was released on May 20, 1998.
Leucine metabolism
References
EC 1.3.8
Flavoproteins
Enzymes of known structure
Mitochondrial proteins |
https://en.wikipedia.org/wiki/Kynurenate-7%2C8-dihydrodiol%20dehydrogenase | In enzymology, a kynurenate-7,8-dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
7,8-dihydro-7,8-dihydroxykynurenate + NAD+ 7,8-dihydroxykynurenate + NADH + H+
Thus, the two substrates of this enzyme are 7,8-dihydro-7,8-dihydroxykynurenate and NAD+, whereas its 3 products are 7,8-dihydroxykynurenate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase. Other names in common use include 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase, and 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase. This enzyme participates in tryptophan metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-galactonolactone%20oxidase | In enzymology, a L-galactonolactone oxidase () is an enzyme that catalyzes the chemical reaction
L-galactono-1,4-lactone + O2 L-ascorbate + H2O2
Thus, the two substrates of this enzyme are L-galactono-1,4-lactone and O2, whereas its two products are L-ascorbic acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-galactono-1,4-lactone:oxygen 3-oxidoreductase. This enzyme is also called L-galactono-1,4-lactone oxidase. This enzyme participates in ascorbic acid and aldaric acid metabolism. It employs one cofactor, FAD.
References
EC 1.3.3
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maleylacetate%20reductase | In enzymology, a maleylacetate reductase () is an enzyme that catalyzes the chemical reaction
3-oxoadipate + NAD(P)+ 2-maleylacetate + NAD(P)H + H+
The 3 substrates of this enzyme are 3-oxoadipate, NAD+, and NADP+, whereas its 4 products are 2-maleylacetate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-oxoadipate:NAD(P)+ oxidoreductase. This enzyme is also called maleolylacetate reductase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, benzoate degradation via hydroxylation, and 1,4-dichlorobenzene degradation.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Meso-tartrate%20dehydrogenase | In enzymology, a meso-tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
meso-tartrate + NAD+ dihydroxyfumarate + NADH + H+
Thus, the two substrates of this enzyme are meso-tartaric acid and NAD+, whereas its 3 products are dihydroxyfumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is meso-tartrate:NAD+ oxidoreductase. This enzyme participates in glyoxylic acid and dicarboxylic acid metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Orotate%20reductase%20%28NADH%29 | In enzymology, an orotate reductase (NADH) () is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NAD+ orotate + NADH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NAD+, whereas its 3 products are orotate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NAD+ oxidoreductase. This enzyme is also called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism. It has 2 cofactors: FAD, and FMN.
References
EC 1.3.1
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Orotate%20reductase%20%28NADPH%29 | In enzymology, an orotate reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(S)-dihydroorotate + NADP+ orotate + NADPH + H+
Thus, the two substrates of this enzyme are (S)-dihydroorotate and NADP+, whereas its 3 products are orotate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-dihydroorotate:NADP+ oxidoreductase. Other names in common use include orotate reductase, dihydroorotate dehydrogenase, dihydro-orotic dehydrogenase, L-5,6-dihydro-orotate:NAD+ oxidoreductase, and orotate reductase (NADPH). It has one cofactor, FAD.
References
EC 1.3.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phloroglucinol%20reductase | In enzymology, a phloroglucinol reductase () is an enzyme that catalyzes the chemical reaction
dihydrophloroglucinol + NADP+ phloroglucinol + NADPH + H+
Thus, the two substrates of this enzyme are dihydrophloroglucinol and NADP+, whereas its 3 products are phloroglucinol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrophloroglucinol:NADP+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%20desaturase | In enzymology, a phosphatidylcholine desaturase (, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD+ 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH + H+
Thus, the two substrates of this enzyme are 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine and NAD+, whereas its 3 products are 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine:NAD+ Delta12-oxidoreductase. Other names in common use include oleate desaturase, linoleate synthase, oleoyl-CoA desaturase, and oleoylphosphatidylcholine desaturase.
References
EC 1.14.19
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phthalate%204%2C5-cis-dihydrodiol%20dehydrogenase | In enzymology, a phthalate 4,5-cis-dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD+ 4,5-dihydroxyphthalate + NADH + H+
Thus, the two substrates of this enzyme are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate and NAD+, whereas its 3 products are 4,5-dihydroxyphthalate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phycocyanobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phycocyanobilin:ferredoxin oxidoreductase (PcyA, ) is an enzyme that catalyzes the chemical reaction
(3Z)-phycocyanobilin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phycocyanobilin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phycocyanobilin:ferredoxin oxidoreductase. This enzyme participates in porphyrin and chlorophyll metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.3.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phycoerythrobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phycoerythrobilin:ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction
(3Z)-phycoerythrobilin + oxidized ferredoxin 15,16-dihydrobiliverdin + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phycoerythrobilin and oxidized ferredoxin, whereas its two products are 15,16-dihydrobiliverdin and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phycoerythrobilin:ferredoxin oxidoreductase. This enzyme is also called PebB. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phytochromobilin%3Aferredoxin%20oxidoreductase | In enzymology, a phytochromobilin:ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction
(3Z)-phytochromobilin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
Thus, the two substrates of this enzyme are (3Z)-phytochromobilin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is (3Z)-phytochromobilin:ferredoxin oxidoreductase. Other names in common use include HY2, PPhiB synthase, and phytochromobilin synthase. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pimeloyl-CoA%20dehydrogenase | In enzymology, a pimeloyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
pimeloyl-CoA + NAD+ 6-carboxyhex-2-enoyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are pimeloyl-CoA and NAD+, whereas its 3 products are 6-carboxyhex-2-enoyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-2%20dehydrogenase | In enzymology, a precorrin-2 dehydrogenase () is an enzyme that catalyzes the chemical reaction
precorrin-2 + NAD+ sirohydrochlorin + NADH + H+
The two substrates of this enzyme are precorrin-2 and NAD+; its three products are sirohydrochlorin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is precorrin-2:NAD+ oxidoreductase. Other names in common use include Met8p, SirC, and CysG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria and to Cofactor F430.
See also
Cobalamin biosynthesis
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-6A%20reductase | In enzymology, a precorrin-6A reductase () is an enzyme that catalyzes the chemical reaction
precorrin-6A + NADPH + H+ precorrin-6B + NADP+
The three substrates of this enzyme are precorrin 6A, NADPH and a proton; its two products are precorrin 6B and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH=CH group of an acceptor with NAD or NADPH as donor. The systematic name of this enzyme class is precorrin-6B:NADP+ oxidoreductase. Other names in common use include precorrin-6X reductase, precorrin-6Y:NADP+ oxidoreductase and CobK. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Prephenate%20dehydrogenase | Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine.
Nomenclature
Gene: (Saccharomyces Cerevisiae) TYR1
Shikimate pathway: Arogenate/Prephenate (ADH/PDH). Although in the shikimate pathway arogenate and prephenate dehydrogenase catalyze different reactions, they can at times be used interchangeably.
TyrA (tyrosine A: within the tyrosine pathway)
Prephenate dehydrogenase
Prephenate (Nicotinamide adenine dinucleotide phosphate) dehydrogenase
Prephenate dehydrogenase (NADP)
NADP+ oxidoreductase
Homology
This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria (mostly cyanobacteria) and four different kinds of plants (mostly different kinds of beans).
Bacteria organisms (examples): Acenitobacter calcoaceticus, Fischerella sp., Flavobacterium so., Comamonas testosteroni, and nostoc sp.
Plant organisms: phaseolus coccineus, phaseolus vulgaris, vicia faba, vigna radiata
Function
Present in the shikimate pathway, in the pathway to synthesize tyrosine (a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4-hydroxyphenylpyruvate.
Reaction
In enzymology, a prephenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
prephenate + NAD+ 4-hydroxyphenylpyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are prephenate and NAD+, whereas its 3 products are |
https://en.wikipedia.org/wiki/Prephenate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, a prephenate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
prephenate + NADP+ 4-hydroxyphenylpyruvate + CO2 + NADPH
Thus, the two substrates of this enzyme are prephenate and NADP+, whereas its 3 products are 4-hydroxyphenylpyruvate, CO2, and NADPH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include prephenate dehydrogenase, prephenate (nicotinamide adenine dinucleotide phosphate), dehydrogenase, and prephenate dehydrogenase (NADP). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Progesterone%205alpha-reductase | In enzymology, a progesterone 5alpha-reductase () is an enzyme that catalyzes the chemical reaction
5alpha-pregnan-3,20-dione + NADP+ progesterone + NADPH + H+
Thus, the two substrates of this enzyme are 5alpha-pregnan-3,20-dione and NADP+, whereas its 3 products are progesterone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. It is a C21-steroid hormone that is a 5α-pregnane substituted with a oxo groups at positions 3 and 20. It is an intermediate in the conversion of progesterone to allopregnalone and isopregnanolone, other common forms of neurosteroids. The systematic name of this enzyme class is 5alpha-pregnan-3,20-dione:NADP+ 5-oxidoreductase. Other names in common use include steroid 5-alpha-reductase, and Delta4-steroid 5alpha-reductase (progesterone).
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protochlorophyllide%20reductase | In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.
There are two structurally unrelated proteins with this sort of activity, referred to as light-dependent (LPOR) and dark-operative (DPOR). The light- and NADPH-dependent reductase is part of the short-chain dehydrogenase/reductase (SDR) superfamily and is found in plants and oxygenic photosynthetic bacteria, while the ATP-dependent dark-operative version is a completely different protein, consisting of three subunits that exhibit significant sequence and quaternary structure similarity to the three subunits of nitrogenase. This enzyme may be evolutionary older; due to its bound iron-sulfur clusters is highly sensitive to free oxygen and does not function if the atmospheric oxygen concentration exceeds about 3%. It is possible that evolutionary pressure associated with the great oxidation event resulted in the development of the light-dependent system.
The light-dependent version () uses NADPH:
protochlorophyllide + NADPH + H+ chlorophyllide a + NADP+
While the light-independent or dark-operative version () uses ATP and ferredoxin:
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
Light-dependent
The light-dependent version has the accepted name protochlorophyllide reductase. Th |
https://en.wikipedia.org/wiki/Pyrroloquinoline-quinone%20synthase | In enzymology, a pyrroloquinoline-quinone synthase () is an enzyme that catalyzes the chemical reaction
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate + 3 O2 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline- 2,7,9-tricarboxylate + 2 H2O2 + 2 H2O
The two substrates of this enzyme are 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate, and O2, whereas its 3 products are 4,5-dioxo-3a,4,5,6,7,8,9,9b-octahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate, H2O2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinol ine-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing). This enzyme is also called PqqC.
References
EC 1.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinaldate%204-oxidoreductase | In enzymology, a quinaldate 4-oxidoreductase () is an enzyme that catalyzes the chemical reaction
quinaldate + acceptor + H2O kynurenate + reduced acceptor
The 3 substrates of this enzyme are quinaldate, acceptor, and H2O, whereas its two products are kynurenate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating). This enzyme is also called quinaldic acid 4-oxidoreductase.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinoline%202-oxidoreductase | In enzymology, a quinoline 2-oxidoreductase () is an enzyme that catalyzes the chemical reaction
quinoline + acceptor + H2O quinolin-1(2H)-one + reduced acceptor
The 3 substrates of this enzyme are quinoline, acceptor, and H2O, whereas its two products are quinolin-1(2H)-one and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline:acceptor 2-oxidoreductase (hydroxylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.3.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Quinoline-4-carboxylate%202-oxidoreductase | In enzymology, a quinoline-4-carboxylate 2-oxidoreductase () is an enzyme that catalyzes the chemical reaction
quinoline-4-carboxylate + acceptor + H2O 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor
The 3 substrates of this enzyme are quinoline-4-carboxylate, acceptor, and H2O, whereas its two products are 2-oxo-1,2-dihydroquinoline-4-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating). Other names in common use include quinaldic acid 4-oxidoreductase, and quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating).
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Secologanin%20synthase | In enzymology, a secologanin synthase (, was wrongly classified as in the past) is an enzyme that catalyzes the chemical reaction
loganin + NADPH + H+ + O2 secologanin + NADP+ + 2 H2O
The 4 substrates of this enzyme are loganin, NADPH, H+, and O2, whereas its 3 products are secologanin, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is loganin:oxygen oxidoreductase (ring-cleaving). This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.14.19
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Terephthalate%201%2C2-cis-dihydrodiol%20dehydrogenase | In enzymology, a terephthalate 1,2-cis-dihydrodiol dehydrogenase () is an enzyme that catalyzes the chemical reaction:
cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD+ 3,4-dihydroxybenzoate + CO2 + NADH
Thus, the two substrates of this enzyme are cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate and NAD+, whereas its 3 products are 3,4-dihydroxybenzoate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/R%C4%83zvan%20Neagu | Răzvan Neagu (born 25 May 1987) is a Romanian former football player.
Statistics
Statistics accurate as of 1 November 2011
Career honours
SC Vaslui
Cupa României
Runner-up: 2010
UEFA Intertoto Cup
Winner: 2008
External links
1987 births
Living people
Footballers from Bacău
Romanian men's footballers
CS Sporting Vaslui players
FCM Bacău players
ACF Gloria Bistrița players
FC Petrolul Ploiești players
Liga I players
CS Turnu Severin players
Men's association football forwards |
https://en.wikipedia.org/wiki/Tetrahydroberberine%20oxidase | (S)-Tetrahydroberberine oxidase (EC 1.3.3.8) is an enzyme that catalyzes the final transformation in the biosynthesis of berberine, a quaternary benzylisoquinoline alkaloid of the protoberberine structural subgroup. This reaction pathway catalyzes the four-electron oxidation of (S)-tetrahydroberberine (also known as (S)-canadine) in the presence of oxygen to produce berberine and hydrogen peroxide as products.
(S)-Tetrahydroberberine + 2 O2 ⇌ Berberine + 2 H2O2
This enzyme belongs to the family known as oxidoreductases, in this instance the CH-CH moiety acts as the electron donor with oxygen acting as the electron acceptor. The systematic name of this enzyme is (S)-tetrahydroberberine:oxygen oxidoreductase; but it is also known as (S)-THB oxidase, tetrahydroberberine oxidase, and decreasingly, as (S)-tetrahydroprotoberberine oxidase.
References
EC 1.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-1%2C2-dihydrobenzene-1%2C2-diol%20dehydrogenase | In enzymology, a trans-1,2-dihydrobenzene-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
trans-1,2-dihydrobenzene-1,2-diol + NADP+ catechol + NADPH + H+
Thus, the two substrates of this enzyme are trans-1,2-dihydrobenzene-1,2-diol and NADP+, whereas its three products are catechol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase. This enzyme is also called dihydrodiol dehydrogenase. This enzyme participates in metabolism of xenobiotics by cytochrome p450.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , and .
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Trans-2-enoyl-CoA%20reductase%20%28NAD%2B%29 | In enzymology, a trans-2-enoyl-CoA reductase (NAD+) () is an enzyme that catalyzes the chemical reaction
trans-2,3-dehydroacyl-CoA + NADH + H+ acyl-CoA + NAD+
Thus, the three substrates of this enzyme are trans-didehydroacyl-CoA, NADH, and H+, whereas its two products are acyl-CoA and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NAD+ trans-2-oxidoreductase. This enzyme is also called trans-2-enoyl-CoA reductase (NAD+). This enzyme participates in butanoate metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-2-enoyl-CoA%20reductase%20%28NADPH%29 | In enzymology, a (NADPH) () is an enzyme that catalyzes the chemical reaction
trans-2,3-dehydroacyl-CoA + NADPH + H+ acyl-CoA + NADP+
Thus, the three substrates of this enzyme are , NADPH, and H+, whereas its two products are acyl-CoA and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ trans-2-oxidoreductase. Other names in common use include NADPH-dependent trans-2-enoyl-CoA reductase, reductase, trans-enoyl coenzyme A, and trans-2-enoyl-CoA reductase (NADPH). This enzyme participates in fatty acid elongation in mitochondria and polyunsaturated fatty acid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tryptophan%20alpha%2Cbeta-oxidase | In enzymology, a tryptophan alpha,beta-oxidase () is an enzyme that catalyzes the chemical reaction
L-tryptophan + O2 alpha,beta-didehydrotryptophan + H2O2
Thus, the two substrates of this enzyme are L-tryptophan and O2, whereas its two products are alpha,beta-didehydrotryptophan and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-tryptophan:oxygen alpha,beta-oxidoreductase. Other names in common use include L-tryptophan 2',3'-oxidase, and L-tryptophan alpha,beta-dehydrogenase. It employs one cofactor, heme.
References
EC 1.3.3
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Xanthommatin%20reductase | In enzymology, a xanthommatin reductase () is an enzyme that catalyzes the chemical reaction
5,12-dihydroxanthommatin + NAD+ xanthommatin + NADH + H+
Thus, the two substrates of this enzyme are 5,12-dihydroxanthommatin and NAD+, whereas its three products are xanthommatin, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,12-dihydroxanthommatin:NAD+ oxidoreductase.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Zeatin%20reductase | In enzymology, a zeatin reductase () is an enzyme that catalyzes the chemical reaction
dihydrozeatin + NADP+ zeatin + NADPH + H+
Thus, the two substrates of this enzyme are dihydrozeatin and NADP+, whereas its 3 products are zeatin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrozeatin:NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Promyelocytic%20leukemia%20protein | Promyelocytic leukemia protein (PML) (also known as MYL, RNF71, PP8675 or TRIM19) is the protein product of the PML gene. PML protein is a tumor suppressor protein required for the assembly of a number of nuclear structures, called PML-nuclear bodies, which form amongst the chromatin of the cell nucleus. These nuclear bodies are present in mammalian nuclei, at about 1 to 30 per cell nucleus. PML-NBs are known to have a number of regulatory cellular functions, including involvement in programmed cell death, genome stability, antiviral effects and controlling cell division. PML mutation or loss, and the subsequent dysregulation of these processes, has been implicated in a variety of cancers.
History
PML was poorly understood until described in the findings of Grignani et al in their 1996 study of patients with acute promyelocytic leukemia (APL). It was found that the karyotype of 90% of APL patients included a reciprocal translocation, resulting in the fusion of the gene encoding retinoic acid receptor alpha, RARA, of chromosome 17 and the PML gene of chromosome 15, which had not previously been characterized. The resultant PML/RARalpha oncofusion gene was shown to disturb normal PML and RARalpha function, thus inhibiting the terminal differentiation of blood precursor cells and allowing the maintenance of a reserve of undifferentiated cells for cancerous progression. This implication of the PML gene in a pathological context led to a greater focus on the gene in future years |
https://en.wikipedia.org/wiki/Chlorate%20reductase | In enzymology, a chlorate reductase () is an enzyme that catalyzes the chemical reaction
AH2 + chlorate A + H2O + chlorite
Thus, the two substrates of this enzyme are a reduced electron acceptor (denoted AH2) and chlorate, whereas its 3 products are an oxidized electron acceptor (denoted A), water, and chlorite. It is closely related to the enzyme perchlorate reductase which reduces both chlorate and perchlorate.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorite:acceptor oxidoreductase. This enzyme is also called chlorate reductase C.
References
EC 1.97.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28Formate-C-acetyltransferase%29-activating%20enzyme | In enzymology, a [formate-C-acetyltransferase]-activating enzyme () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical
The 3 substrates of this enzyme are S-adenosyl-L-methionine, dihydroflavodoxin, and formate C-acetyltransferase-glycine, whereas its 4 products are 5'-deoxyadenosine, L-methionine, flavodoxin semiquinone, and formate C-acetyltransferase-glycin-2-yl radical.
This radical SAM enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is [formate C-acetyltransferase]-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving). Other names in common use include PFL activase, PFL-glycine:S-adenosyl-L-methionine H transferase (flavodoxin-oxidizing, S-adenosyl-L-methionine-cleaving), formate acetyltransferase activating enzyme, formate acetyltransferase-glycine dihydroflavodoxin:S-adenosyl-L-methionine oxidoreductase (S-adenosyl-L-methionine cleaving).
References
EC 1.97.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrogallol%20hydroxytransferase | In enzymology, a pyrogallol hydroxytransferase () is an enzyme that catalyzes the chemical reaction
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene
Thus, the two substrates of this enzyme are 1,2,3,5-tetrahydroxybenzene and 1,2,3-trihydroxybenzene (pyrogallol), whereas its two products are 1,3,5-trihydroxybenzene (phloroglucinol) and 1,2,3,5-tetrahydroxybenzene.
This enzyme participates in benzoic acid degradation via CoA ligation.
Nomenclature
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene hydroxytransferase. Other names in common use include 1,2,3,5-tetrahydroxybenzene hydroxyltransferase, 1,2,3,5-tetrahydroxybenzene:pyrogallol transhydroxylase, 1,2,3,5-tetrahydroxybenzene-pyrogallol hydroxyltransferase (transhydroxylase), pyrogallol hydroxyltransferase, 1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene hydroxyltransferase.
References
EC 1.97.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Selenate%20reductase | In enzymology, a selenate reductase () is an enzyme that catalyzes the chemical reaction
selenite + H2O + acceptor selenate + reduced acceptor
The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.
References
EC 1.97.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfhydrogenase | In enzymology, a sulfhydrogenase (), also known as sulfur reductase, is an enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide using hydrogen as electron donor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is H2:polysulfide oxidoreductase.
References
Further reading
EC 1.12.98
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrachloroethene%20reductive%20dehalogenase | In enzymology, a tetrachloroethene reductive dehalogenase () is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family.
trichloroethene + chloride + acceptor tetrachloroethene + reduced acceptor
The 3 substrates of this enzyme are trichloroethene, chloride, and acceptor, whereas its two products are tetrachloroethene and reduced acceptor.
This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is acceptor:trichloroethene oxidoreductase (chlorinating). This enzyme is also called tetrachloroethene reductase. This enzyme participates in tetrachloroethene degradation.
Note that the physiologically relevant reaction actually occurs in the reverse direction from that shown above. In other words, in the bacterial species where this enzyme is found, tetrachloroethene is reductively dechlorinated to trichloroethene and chloride.
This enzyme is one member of a family of enzymes including trichloroethene dehalogenase and vinyl chloride dehalogenase. The other members of this family do not have their own EC numbers at present.
Reductive dehalogenases are key enzymes for anaerobic respiratory process, termed organohalide respiration.
References
Further reading
EC 1.97.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-cyclopiazonate%20dehydrogenase | Beta-cyclopiazonate dehydrogenase () is an enzyme that catalyzes the chemical reaction
beta-cyclopiazonate + acceptor alpha-cyclopiazonate + reduced acceptor
Thus, the two substrates of this enzyme are beta-cyclopiazonate and an acceptor, whereas its two products are alpha-cyclopiazonate and a reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with other acceptors. The systematic name of this enzyme class is beta-cyclopiazonate:acceptor oxidoreductase (cyclizing). Other names in common use include beta-cyclopiazonate oxidocyclase, beta-cyclopiazonic oxidocyclase, and beta-cyclopiazonate:(acceptor) oxidoreductase (cyclizing). It employs one cofactor, FAD.
References
EC 1.21.99
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Betaine%20reductase | Betaine reductase () is an enzyme that catalyzes the chemical reaction
acetyl phosphate + trimethylamine + thioredoxin disulfide N,N,N-trimethylglycine + phosphate + thioredoxin
The 3 substrates of this enzyme are acetyl phosphate, trimethylamine, and thioredoxin disulfide, whereas its 3 products are N,N,N-trimethylglycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming).
References
EC 1.21.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Columbamine%20oxidase | In enzymology, a columbamine oxidase () is an enzyme that catalyzes the chemical reaction
2 columbamine + O2 2 berberine + 2 H2O
Thus, the two substrates of this enzyme are columbamine and O2, whereas its two products are berberine and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is columbamine:oxygen oxidoreductase (cyclizing). This enzyme is also called berberine synthase. This enzyme participates in alkaloid biosynthesis i. It employs one cofactor, iron.
References
EC 1.21.3
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-proline%20reductase%20%28dithiol%29 | In enzymology, a D-proline reductase (dithiol) () is an enzyme that catalyzes the chemical reaction
5-aminopentanoate + lipoate D-proline + dihydrolipoate
Thus, the two substrates of this enzyme are 5-aminopentanoate and lipoate, whereas its two products are D-proline and dihydrolipoate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is 5-aminopentanoate:lipoate oxidoreductase (cyclizing). This enzyme participates in arginine and proline metabolism. It employs one cofactor, pyruvate.
References
EC 1.21.4
Pyruvate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20reductase | In enzymology, a glycine reductase () is an enzyme that catalyzes the chemical reaction
acetyl phosphate + NH3 + thioredoxin disulfide + H2O glycine + phosphate + thioredoxin
The 4 substrates of this enzyme are acetyl phosphate, NH3, thioredoxin disulfide, and H2O, whereas its 3 products are glycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming).
References
EC 1.21.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isopenicillin%20N%20synthase | Isopenicillin N synthase (IPNS) is a non-heme iron protein belonging to the 2-oxoglutarate (2OG)-dependent dioxygenases oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV).
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 isopenicillin N + 2 H2O
This reaction is a key step in the biosynthesis of penicillin and cephalosporin antibiotics.
The active sites of most isopenicillin N synthases contain an iron ion.
This enzyme is also called isopenicillin N synthetase.
Mechanism
A Fe(II) metal ion in the active site of the enzyme is coordinated by at least two histidine residues, an aspartate residue, a glutamine residue, and two water molecules in the absence of a bound substrate. Just two histidine residues and one aspartic acid residue are entirely conserved. Therefore, it is highly significant that these two histidine residues, His214 and His270, and one aspartic acid residue, Asp216, are precisely the ones essential for activity. When ACV binds the active site, Gln330 and one water molecule are replaced by the ACV thiolate.
The linear tripeptide δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV) must first be assembled from its component amino acids by N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (ACV synthase). This allows for the binding of the substrate ACV to the deprotonated thiol group of the cysteine residue. This ligation of the thiolate to the i |
https://en.wikipedia.org/wiki/Reticuline%20oxidase | In enzymology, a reticuline oxidase () is an enzyme that catalyzes the chemical reaction
(S)-reticuline + O2 (S)-scoulerine + H2O2
Thus, the two substrates of this enzyme are (S)-reticuline and O2, whereas its two products are (S)-scoulerine and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming). Other names in common use include BBE, berberine bridge enzyme, berberine-bridge-forming enzyme, and tetrahydroprotoberberine synthase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.21.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sarcosine%20reductase | In enzymology, a sarcosine reductase () is an enzyme that catalyzes the chemical reaction
acetyl phosphate + methylamine + thioredoxin disulfide N-methylglycine + phosphate + thioredoxin
The 3 substrates of this enzyme are acetyl phosphate, methylamine, and thioredoxin disulfide, whereas its 3 products are N-methylglycine, phosphate, and thioredoxin.
This enzyme belongs to the family of oxydoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is acetyl-phosphate methilamine:thioredoxin disulfide oxydoreductase (M-methylglycine-forming).
References
Further reading
EC 1.21.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulochrin%20oxidase%20%28%28-%29-bisdechlorogeodin-forming%29 | In enzymology, a sulochrin oxidase [(−)-bisdechlorogeodin-forming] () is an enzyme that catalyzes the chemical reaction
2 sulochrin + O2 2 (−)-bisdechlorogeodin + 2 H2O
Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (−)-bisdechlorogeodin and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (−)-specific). This enzyme is also called sulochrin oxidase.
References
EC 1.21.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulochrin%20oxidase%20%28%28%2B%29-bisdechlorogeodin-forming%29 | In enzymology, a sulochrin oxidase [(+)-bisdechlorogeodin-forming] () is an enzyme that catalyzes the chemical reaction
2 sulochrin + O2 2 (+)-bisdechlorogeodin + 2 H2O
Thus, the two substrates of this enzyme are sulochrin and O2, whereas its two products are (+)-bisdechlorogeodin and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is sulochrin:oxygen oxidoreductase (cyclizing, (+)-specific). This enzyme is also called sulochrin oxidase.
References
EC 1.21.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C4-dichlorophenol%206-monooxygenase | In enzymology, a 2,4-dichlorophenol 6-monooxygenase () is an enzyme that catalyzes the chemical reaction
2,4-dichlorophenol + NADPH + H+ + O2 3,5-dichlorocatechol + NADP+ + H2O
The 4 substrates of this enzyme are 2,4-dichlorophenol, NADPH, H+, and O2, whereas its 3 products are 3,5-dichlorocatechol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2,4-dichlorophenol,NADPH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include 2,4-dichlorophenol hydroxylase, and 2,4-dichlorophenol monooxygenase. This enzyme participates in 1,4-dichlorobenzene degradation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/24-hydroxycholesterol%207alpha-hydroxylase | In enzymology, a 24-hydroxycholesterol 7alpha-hydroxylase () is an enzyme that catalyzes the chemical reaction
(24R)-cholest-5-ene-3beta,24-diol + NADPH + H+ + O2 (24R)-cholest-5-ene-3beta,7alpha,24-triol + NADP+ + H2O
The 4 substrates of this enzyme are (24R)-cholest-5-ene-3beta,24-diol, NADPH, H+, and O2, whereas its 3 products are (24R)-cholest-5-ene-3beta,7alpha,24-triol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (24R)-cholest-5-ene-3beta,24-diol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). Other names in common use include 24-hydroxycholesterol 7alpha-monooxygenase, CYP39A1, and CYP39A1 oxysterol 7alpha-hydroxylase.
See also
Steroidogenic enzyme
References
External links
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C6-dihydroxypyridine%203-monooxygenase | In enzymology, a 2,6-dihydroxypyridine 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
2,6-dihydroxypyridine + NADH + H+ + O2 2,3,6-trihydroxypyridine + NAD+ + H2O
The 4 substrates of this enzyme are 2,6-dihydroxypyridine, NADH, H+, and O2, whereas its 3 products are 2,3,6-trihydroxypyridine, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2,6-dihydroxypyridine,NADH:oxygen oxidoreductase (3-hydroxylating). This enzyme is also called 2,6-dihydroxypyridine oxidase. It has 2 cofactors: FAD, and Flavoprotein.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/27-hydroxycholesterol%207alpha-monooxygenase | In enzymology, a 27-hydroxycholesterol 7alpha-monooxygenase () is an enzyme that catalyzes the chemical reaction
27-hydroxycholesterol + NADPH + H+ + O2 7alpha,27-dihydroxycholesterol + NADP+ + H2O
The 4 substrates of this enzyme are 27-hydroxycholesterol, NADPH, H+, and O2, whereas its 3 products are 7alpha,27-dihydroxycholesterol, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 27-hydroxycholesterol,NADPH:oxygen oxidoreductase (7alpha-hydroxylating). This enzyme is also called 27-hydroxycholesterol 7alpha-hydroxylase. It employs one cofactor, heme-thiolate(P-450).
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-aminobenzenesulfonate%202%2C3-dioxygenase | In enzymology, a 2-aminobenzenesulfonate 2,3-dioxygenase () is an enzyme that catalyzes the chemical reaction
2-aminobenzenesulfonate + NADH + H+ + O2 2,3-dihydroxybenzenesulfonate + NH3 + NAD+
The 4 substrates of this enzyme are 2-aminobenzenesulfonate, NADH, H+, and O2, whereas its 3 products are 2,3-dihydroxybenzenesulfonate, NH3, and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzenesulfonate,NADH:oxygen oxidoreductase (2,3-hydroxylating, ammonia-forming). This enzyme is also called 2-aminosulfobenzene 2,3-dioxygenase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-chlorobenzoate%201%2C2-dioxygenase | In enzymology, a 2-chlorobenzoate 1,2-dioxygenase () is an enzyme that catalyzes the chemical reaction
2-chlorobenzoate + NADH + H+ + O2 catechol + chloride + NAD+ + CO2
The 4 substrates of this enzyme are 2-chlorobenzoate, NADH, H+, and O2, whereas its 4 products are catechol, chloride, NAD+, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is 2-chlorobenzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating, dechlorinating, decarboxylating). This enzyme is also called 2-halobenzoate 1,2-dioxygenase. This enzyme participates in benzoate degradation via coa ligation. It employs one cofactor, iron.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%27-deoxymugineic-acid%202%27-dioxygenase | In enzymology, a 2'-deoxymugineic-acid 2'-dioxygenase () is an enzyme that catalyzes the chemical reaction
2'-deoxymugineic acid + 2-oxoglutarate + O2 mugineic acid + succinate + CO2
The 3 substrates of this enzyme are 2'-deoxymugineic acid, 2-oxoglutarate, and O2, whereas its 3 products are mugineic acid, (a compound related to azetidine-2-carboxylic acid) succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is 2'-deoxymugineic acid,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating). This enzyme is also called IDS3.
References
EC 1.14.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxybiphenyl%203-monooxygenase | In enzymology, a 2-hydroxybiphenyl 3-monooxygenase () is an enzyme that catalyzes the chemical reaction
2-hydroxybiphenyl + NADH + H+ + O2 2,3-dihydroxybiphenyl + NAD+ + H2O
The 4 substrates of this enzyme are 2-hydroxybiphenyl, NADH, H+, and O2, whereas its 3 products are 2,3-dihydroxybiphenyl, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-hydroxybiphenyl,NADH:oxygen oxidoreductase (3-hydroxylating).
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxycyclohexanone%202-monooxygenase | In enzymology, a 2-hydroxycyclohexanone 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
2-hydroxycyclohexan-1-one + NADPH + H+ + O2 6-hydroxyhexan-6-olide + NADP+ + H2O
The 4 substrates of this enzyme are 2-hydroxycyclohexan-1-one, NADPH, H+, and O2, whereas its 3 products are 6-hydroxyhexan-6-olide, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-hydroxycyclohexan-1-one,NADPH:oxygen 2-oxidoreductase (1,2-lactonizing).
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxypyridine%205-monooxygenase | In enzymology, a 2-hydroxypyridine 5-monooxygenase () is an enzyme that catalyzes the chemical reaction
2-hydroxypyridine + AH2 + O2 2,5-dihydroxypyridine + A + H2O
The 3 substrates of this enzyme are 2-hydroxypyridine, an electron acceptor AH2, and O2, whereas its 3 products are 2,5-dihydroxypyridine, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 2-hydroxypyridine,hydrogen-donor:oxygen oxidoreductase (5-hydroxylating). This enzyme is also called 2-hydroxypyridine oxygenase.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxyquinoline%205%2C6-dioxygenase | In enzymology, a 2-hydroxyquinoline 5,6-dioxygenase () is an enzyme that catalyzes the chemical reaction
quinolin-2-ol + NADH + H+ + O2 2,5,6-trihydroxy-5,6-dihydroquinoline + NAD+
The 4 substrates of this enzyme are quinolin-2-ol, NADH, H+, and O2, whereas its two products are 2,5,6-trihydroxy-5,6-dihydroquinoline and NAD+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is quinolin-2-ol,NADH:oxygen oxidoreductase (5,6-hydroxylating). Other names in common use include 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase, quinolin-2-ol 5,6-dioxygenase, and quinolin-2(1H)-one 5,6-dioxygenase.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxyquinoline%208-monooxygenase | In enzymology, a 2-hydroxyquinoline 8-monooxygenase () is an enzyme that catalyzes the chemical reaction
quinolin-2-ol + NADH + H+ + O2 quinolin-2,8-diol + NAD+ + H2O
The 4 substrates of this enzyme are quinolin-2-ol, NADH, H+, and O2, whereas its 3 products are quinolin-2,8-diol, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating). This enzyme is also called 2-oxo-1,2-dihydroquinoline 8-monooxygenase. It employs one cofactor, iron.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-nitrophenol%202-monooxygenase | In enzymology, a 2-nitrophenol 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
2-nitrophenol + NADPH + H+ + O2 catechol + nitrite + NADP+ + H2O
The 4 substrates of this enzyme are 2-nitrophenol, NADPH, H+, and O2, whereas its 4 products are catechol, nitrite, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-nitrophenol,NADPH:oxygen 2-oxidoreductase (2-hydroxylating, nitrite-forming). Other names in common use include 2-nitrophenol oxygenase, and nitrophenol oxygenase.
References
EC 1.14.13
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%2C9-dihydroxypterocarpan%206a-monooxygenase | In enzymology, a 3,9-dihydroxypterocarpan 6a-monooxygenase () is an enzyme that catalyzes the chemical reaction
(6aR,11aR)-3,9-dihydroxypterocarpan + NADPH + H+ + O2 (6aS,11aS)-3,6a,9-trihydroxypterocarpan + NADP+ + H2O
The 4 substrates of this enzyme are (6aR,11aR)-3,9-dihydroxypterocarpan, NADPH, H+, and O2, whereas its 3 products are (6aS,11aS)-3,6a,9-trihydroxypterocarpan, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (6aR,11aR)-3,9-dihydroxypterocarpan,NADPH:oxygen oxidoreductase (6a-hydroxylating). Other names in common use include 3,9-dihydroxypterocarpan 6a-hydroxylase, and 3,9-dihydroxypterocarpan 6alpha-monooxygenase (erroneous). This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.
References
EC 1.14.13
NADPH-dependent enzymes
Heme enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/3-hydroxy-2-methylpyridinecarboxylate%20dioxygenase | In enzymology, a 3-hydroxy-2-methylpyridinecarboxylate dioxygenase () is an enzyme that catalyzes the chemical reaction
3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + H+ + O2 2-(acetamidomethylene)succinate + NAD(P)+
The 5 substrates of this enzyme are 3-hydroxy-2-methylpyridine-5-carboxylate, NADH, NADPH, H+, and O2, whereas its 3 products are 2-(acetamidomethylene)succinate, NAD+, and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxy-2-methylpyridine-5-carboxylate,NAD(P)H:oxygen oxidoreductase (decyclizing). Other names in common use include methylhydroxypyridinecarboxylate oxidase, 2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase, methylhydroxypyridine carboxylate dioxygenase, and 3-hydroxy-3-methylpyridinecarboxylate dioxygenase [incorrect]. This enzyme participates in vitamin B6 metabolism. It employs one cofactor, FAD.
References
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxybenzoate%202-monooxygenase | In enzymology, a 3-hydroxybenzoate 2-monooxygenase () is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + AH2 + O2 2,3-dihydroxybenzoate + A + H2O
The 3 substrates of this enzyme are 3-hydroxybenzoate, an electron acceptor AH2, and O2, whereas its 3 products are 2,3-dihydroxybenzoate, the reduction product A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is 3-hydroxybenzoate,hydrogen-donor:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 3-hydroxybenzoate 2-hydroxylase, and 3-HBA-2-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 1.14.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxybenzoate%204-monooxygenase | In enzymology, a 3-hydroxybenzoate 4-monooxygenase () is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + NADPH + H+ + O2 3,4-dihydroxybenzoate + NADP+ + H2O
The 4 substrates of this enzyme are 3-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are 3,4-dihydroxybenzoate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxybenzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). This enzyme is also called 3-hydroxybenzoate 4-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 1.14.13
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-hydroxybenzoate%206-monooxygenase | In enzymology, a 3-hydroxybenzoate 6-monooxygenase () is an enzyme that catalyzes the chemical reaction
3-hydroxybenzoate + NADH + H+ + O2 2,5-dihydroxybenzoate + NAD+ + H2O
The 4 substrates of this enzyme are 3-hydroxybenzoate, NADH, H+, and O2, whereas its 3 products are 2,5-dihydroxybenzoate, NAD+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating). Other names in common use include 3-hydroxybenzoate 6-hydroxylase, m-hydroxybenzoate 6-hydroxylase, and 3-hydroxybenzoic acid-6-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation. It employs one cofactor, FAD.
References
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxyphenylacetate%206-hydroxylase | In enzymology, a 3-hydroxyphenylacetate 6-hydroxylase () is an enzyme that catalyzes the chemical reaction
3-hydroxyphenylacetate + NAD(P)H + H+ + O2 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
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-phenylpropanoate%20dioxygenase | In enzymology, a 3-phenylpropanoate dioxygenase () is an enzyme that catalyzes the chemical reaction
3-phenylpropanoate + NADH + H+ + O2 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
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-aminobenzoate%201-monooxygenase | In enzymology, a 4-aminobenzoate 1-monooxygenase () is an enzyme that catalyzes the chemical reaction
4-aminobenzoate + NAD(P)H + 2 H+ + O2 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
EC 1.14.13
NADPH-dependent enzymes
NADH-dependent enzymes
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-chlorophenylacetate%203%2C4-dioxygenase | In enzymology, a 4-chlorophenylacetate 3,4-dioxygenase () is an enzyme that catalyzes the chemical reaction
4-chlorophenylacetate + NADH + H+ + O2 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
EC 1.14.12
NADPH-dependent enzymes
NADH-dependent enzymes
Iron enzymes
Enzymes of unknown structure |
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