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https://en.wikipedia.org/wiki/Sorbitol-6-phosphate%202-dehydrogenase | In enzymology, a sorbitol-6-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-sorbitol 6-phosphate + NAD+ D-fructose 6-phosphate + NADH + H+
Thus, the two substrates of this enzyme are D-sorbitol 6-phosphate and NAD+, whereas its 3 products are D-fructose 6-phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase. Other names in common use include ketosephosphate reductase, ketosephosphate reductase, D-sorbitol 6-phosphate dehydrogenase, D-sorbitol-6-phosphate dehydrogenase, sorbitol-6-P-dehydrogenase, and D-glucitol-6-phosphate dehydrogenase. This enzyme participates in fructose and mannose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sorbose%20dehydrogenase | In enzymology, a sorbose dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-sorbose + acceptor 5-dehydro-D-fructose + reduced acceptor
Thus, the two substrates of this enzyme are L-sorbose and acceptor, whereas its two products are 5-dehydro-D-fructose and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is L-sorbose:acceptor 5-oxidoreductase. This enzyme is also called L-sorbose:(acceptor) 5-oxidoreductase.
References
EC 1.1.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Spermidine%20dehydrogenase | In enzymology, a spermidine dehydrogenase () is an enzyme that catalyzes the chemical reaction
spermidine + acceptor + H2O propane-1,3-diamine + 4-aminobutanal + reduced acceptor
The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase. This enzyme participates in urea cycle and metabolism of amino groups and beta-alanine metabolism. It has 2 cofactors: FAD, and Heme.
References
EC 1.5.99
Flavoproteins
Heme enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinate-semialdehyde%20dehydrogenase | In enzymology, a succinate-semialdehyde dehydrogenase (SSADH) () is an enzyme that catalyzes the chemical reaction
succinate semialdehyde + NAD+ + H2O succinate + NADH + 2 H+
The 3 substrates of this enzyme are succinate semialdehyde, NAD+, and H2O, whereas its 3 products are succinate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase, succinic semialdehyde dehydrogenase, succinyl semialdehyde dehydrogenase, and succinate semialdehyde:NAD+ oxidoreductase. This enzyme participates in glutamate and butyrate metabolism.
Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation of γ-aminobutyric acid in humans, and deficiency of the enzyme causes serious health effects (succinic semialdehyde dehydrogenase deficiency).
In bacteria, the enzyme is also involved in γ-aminobutyric acid degradation, but can be recruited to facilitate other functions, such as converting succinate-semialdehyde formed during fission of the pyridine ring to succinic acid for entry into the Krebs Cycle.
References
Further reading
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinylglutamate-semialdehyde%20dehydrogenase | In enzymology, a succinylglutamate-semialdehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O N-succinyl-L-glutamate + NADH + 2 H+
The 3 substrates of this enzyme are N-succinyl-L-glutamate 5-semialdehyde, NAD+, and H2O, whereas its 3 products are N-succinyl-L-glutamate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinylglutamic semialdehyde dehydrogenase, N-succinylglutamate 5-semialdehyde dehydrogenase, SGSD, AruD, and AstD. This enzyme participates in arginine and proline metabolism.
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfite%20dehydrogenase | In enzymology, a sulfite dehydrogenase () is an enzyme that catalyzes the chemical reaction
sulfite + 2 ferricytochrome c + H2O sulfate + 2 ferrocytochrome c + 2 H+
The 3 substrates of this enzyme are sulfite, ferricytochrome c, and H2O, whereas its 3 products are sulfate, ferrocytochrome c, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is sulfite:ferricytochrome-c oxidoreductase. Other names in common use include sulfite cytochrome c reductase, sulfite-cytochrome c oxidoreductase, and sulfite oxidase. This enzyme participates in sulfur metabolism.
References
EC 1.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ephedrine%20dehydrogenase | In enzymology, an ephedrine dehydrogenase () is an enzyme that catalyzes the chemical reaction
(-)-ephedrine + NAD+ (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+
Thus, the two substrates of this enzyme are (-)-ephedrine and NAD+, whereas its 3 products are (R)-2-methylimino-1-phenylpropan-1-ol, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-ephedrine:NAD+ 2-oxidoreductase.
References
EC 1.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Erythrose-4-phosphate%20dehydrogenase | In enzymology, an erythrose-4-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-erythrose 4-phosphate + NAD+ + H2O 4-phosphoerythronate + NADH + 2 H+
The 3 substrates of this enzyme are D-erythrose 4-phosphate, NAD+, and H2O, whereas its 3 products are 4-phosphoerythronat, NADH, and H+.
[explainpolicedepartment]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-erythrose 4-phosphate:NAD+ oxidoreductase. Other names in common use include erythrose 4-phosphate dehydrogenase, E4PDH, GapB, Epd dehydrogenase, and E4P dehydrogenase. This enzyme participates in vitamin B6 metabolism (see DXP-dependent biosynthesis of pyridoxal phosphate).
References
EC 1.2.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estradiol%2017alpha-dehydrogenase | In enzymology, an estradiol 17alpha-dehydrogenase () is an enzyme that catalyzes the chemical reaction
estradiol-17alpha + NAD(P)+ estrone + NAD(P)H + H+
The three substrates of this enzyme are estradiol-17alpha, NAD+, and NADP+, whereas its four products are estrone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17alpha-hydroxysteroid:NAD(P)+ 17-oxidoreductase. Other names in common use include 17alpha-estradiol dehydrogenase, 17alpha-hydroxy steroid dehydrogenase, 17alpha-hydroxy steroid oxidoreductase, 17alpha-hydroxysteroid oxidoreductase, and estradiol 17alpha-oxidoreductase. This enzyme participates in androgen and estrogen metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estradiol%2017beta-dehydrogenase | In enzymology, an estradiol 17beta-dehydrogenase () is an enzyme that catalyzes the chemical reaction
estradiol-17beta + NAD(P)+ estrone + NAD(P)H + H+
The 3 substrates of this enzyme are estradiol-17beta, NAD+, and NADP+, whereas its 4 products are estrone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is estradiol-17beta:NAD(P)+ 17-oxidoreductase. Other names in common use include 20alpha-hydroxysteroid dehydrogenase, 17beta,20alpha-hydroxysteroid dehydrogenase, 17beta-estradiol dehydrogenase, estradiol dehydrogenase, estrogen 17-oxidoreductase, and 17beta-HSD. This enzyme participates in androgen and estrogen metabolism.
Structural studies
As of late 2007, 29 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure
Steroid hormone biosynthesis |
https://en.wikipedia.org/wiki/Vellosimine%20dehydrogenase | In enzymology, a vellosimine dehydrogenase () is an enzyme that catalyzes the chemical reaction
10-deoxysarpagine + NADP+ vellosimine + NADPH + H+
Thus, the two substrates of this enzyme are 10-deoxysarpagine and NADP+, whereas its 3 products are vellosimine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-deoxysarpagine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vomifoliol%20dehydrogenase | In enzymology, a vomifoliol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(6S,9R)-6-hydroxy-3-oxo-alpha-ionol + NAD+ (6R)-6-hydroxy-3-oxo-alpha-ionone + NADH + H+
Thus, the two substrates of this enzyme are (6S,9R)-6-hydroxy-3-oxo-alpha-ionol and NAD+, whereas its 3 products are (6R)-6-hydroxy-3-oxo-alpha-ionone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vomifoliol:NAD+ oxidoreductase. Other names in common use include vomifoliol 4'-dehydrogenase, and vomifoliol:NAD+ 4'-oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoacetyl-CoA%20reductase | In enzymology, an acetoacetyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
(R)-3-hydroxyacyl-CoA + NADP+ 3-oxoacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are (R)-3-hydroxyacyl-CoA and NADP+, whereas its 3 products are 3-oxoacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase. Other names in common use include acetoacetyl coenzyme A reductase, hydroxyacyl coenzyme-A dehydrogenase, NADP+-linked acetoacetyl CoA reductase, NADPH:acetoacetyl-CoA reductase, D(−)-beta-hydroxybutyryl CoA-NADP+ oxidoreductase, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase, beta-ketoacyl-CoA reductase, D-3-hydroxyacyl-CoA reductase, and (R)-3-hydroxyacyl-CoA dehydrogenase. This enzyme participates in butanoate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acylglycerone-phosphate%20reductase | In enzymology, an acylglycerone-phosphate reductase () is an enzyme that catalyzes the chemical reaction
1-palmitoylglycerol 3-phosphate + NADP+ palmitoylglycerone phosphate + NADPH + H+
Thus, the two substrates of this enzyme are 1-palmitoylglycerol 3-phosphate and NADP+, whereas its 3 products are palmitoylglycerone phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase. Other names in common use include palmitoyldihydroxyacetone-phosphate reductase, palmitoyl dihydroxyacetone phosphate reductase, palmitoyl-dihydroxyacetone-phosphate reductase, acyldihydroxyacetone phosphate reductase, and palmitoyl dihydroxyacetone phosphate reductase. This enzyme participates in glycerophospholipid and ether lipid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldose%201-dehydrogenase | In enzymology, an aldose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-aldose + NAD+ D-aldonolactone + NADH + H+
Thus, the two substrates of this enzyme are D-aldose and NAD+, whereas its 3 products are D-aldonolactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-aldose:NAD+ 1-oxidoreductase. Other names in common use include aldose dehydrogenase, and dehydrogenase, D-aldohexose.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldose-6-phosphate%20reductase%20%28NADPH%29 | In enzymology, an aldose-6-phosphate reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
D-sorbitol 6-phosphate + NADP+ D-glucose 6-phosphate + NADPH + H+
Thus, the two substrates of this enzyme are D-sorbitol 6-phosphate and NADP+, whereas its 3 products are D-glucose 6-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-aldose-6-phosphate:NADP+ 1-oxidoreductase. Other names in common use include aldose 6-phosphate reductase, NADP+-dependent aldose 6-phosphate reductase, A6PR, aldose-6-P reductase, aldose-6-phosphate reductase, alditol 6-phosphate:NADP+ 1-oxidoreductase, and aldose-6-phosphate reductase (NADPH).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allyl-alcohol%20dehydrogenase | In enzymology, an allyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
allyl alcohol + NADP+ acrolein + NADPH + H+
Thus, the two substrates of this enzyme are allyl alcohol and NADP+, whereas its 3 products are acrolein, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Apiose%201-reductase | In enzymology, an apiose 1-reductase () is an enzyme that catalyzes the chemical reaction
D-apiitol + NAD+ D-apiose + NADH + H+
Thus, the two substrates of this enzyme are D-apiitol and NAD+, whereas its 3 products are D-apiose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-apiitol:NAD+ 1-oxidoreductase. Other names in common use include D-apiose reductase, and D-apiitol reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aryl-alcohol%20dehydrogenase | In enzymology, an aryl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
an aromatic alcohol + NAD+ an aromatic aldehyde + NADH + H+
Thus, the two substrates of this enzyme are aromatic alcohol and NAD+, whereas its 3 products are aromatic aldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-alcohol:NAD+ oxidoreductase. Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and coniferyl alcohol dehydrogenase. This enzyme participates in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, biphenyl degradation, toluene and xylene degradation, and caprolactam degradation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aryl-alcohol%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Aryl-alcohol dehydrogenase (NADP+)}}
In enzymology, an aryl-alcohol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
an aromatic alcohol + NADP+ an aromatic aldehyde + NADPH + H+
Thus, the two substrates of this enzyme are aromatic alcohol and NADP+, whereas its 3 products are aromatic aldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is aryl-alcohol:NADP+ oxidoreductase. Other names in common use include aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide, phosphate), coniferyl alcohol dehydrogenase, NADPH-linked benzaldehyde reductase, and aryl-alcohol dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzyl-2-methyl-hydroxybutyrate%20dehydrogenase | In enzymology, a benzyl-2-methyl-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP+ benzyl 2-methyl-3-oxobutanoate + NADPH + H+
Thus, the two substrates of this enzyme are benzyl (2R,3S)-2-methyl-3-hydroxybutanoate and NADP+, whereas its 3 products are benzyl 2-methyl-3-oxobutanoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzyl-(2R,3S)-2-methyl-3-hydroxybutanoate:NADP+ 3-oxidoreductase. This enzyme is also called benzyl 2-methyl-3-hydroxybutyrate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carbonyl%20reductase%20%28NADPH%29 | In enzymology, a carbonyl reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
R-CO-R' + NADPH + H+ :R-CHOH-R' + NADP+
Thus, the two products of this enzyme are R-CHOH-R' and NADP+, whereas its 3 substrates are R-CO-R', NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde reductase 1, prostaglandin 9-ketoreductase, xenobiotic ketone reductase, NADPH-dependent carbonyl reductase, ALR3, carbonyl reductase, nonspecific NADPH-dependent carbonyl reductase, aldehyde reductase 1, and carbonyl reductase (NADPH). This enzyme participates in arachidonic acid metabolism, and has recently been shown to catabolize S-Nitrosoglutathione, as a means to degrade NO in an NADPH-dependent manner.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Carnitine%203-dehydrogenase | In enzymology, a carnitine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
carnitine + NAD+ 3-dehydrocarnitine + NADH + H+
Thus, the two substrates of this enzyme are carnitine and NAD+, whereas its 3 products are 3-dehydrocarnitine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carveol%20dehydrogenase | In enzymology, a carveol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(-)-trans-carveol + NADP+ (-)-carvone + NADPH + H+
Thus, the two substrates of this enzyme are (-)-trans-carveol and NADP+, whereas its 3 products are (-)-carvone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-carveol:NADP+ oxidoreductase. This enzyme is also called (-)-trans-carveol dehydrogenase. This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlordecone%20reductase | In enzymology, a chlordecone reductase () is an enzyme that catalyzes the chemical reaction
chlordecone alcohol + NADP+ chlordecone + NADPH + H+
Thus, the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cholest-5-ene-3beta%2C7alpha-diol%203beta-dehydrogenase | In enzymology, a cholest-5-ene-3β,7α-diol 3β-dehydrogenase () is an enzyme that catalyzes the chemical reaction
cholest-5-ene-3β,7α-diol + NAD+ 7α-hydroxycholest-4-en-3-one + NADH + H+
Thus, the two substrates of this enzyme are cholest-5-ene-3β,7α-diol and NAD+, whereas its 3 products are 7α-hydroxycholest-4-en-3-one, NADH, and H+.
The systematic name of this enzyme class is cholest-5-ene-3β,7α-diol:NAD+ 3-oxidoreductase. This enzyme is also called 3β-hydroxy-Δ5-C27-steroid oxidoreductase. The human version of this enzyme is known as hydroxy-Δ-5-steroid dehydrogenase, 3 β- and steroid delta-isomerase 7 or HSD3B7 which is encoded by the HSD3B7 gene.
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme is involved in the initial stages of the synthesis of bile acids from cholesterol and a member of the short-chain dehydrogenase/reductase superfamily. This enzyme is a membrane-associated endoplasmic reticulum protein which is active against 7-alpha hydrosylated sterol substrates.
Clinical significance
Mutations in the HSD3B7 gene are associated with a congenital bile acid synthesis defect which leads to neonatal cholestasis, a form of progressive liver disease.
See also
3-beta-HSD
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cholestanetetraol%2026-dehydrogenase | In enzymology, a cholestanetetraol 26-dehydrogenase () is an enzyme that catalyzes the chemical reaction
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + NAD+ (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + NADH + H+
Thus, the two substrates of this enzyme are (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol and NAD+, whereas its 3 products are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+ 26-oxidoreductase. Other names in common use include cholestanetetraol 26-dehydrogenase, 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase, TEHC-NAD oxidoreductase, 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+, and 26-oxidoreductase. This enzyme participates in bile acid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cinnamyl-alcohol%20dehydrogenase | In enzymology, a cinnamyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cinnamyl alcohol + NADP+ cinnamaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are cinnamyl alcohol and NADP+, whereas its 3 products are cinnamaldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl alcohol dehydrogenase, and CAD. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure
Phenylpropanoids metabolism |
https://en.wikipedia.org/wiki/Codeinone%20reductase%20%28NADPH%29 | In enzymology, a codeinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
codeine + NADP+ codeinone + NADPH + H+
Thus, the two substrates of this enzyme are codeine and NADP+, whereas its 3 products are codeinone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is codeine:NADP+ oxidoreductase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coniferyl-alcohol%20dehydrogenase | In enzymology, a coniferyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
coniferyl alcohol + NADP+ coniferyl aldehyde + NADPH + H+
Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexane-1%2C2-diol%20dehydrogenase | In enzymology, a cyclohexane-1,2-diol dehydrogenase () is an enzyme that catalyzes the chemical reaction
trans-cyclohexane-1,2-diol + NAD+ 2-hydroxycyclohexan-1-one + NADH + H+
Thus, the two substrates of this enzyme are trans-cyclohexane-1,2-diol and NAD+, whereas its 3 products are 2-hydroxycyclohexan-1-one, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trans-cyclohexane-1,2-diol:NAD+ 1-oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexanol%20dehydrogenase | In enzymology, a cyclohexanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cyclohexanol + NAD+ cyclohexanone + NADH + H+
Thus, the two substrates of this enzyme are cyclohexanol and NAD+, whereas its 3 products are cyclohexanone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclohexanol:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclopentanol%20dehydrogenase | In enzymology, a cyclopentanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
cyclopentanol + NAD+ cyclopentanone + NADH + H+
Thus, the two substrates of this enzyme are cyclopentanol and NAD+, whereas its 3 products are cyclopentanone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclopentanol:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinitol%202-dehydrogenase | In enzymology, a D-arabinitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinitol + NAD+ ⇌ D-ribulose + NADH + H+
Thus, the two substrates of this enzyme are D-arabinitol and NAD+, whereas its 3 products are D-ribulose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming). This enzyme is also called D-arabinitol 2-dehydrogenase (ribulose-forming).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinitol%204-dehydrogenase | In enzymology, a D-arabinitol 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinitol + NAD+ D-xylulose + NADH + H+
Thus, the two substrates of this enzyme are D-arabinitol and NAD+, whereas its 3 products are D-xylulose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinitol:NAD+ 4-oxidoreductase. Other names in common use include D-arabitol dehydrogenase and arabitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
References
Characterization of Arabitol Dehyrogenase in Transplastomic Plants. LAP Lambert Academic Publishing.
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinose%201-dehydrogenase | In enzymology, a D-arabinose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-arabinose + NAD+ D-arabinono-1,4-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-arabinose and NAD+, whereas its 3 products are D-arabinono-1,4-lactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinose:NAD+ 1-oxidoreductase. Other names in common use include NAD+-pentose-dehydrogenase, and arabinose(fucose)dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-iditol%202-dehydrogenase | In enzymology, a -iditol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
-iditol + NAD+ -sorbose + NADH + H+
Thus, the two substrates of this enzyme are -iditol and NAD+, whereas its 3 products are -sorbose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is -iditol:NAD+ 2-oxidoreductase. This enzyme is also called -sorbitol dehydrogenase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diethyl%202-methyl-3-oxosuccinate%20reductase | In enzymology, a diethyl 2-methyl-3-oxosuccinate reductase () is an enzyme that catalyzes the chemical reaction
diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP+ diethyl 2-methyl-3-oxosuccinate + NADPH + H+
Thus, the two substrates of this enzyme are diethyl (2R,3R)-2-methyl-3-hydroxysuccinate and NADP+, whereas its 3 products are diethyl 2-methyl-3-oxosuccinate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is diethyl-(2R,3R)-2-methyl-3-hydroxysuccinate:NADP+ 3-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrobunolol%20dehydrogenase | In enzymology, a dihydrobunolol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- naphthol + NADP+ (+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)- naphthalenone + NADPH + H+
The three substrates of this enzyme are [[(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-naphthol]], and NADP+, whereas its 4 products are [[(+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-3,4-dihydro-1(2H)-]], naphthalenone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (+/−)-5-[(tert-butylamino)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1-n aphthol:NADP+ oxidoreductase. This enzyme is also termed bunolol reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrokaempferol%204-reductase | In enzymology, a dihydrokaempferol 4-reductase () is an enzyme that catalyzes the chemical reaction
cis-3,4-leucopelargonidin + NADP+ (+)-dihydrokaempferol + NADPH + H+
Thus, the two substrates of this enzyme are cis-3,4-leucopelargonidin and NADP+, whereas its 3 products are (+)-dihydrokaempferol, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-3,4-leucopelargonidin:NADP+ 4-oxidoreductase. Other names in common use include dihydroflavanol 4-reductase (DFR), dihydromyricetin reductase, NADPH-dihydromyricetin reductase, and dihydroquercetin reductase. This enzyme participates in flavonoid biosynthesis.
Function
Anthocyanidins, common plant pigments, are further reduced by the enzyme dihydroflavonol 4-reductase (DFR) to the corresponding colorless leucoanthocyanidins.
DFR uses dihydromyricetin (ampelopsin) NADPH and 2 H+ to produce leucodelphinidin and NADP.
A cDNA for DFR has been cloned from the orchid Bromheadia finlaysoniana.
Researchers in Japan have genetically manipulated roses by using RNA interference to knock out endogenous DFR, adding a gene DFR from an iris, and adding a gene for the blue pigment, delphinidin, in an effort to create a blue rose, which is being sold worldwide.
Dihydroflavonol 4-reductase is an enzyme part of the lignin biosynthesis pathway. In Arabidopsis thaliana, the enzyme uses sinap |
https://en.wikipedia.org/wiki/Diiodophenylpyruvate%20reductase | In enzymology, a diiodophenylpyruvate reductase () is an enzyme that catalyzes the chemical reaction
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+
Thus, the two substrates of this enzyme are 3-(3,5-diiodo-4-hydroxyphenyl)lactate and NAD+, whereas its 3 products are 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase. Other names in common use include aromatic alpha-keto acid, KAR, and 2-oxo acid reductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dimethylmalate%20dehydrogenase | In enzymology, a dimethylmalate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-3,3-dimethylmalate + NAD+ 3-methyl-2-oxobutanoate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-3,3-dimethylmalate and NAD+, whereas its 3 products are 3-methyl-2-oxobutanoate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating). This enzyme is also called beta,beta-dimethylmalate dehydrogenase. This enzyme participates in pantothenate and coa biosynthesis. It has 5 cofactors: ammonia, manganese, cobalt, potassium, and NH4+.
References
EC 1.1.1
NADH-dependent enzymes
Manganese enzymes
Cobalt enzymes
Potassium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-malate%20dehydrogenase%20%28decarboxylating%29 | In enzymology, a D-malate dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
(R)-malate + NAD+ pyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). This enzyme participates in butanoate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-pinitol%20dehydrogenase | In enzymology, a D-pinitol dehydrogenase () is an enzyme that catalyzes the chemical reaction
1D-3-O-methyl-chiro-inositol + NADP+ 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+
Thus, the two substrates of this enzyme are 1D-3-O-methyl-chiro-inositol and NADP+, whereas its 3 products are 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase. This enzyme is also called 5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-dehydro-6-deoxyglucose%20reductase | In enzymology, a dTDP-4-dehydro-6-deoxyglucose reductase () is an enzyme that catalyzes the chemical reaction
dTDP-D-fucose + NADP+ dTDP-4-dehydro-6-deoxy-D-glucose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-D-fucose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-D-glucose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-D-fucose:NADP+ oxidoreductase. This enzyme is also called dTDP-4-keto-6-deoxyglucose reductase. This enzyme participates in polyketide sugar unit biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-4-dehydrorhamnose%20reductase | In enzymology, a dTDP-4-dehydrorhamnose reductase () is an enzyme that catalyzes the chemical reaction
dTDP-6-deoxy-L-mannose + NADP+ dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-6-deoxy-L-mannose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-L-mannose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase. Other names in common use include dTDP-4-keto-L-rhamnose reductase, reductase, thymidine diphospho-4-ketorhamnose, dTDP-4-ketorhamnose reductase, TDP-4-keto-rhamnose reductase, and thymidine diphospho-4-ketorhamnose reductase. This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/DTDP-6-deoxy-L-talose%204-dehydrogenase | In enzymology, a dTDP-6-deoxy-L-talose 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
dTDP-6-deoxy-L-talose + NADP+ dTDP-4-dehydro-6-deoxy-L-mannose + NADPH + H+
Thus, the two substrates of this enzyme are dTDP-6-deoxy-L-talose and NADP+, whereas its 3 products are dTDP-4-dehydro-6-deoxy-L-mannose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase. Other names in common use include thymidine diphospho-6-deoxy-L-talose dehydrogenase, TDP-6-deoxy-L-talose dehydrogenase, thymidine diphospho-6-deoxy-L-talose dehydrogenase, and dTDP-6-deoxy-L-talose dehydrogenase (4-reductase). This enzyme participates in nucleotide sugars metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DTDP-galactose%206-dehydrogenase | In enzymology, a dTDP-galactose 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
dTDP-D-galactose + 2 NADP+ + H2O dTDP-D-galacturonate + 2 NADPH + 2 H+
The 3 substrates of this enzyme are dTDP-D-galactose, NADP+, and H2O, whereas its 3 products are dTDP-D-galacturonate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dTDP-D-galactose:NADP+ 6-oxidoreductase. This enzyme is also called thymidine-diphosphate-galactose dehydrogenase. This enzyme participates in nucleotide sugars metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-threo-aldose%201-dehydrogenase | In enzymology, a D-threo-aldose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
a D-threo-aldose + NAD+ a D-threo-aldono-1,5-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-threo-aldose and NAD+, whereas its 3 products are D-threo-aldono-1,5-lactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-threo-aldose:NAD+ 1-oxidoreductase. Other names in common use include L-fucose dehydrogenase, (2S,3R)-aldose dehydrogenase, dehydrogenase, L-fucose, and L-fucose (D-arabinose) dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-xylose%201-dehydrogenase | In enzymology, a D-xylose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-xylose + NAD+ D-xylonolactone + NADH + H+
Thus, the two substrates of this enzyme are D-xylose and NAD+, whereas its 3 products are D-xylonolactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-xylose:NAD+ 1-oxidoreductase. Other names in common use include NAD+-D-xylose dehydrogenase, D-xylose dehydrogenase, and (NAD+)-linked D-xylose dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-xylose%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:D-xylose 1-dehydrogenase (NADP+)}}
In enzymology, a D-xylose 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-xylose + NADP+ D-xylono-1,5-lactone + NADPH + H+
Thus, the two substrates of this enzyme are D-xylose and NADP+, whereas its 3 products are D-xylono-1,5-lactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-xylose:NADP+ 1-oxidoreductase. Other names in common use include D-xylose (nicotinamide adenine dinucleotide phosphate), dehydrogenase, D-xylose-NADP+ dehydrogenase, D-xylose:NADP+ oxidoreductase, and D-xylose 1-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-xylulose%20reductase | In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that is classified as an Oxidoreductase (EC 1) specifically acting on the CH-OH group of donors (EC 1.1.1) that uses NAD+ or NADP+ as an acceptor (EC 1.1.1.9). This enzyme participates in pentose and glucuronate interconversions; a set of metabolic pathways that involve converting pentose sugars and glucuronate into other compounds.
Nomenclature
The systematic name of this enzyme class is xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming). Other common names used include :
NAD+-dependent xylitol dehydrogenase
xylitol dehydrogenase* erythritol dehydrogenase (as this enzyme also acts as an L-erythrylose reductase)
2,3-cis-polyol(DPN) dehydrogenase (C3-5)
pentitol-DPN dehydrogenase, and
xylitol-2-dehydrogenase
EC number
An Enzyme Commission (EC) number is a classification identifier given to all enzymes that helps identify their function and relationships to other enzymes. The EC number for D-xylulose reductase is 1.1.1.9, the breakdown is as follows:
EC 1: Oxidoreductase enzymes
EC 1.1.1: An oxidoreductase enzyme that acts on CH-OH group of donors
EC 1.1.1.9: An oxidoreductase enzyme that acts on the CH-OH group of donors that uses NAD+ or NADP+ as an acceptor
Catalyzed reaction
D-xylulose reductase catalyzes the chemical reaction
xylitol + NAD+ ⇌ D-xylulose + NADH + H+
where xylitol and NAD are the substrates and D-xylulose, NADH and H+ are the products.
NAD+ acts as the coenzyme for the chem |
https://en.wikipedia.org/wiki/Erythrulose%20reductase | In enzymology, an erythrulose reductase () is an enzyme that catalyzes the chemical reaction
erythritol + NADP+ D-erythrulose + NADPH + H+
Thus, the two substrates of this enzyme are erythritol and NADP+, whereas its 3 products are D-erythrulose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is erythritol:NADP+ oxidoreductase. This enzyme is also called D-erythrulose reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Farnesol%20dehydrogenase | In enzymology, a farnesol dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-trans,6-trans-farnesol + NADP+ 2-trans,6-trans-farnesal + NADPH + H+
Thus, the two substrates of this enzyme are 2-trans,6-trans-farnesol and NADP+, whereas its 3 products are 2-trans,6-trans-farnesal, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-trans,6-trans-farnesol:NADP+ 1-oxidoreductase. Other names in common use include NADP+-farnesol dehydrogenase, and farnesol (nicotinamide adenine dinucleotide phosphate) dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Flavanone%204-reductase | In enzymology, a flavanone 4-reductase () is an enzyme that catalyzes the chemical reaction
(2S)-flavan-4-ol + NADP+ (2S)-flavanone + NADPH + H+
Thus, the two substrates of this enzyme are (2S)-flavan-4-ol and NADP+, whereas its 3 products are (2S)-flavanone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2S)-flavan-4-ol:NADP+ 4-oxidoreductase. This enzyme participates in flavonoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure
Flavanones metabolism |
https://en.wikipedia.org/wiki/Fluoren-9-ol%20dehydrogenase | In enzymology, a fluoren-9-ol dehydrogenase () is an enzyme that catalyzes the chemical reaction
fluoren-9-ol + 2 NAD(P)+ fluoren-9-one + 2 NAD(P)H + 2 H+
The 3 substrates of this enzyme are fluoren-9-ol, NAD+, and NADP+, whereas its 4 products are fluoren-9-one, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is fluoren-9-ol:NAD(P)+ oxidoreductase. This enzyme participates in fluorene degradation.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fructose%205-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Fructose 5-dehydrogenase (NADP+)}}
In enzymology, a fructose 5-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-fructose + NADP+ 5-dehydro-D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are D-fructose and NADP+, whereas its 3 products are 5-dehydro-D-fructose, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-fructose:NADP+ 5-oxidoreductase. Other names in common use include 5-ketofructose reductase (NADP+), 5-keto-D-fructose reductase (NADP+), fructose 5-(nicotinamide adenine dinucleotide phosphate), dehydrogenase, D-(-)fructose:(NADP+) 5-oxidoreductase, and fructose 5-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-arabinose%201-dehydrogenase%20%28NAD%28P%29%2B%29 | {{DISPLAYTITLE:D-arabinose 1-dehydrogenase (NAD(P)+)}}
In enzymology, a D-arabinose 1-dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
D-arabinose + NAD(P)+ D-arabinono-1,4-lactone + NAD(P)H + H+
The 3 substrates of this enzyme are D-arabinose, NAD+, and NADP+, whereas its 4 products are D-arabinono-1,4-lactone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-arabinose:NAD(P)+ 1-oxidoreductase. This enzyme is also called D-arabinose 1-dehydrogenase [NAD(P)+].
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Fructuronate%20reductase | In enzymology, a fructuronate reductase () is an enzyme that catalyzes the chemical reaction
D-mannonate + NAD+ D-fructuronate + NADH + H+
Thus, the two substrates of this enzyme are D-mannonate and NAD+, whereas its 3 products are D-fructuronate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-mannonate:NAD+ 5-oxidoreductase. Other names in common use include mannonate oxidoreductase, mannonic dehydrogenase, D-mannonate dehydrogenase, and D-mannonate:NAD+ oxidoreductase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactitol-1-phosphate%205-dehydrogenase | In enzymology, a galactitol-1-phosphate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
galactitol-1-phosphate + NAD+ L-tagatose 6-phosphate + NADH + H+
Thus, the two substrates of this enzyme are galactitol-1-phosphate and NAD+, whereas its 3 products are L-tagatose 6-phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is galactitol-1-phosphate:NAD+ oxidoreductase. This enzyme participates in galactose metabolism. It employs one cofactor, zinc.
References
EC 1.1.1
NADH-dependent enzymes
Zinc enzymes
Enzymes of unknown structure
Protein families |
https://en.wikipedia.org/wiki/Galactitol%202-dehydrogenase | In enzymology, a galactitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
galactitol + NAD+ D-tagatose + NADH + H+
Thus, the two substrates of this enzyme are galactitol and NAD+, whereas its 3 products are D-tagatose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is galactitol:NAD+ 2-oxidoreductase. This enzyme is also called dulcitol dehydrogenase. This enzyme participates in galactose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Galactose%201-dehydrogenase | In enzymology, a galactose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-galactose + NAD+ D-galactono-1,4-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-galactose:NAD+ 1-oxidoreductase. Other names in common use include D-galactose dehydrogenase, beta-galactose dehydrogenase, and NAD+-dependent D-galactose dehydrogenase. This enzyme participates in galactose metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactose%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Galactose 1-dehydrogenase (NADP+)}}
In enzymology, a galactose 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-galactose + NADP+ D-galactonolactone + NADPH + H+
Thus, the two substrates of this enzyme are D-galactose and NADP+, whereas its 3 products are D-galactonolactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-galactose:NADP+ 1-oxidoreductase. Other names in common use include D-galactose dehydrogenase (NADP+), and galactose 1-dehydrogenase (NADP+). This enzyme participates in galactose metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-4-dehydro-6-deoxy-D-mannose%20reductase | In enzymology, a GDP-4-dehydro-6-deoxy-D-mannose reductase () is an enzyme that catalyzes the chemical reaction
GDP-6-deoxy-D-mannose + NAD(P)+ GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+
The 3 substrates of this enzyme are GDP-6-deoxy-D-mannose, NAD+, and NADP+, whereas its 4 products are GDP-4-dehydro-6-deoxy-D-mannose, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase (D-rhamnose-forming). Other names in common use include GDP-4-keto-6-deoxy-D-mannose reductase [ambiguous], GDP-6-deoxy-D-lyxo-4-hexulose reductase, and Rmd. This enzyme participates in fructose and mannose metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alcohol%20dehydrogenase%20%28NAD%28P%29%2B%29 | {{DISPLAYTITLE:Alcohol dehydrogenase (NAD(P)+)}}
In enzymology, an alcohol dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
an alcohol + NAD(P)+ an aldehyde + NAD(P)H + H+
The 3 substrates of this enzyme are alcohol, NAD+, and NADP+, whereas its 4 products are aldehyde, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is alcohol:NAD(P)+ oxidoreductase. Other names in common use include retinal reductase, aldehyde reductase (NADPH/NADH), and alcohol dehydrogenase [NAD(P)]. This enzyme participates in glycolysis and gluconeogenesis.
See also
Alcohol dehydrogenase
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-4-dehydro-D-rhamnose%20reductase | In enzymology, a GDP-4-dehydro-D-rhamnose reductase () is an enzyme that catalyzes the chemical reaction
GDP-6-deoxy-D-mannose + NAD(P)+ GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+
The 3 substrates of this enzyme are GDP-6-deoxy-D-mannose, NAD+, and NADP+, whereas its 4 products are GDP-4-dehydro-6-deoxy-D-mannose, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-6-deoxy-D-mannose:NAD(P)+ 4-oxidoreductase. Other names in common use include GDP-4-keto-6-deoxy-D-mannose reductase, GDP-4-keto-D-rhamnose reductase, and guanosine diphosphate-4-keto-D-rhamnose reductase. This enzyme participates in fructose and mannose metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-6-deoxy-D-talose%204-dehydrogenase | In enzymology, a GDP-6-deoxy-D-talose 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
GDP-6-deoxy-D-talose + NAD(P)+ GDP-4-dehydro-6-deoxy-D-mannose + NAD(P)H + H+
The 3 substrates of this enzyme are GDP-6-deoxy-D-talose, NAD+, and NADP+, whereas its 4 products are GDP-4-dehydro-6-deoxy-D-mannose, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase. This enzyme is also called guanosine diphospho-6-deoxy-D-talose dehydrogenase. This enzyme participates in fructose and mannose metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homoserine%20dehydrogenase | In enzymology, a homoserine dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-homoserine + NAD(P)+ L-aspartate 4-semialdehyde + NAD(P)H + H+
The 2 substrates of this enzyme are L-homoserine and NAD+ (or NADP+), whereas its 3 products are L-aspartate 4-semialdehyde, NADH (or NADPH), and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-homoserine:NAD(P)+ oxidoreductase. Other names in common use include HSDH, and HSD.
Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta-semialdehyde into homoserine. Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and methionine.
Enzyme structure
The enzyme can be found in a monofunctional form, in some bacteria and yeast. Structural analysis of the yeast monofunctional enzyme indicates that the enzyme is a dimer composed of three distinct regions; an N-terminal nucleotide-binding domain, a short central dimerisation region, and a C-terminal catalytic domain. The N-terminal domain forms a modified Rossmann fold, while the catalytic domain forms a novel alpha-beta mixed sheet.
The enzyme can also be found in a bifunctional form consisting of an N-terminal aspartokinase domain and a C-terminal homoserine dehydrogenase domain, as found in bacteria such as Escherichia coli and in plants |
https://en.wikipedia.org/wiki/GDP-L-fucose%20synthase | In enzymology, a GDP-L-fucose synthase () is an enzyme that catalyzes the chemical reaction
GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+ GDP-L-fucose + NADP+
Thus, the three substrates of this enzyme are GDP-4-dehydro-6-deoxy-D-mannose, NADPH, and H+, whereas its two products are GDP-L-fucose and NADP+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing). This enzyme is also called GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase. This enzyme participates in fructose and mannose metabolism.
Relevance in diseases
It has been reported that some cases of multiple sclerosis that present the HLA variant DRB3, present also autoimmunity against GDP-L-fucose synthase. The same report points out that the autoimmune problem could derive from the gut microbiota.
See also
Guanosine diphosphate
Guanosine diphosphate mannose
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GDP-mannose%206-dehydrogenase | In enzymology, a GDP-mannose 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
GDP-D-mannose + 2 NAD+ + H2O GDP-D-mannuronate + 2 NADH + 2 H+
The 3 substrates of this enzyme are GDP-D-mannose, NAD+, and H2O, whereas its 3 products are GDP-D-mannuronate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is GDP-D-mannose:NAD+ 6-oxidoreductase. Other names in common use include guanosine diphosphomannose dehydrogenase, GDP-mannose dehydrogenase, guanosine diphosphomannose dehydrogenase, and guanosine diphospho-D-mannose dehydrogenase. This enzyme participates in fructose and mannose metabolism.
This protein may use the morpheein model of allosteric regulation.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
Further reading
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28R%2CR%29-butanediol%20dehydrogenase | In enzymology, a (R,R)-butanediol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R,R)-butane-2,3-diol + NAD (R)-acetoin + NADH + H
Thus, the two substrates of this enzyme are (R,R)-butane-2,3-diol and NAD, whereas its 3 products are (R)-acetoin, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R,R)-butane-2,3-diol:NAD oxidoreductase. Other names in common use include butyleneglycol dehydrogenase, D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D-aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD oxidoreductase, 1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism.
References
EC 1.1.1
NADH-dependent enzymes |
https://en.wikipedia.org/wiki/Geraniol%20dehydrogenase | In enzymology, a geraniol dehydrogenase () is an enzyme that catalyzes the chemical reaction
geraniol + NADP+ geranial + NADPH + H+
Thus, the two substrates of this enzyme are geraniol and NADP+, whereas its 3 products are geranial, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geraniol:NADP+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol%20dehydrogenase | Glycerol dehydrogenase (, also known as NAD+-linked glycerol dehydrogenase, glycerol: NAD+ 2-oxidoreductase, GDH, GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone). This enzyme is an oxidoreductase, specifically a metal-dependent alcohol dehydrogenase that plays a role in anaerobic glycerol metabolism and has been isolated from a number of bacteria, including Enterobacter aerogenes, Klebsiella aerogenes, Streptococcus faecalis, Erwinia aeroidea, Bacillus megaterium, and Bacillus stearothermophilus. However, most studies of glycerol dehydrogenase have been performed in Bacillus stearothermophilus, (B. stearothermophilus) due to its thermostability and the following structural and functional information will, therefore, refer primarily to the characterization of the enzyme in this bacterium.
Structure
Glycerol dehydrogenase is a homooctamer composed of eight identical monomer subunits made up of a single polypeptide chain of 370 amino acids (molecular weight 42,000 Da). Each subunit contains 9 beta sheets and 14 alpha helices within two distinct domains (N-terminal, residues 1-162 and C-terminal, residues 163-370). The deep cleft formed between these two domains serves as the enzyme’s active site. This active site consists of one bound metal ion, one NAD+ nicotinamide ring binding site, and a substrate binding site.
Research into the structure of B. stearothermophilus shows |
https://en.wikipedia.org/wiki/Gluconate%202-dehydrogenase | In enzymology, a gluconate 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-gluconate + NADP+ 2-dehydro-D-gluconate + NADPH + H+
Thus, the two substrates of this enzyme are D-gluconate and NADP+, whereas its 3 products are 2-dehydro-D-gluconate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-gluconate:NADP+ oxidoreductase. Other names in common use include 2-keto-D-gluconate reductase, and 2-ketogluconate reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Propanediol-phosphate%20dehydrogenase | In enzymology, a propanediol-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
propane-1,2-diol 1-phosphate + NAD+ hydroxyacetone phosphate + NADH + H+
Thus, the two substrates of this enzyme are propane-1,2-diol 1-phosphate and NAD+, whereas its 3 products are hydroxyacetone phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is propane-1,2-diol-1-phosphate:NAD+ oxidoreductase. Other names in common use include PDP dehydrogenase, 1,2-propanediol-1-phosphate:NAD+ oxidoreductase, and propanediol phosphate dehydrogenase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gluconate%205-dehydrogenase | In enzymology, a gluconate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-gluconate + NAD(P)+ 5-dehydro-D-gluconate + NAD(P)H + H+
The 3 substrates of this enzyme are D-gluconate, NAD+, and NADP+, whereas its 4 products are 5-dehydro-D-gluconate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-gluconate:NAD(P)+ 5-oxidoreductase. Other names in common use include 5-keto-D-gluconate 5-reductase, 5-keto-D-gluconate 5-reductase, 5-ketogluconate 5-reductase, 5-ketogluconate reductase, and 5-keto-D-gluconate reductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose%201-dehydrogenase | In enzymology, a glucose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
beta-D-glucose + NAD(P)+ D-glucono-1,5-lactone + NAD(P)H + H+
The 3 substrates of this enzyme are beta-D-glucose, NAD+, and NADP+, whereas its 4 products are D-glucono-1,5-lactone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is beta-D-glucose:NAD(P)+ 1-oxidoreductase. Another name in common use is D-glucose dehydrogenase (NAD(P)+).
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose%201-dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:Glucose 1-dehydrogenase (NAD+)}}
In enzymology, a glucose 1-dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
D-glucose + NAD+ D-glucono-1,5-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-glucose and NAD+, whereas its 3 products are D-glucono-1,5-lactone, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glucose:NAD+ 1-oxidoreductase. Other names in common use include D-glucose:NAD+ oxidoreductase, D-aldohexose dehydrogenase, and glucose 1-dehydrogenase (NAD+).
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Glucose 1-dehydrogenase (NADP+)}}
In enzymology, a glucose 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-glucose + NADP+ D-glucono-1,5-lactone + NADPH + H+
Thus, the two substrates of this enzyme are D-glucose and NADP+, whereas its 3 products are D-glucono-1,5-lactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glucose:NADP+ 1-oxidoreductase. Other names in common use include nicotinamide adenine dinucleotide phosphate-linked aldohexose, dehydrogenase, NADP+-linked aldohexose dehydrogenase, NADP+-dependent glucose dehydrogenase, and glucose 1-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucuronate%20reductase | In enzymology, a glucuronate reductase () is an enzyme that catalyzes the chemical reaction
L-gulonate + NADP+ D-glucuronate + NADPH + H+
Thus, the two substrates of this enzyme are L-gulonate and NADP+, whereas its 3 products are D-glucuronate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-gulonate:NADP+ 6-oxidoreductase. Other names in common use include aldehyde reductase, L-hexonate:NADP dehydrogenase, TPN-L-gulonate dehydrogenase, aldehyde reductase II, NADP-L-gulonate dehydrogenase, D-glucuronate dehydrogenase, D-glucuronate reductase, and L-glucuronate reductase (incorrect). This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
Jakoby, W. B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, p. 249–260.
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucuronolactone%20reductase | In enzymology, a glucuronolactone reductase () is an enzyme that catalyzes the chemical reaction
L-gulono-1,4-lactone + NADP+ D-glucurono-3,6-lactone + NADPH + H+
Thus, the two substrates of this enzyme are L-gulono-1,4-lactone and NADP+, whereas its 3 products are D-glucurono-3,6-lactone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-gulono-1,4-lactone:NADP+ 1-oxidoreductase. Other names in common use include GRase, and gulonolactone dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerate%20dehydrogenase | In enzymology, a glycerate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(D)-glycerate + NAD+ hydroxypyruvate + NADH + H+
Thus, the two substrates of this enzyme are (R)-glycerate and NAD+, whereas its 3 products are hydroxypyruvate, NADH, and H+. However, in nature these enzymes have the ability to catalyze the reverse reaction as well. That is, hydroxypyruvate, NADH, and H+ can act as the substrates while (R)-glycerate and NAD+ are formed as products. Additionally, NADPH can take the place of NADH in this reaction.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-glycerate:NAD+ oxidoreductase. Other names in common use include D-glycerate dehydrogenase, and hydroxypyruvate reductase (due to the reversibility of the reaction). This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.
Enzyme structure
This class of enzyme is part of a larger superfamily of enzymes known as D-2-hydroxy-acid dehydrogenases.
Many organisms from Hyphomicrobium methylovorum to humans have some form of the glycerate dehydrogenase protein. There are currently several structures that have been solved for this class of enzyme including those for the two mentioned above with PDB access code , D-glycerate dehydrogenase, and the human homolog Glyoxylate reductase/Hydroxypyruvate reduct |
https://en.wikipedia.org/wiki/Sn-glycerol-1-phosphate%20dehydrogenase | In enzymology, a sn-glycerol-1-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
sn-glycerol 1-phosphate + NAD(P)+ glycerone phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are sn-glycerol 1-phosphate, NAD+, and NADP+, whereas its 4 products are glycerone phosphate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase. This enzyme is also called glycerol-1-phosphate dehydrogenase [NAD(P)+].
G-1-P dehydrogenase is responsible for the formation of sn-glycerol 1-phosphate, the backbone of the membrane phospholipids of Archaea. The gene encoding glycerol-1-phosphate dehydrogenase has been detected in all the archaeal species and has not been found in any bacterial or eukaryal species. sn-glycerol 1-phosphate produced by this enzyme is the most fundamental difference by which Archaea and bacteria are discriminated.
The enzyme sn-glycerol-1-phosphate dehydrogenase, usually having 394 amino acids, was also identified in bacteria. More than 5700 sequences have been published in GenBank (September 2023) in a different bacteria, including such well-known ones as Bacillus subtilis (GenBank: AOR99168.1).
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol%202-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Glycerol 2-dehydrogenase (NADP+)}}
In enzymology, a glycerol 2-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
glycerol + NADP+ glycerone + NADPH + H+
Thus, the two substrates of this enzyme are glycerol and NADP+, whereas its 3 products are glycerone, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ 2-oxidoreductase (glycerone-forming). Other names in common use include dihydroxyacetone reductase, dihydroxyacetone (reduced nicotinamide adenine dinucleotide, phosphate) reductase, dihydroxyacetone reductase (NADPH), DHA oxidoreductase, and glycerol 2-dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Glycerol-3-phosphate 1-dehydrogenase (NADP+)}}
In enzymology, a glycerol-3-phosphate 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + NADP+ D-glyceraldehyde 3-phosphate + NADPH + H+
Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and NADP+, whereas its 3 products are D-glyceraldehyde 3-phosphate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:NADP+ 1-oxidoreductase. Other names in common use include glycerol phosphate (nicotinamide adenine dinucleotide phosphate), dehydrogenase, L-glycerol 3-phosphate:NADP+ oxidoreductase, glycerin-3-phosphate dehydrogenase, NADPH-dependent glycerin-3-phosphate dehydrogenase, and glycerol-3-phosphate 1-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:Glycerol-3-phosphate dehydrogenase (NAD+)}}
In enzymology, a glycerol-3-phosphate dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + NAD+ glycerone phosphate + NADH + H+
The two substrates of this enzyme are sn-glycerol 3-phosphate and NAD+, whereas its 3 products are glycerone phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase. Other names in common use include alpha-glycerol phosphate dehydrogenase (NAD+), alpha-glycerophosphate dehydrogenase (NAD+), glycerol 1-phosphate dehydrogenase, glycerol phosphate dehydrogenase (NAD+), glycerophosphate dehydrogenase (NAD+), hydroglycerophosphate dehydrogenase, L-alpha-glycerol phosphate dehydrogenase, L-alpha-glycerophosphate dehydrogenase, L-glycerol phosphate dehydrogenase, L-glycerophosphate dehydrogenase, NAD+-alpha-glycerophosphate dehydrogenase, NAD+-dependent glycerol phosphate dehydrogenase, NAD+-dependent glycerol-3-phosphate dehydrogenase, NAD+-L-glycerol-3-phosphate dehydrogenase, NAD+-linked glycerol 3-phosphate dehydrogenase, NADH-dihydroxyacetone phosphate reductase, and glycerol-3-phosphate dehydrogenase (NAD+). This enzyme participates in glycerophospholipid metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this cla |
https://en.wikipedia.org/wiki/Glycerol%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Glycerol dehydrogenase (NADP+)}}
In enzymology, a glycerol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
glycerol + NADP+ D-glyceraldehyde + NADPH + H+
Thus, the two substrates of this enzyme are glycerol and NADP+, whereas its 3 products are D-glyceraldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ oxidoreductase. This enzyme is also called glycerol dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glyoxylate%20reductase | Glyoxylate reductase (), first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH.
The systematic name of this enzyme class is glycolate:NAD+ oxidoreductase. Other names in common use include NADH-glyoxylate reductase, glyoxylic acid reductase, and NADH-dependent glyoxylate reductase.
Structure
The crystal structure of the glyoxylate reductase enzyme from the hyperthermophilic archeon Pyrococcus horiskoshii OT3 has been reported. The enzyme exists in the dimeric form. Each monomer has two domains: a substrate-binding domain where glyoxylate binds, and a nucleotide-binding domain where the NAD(P)H cofactor binds.
Mechanism
The enzyme catalyzes the transfer of a hydride from NAD(P)H to glyoxylate, causing a reduction of the substrate to glycolate and an oxidation of the cofactor to NAD(P)+. Figure 2 shows the mechanism for this reaction.
It is thought that the two residues Glu270 and His288 are important for the enzyme's catalytic function, while the residue Arg241 is thought to be important for substrate specificity.
Function
The glyoxylate reductase enzyme localizes to the cell cytoplasm in plants. It can use both NADPH and NADH as a cofactor, but prefers NADPH. The enzyme substrate, glyoxylate, is a metabolite in plant photorespiration, and is produced in the peroxisome. Glyoxylate is important in the plant cell as it can deactivate RUBISCO and inhibit its activation. Hence, glyoxyla |
https://en.wikipedia.org/wiki/Glyoxylate%20reductase%20%28NADP%2B%29 | {{DISPLAYTITLE:Glyoxylate reductase (NADP+)}}
In enzymology, a glyoxylate reductase (NADP+) () is an enzyme that catalyzes the chemical reaction
glycolate + NADP+ glyoxylate + NADPH + H+
Thus, the two substrates of this enzyme are glycolate and NADP+, whereas its 3 products are glyoxylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolate:NADP+ oxidoreductase. Other names in common use include NADPH-glyoxylate reductase, and glyoxylate reductase (NADP+). This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hexadecanol%20dehydrogenase | In enzymology, a hexadecanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
hexadecanol + NAD+ hexadecanal + NADH + H+
Thus, the two substrates of this enzyme are hexadecanol and NAD+, whereas its 3 products are hexadecanal, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanol:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Histidinol%20dehydrogenase | In enzymology, histidinol dehydrogenase (HIS4) (HDH) () is an enzyme that catalyzes the chemical reaction
L-histidinol + 2 NAD+ L-histidine + 2 NADH + 2 H+
Thus, the two substrates of this enzyme are L-histidinol and NAD+, whereas its 3 products are L-histidine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD+ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase.
Structure
In bacteria, HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyses three different steps of histidine biosynthesis; and in plants it is expressed as a nuclear encoded protein precursor which is exported to the chloroplast.
Active site
Histidinol is held inside the active site thanks to a zinc ion, but the zinc ion does not participate in the catalysis otherwise. The zinc ion is held in place by His262, Gln259, Asp360 and His419 (which, in homodimeric histidinol dehydrogenases, comes from the other monomer). Histidinol itself is held in place by His327 and His367 from one moment unit and Glu414 from the other monomer unit.
A Cys residue has been implicated in the catalytic mechanism of the second oxidative step. However, according to newer studies with histidinol dehydrogenase from E. coli, the mechanism is catalyzed by four bases, B1-B4. His327 acts as the |
https://en.wikipedia.org/wiki/Homoisocitrate%20dehydrogenase | In enzymology, a homoisocitrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ 2-oxoadipate + CO2 + NADH + H+
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroxycyclohexanecarboxylate%20dehydrogenase | In enzymology, a hydroxycyclohexanecarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+
Thus, the two substrates of this enzyme are (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate and NAD+, whereas its 3 products are (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ 3-oxidoreductase. Other names in common use include dihydroxycyclohexanecarboxylate dehydrogenase, and (−)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/W95 | W95 may refer to:
Ocracoke Island Airport, in Hyde County, North Carolina, United States
Truncated great icosahedron
Windows 95, an operating system
W95, a classification in masters athletics |
https://en.wikipedia.org/wiki/Hydroxymalonate%20dehydrogenase | In enzymology, a hydroxymalonate dehydrogenase () is an enzyme that catalyzes the chemical reaction
hydroxymalonate + NAD+ oxomalonate + NADH + H+
Thus, the two substrates of this enzyme are hydroxymalonate and NAD+, whereas its 3 products are oxomalonate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydroxymalonate:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA%20reductase%20%28NADPH%29 | In enzymology, a hydroxymethylglutaryl-CoA reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(R)-mevalonate + CoA + 2 NADP+ (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
The 3 substrates of this enzyme are (R)-mevalonate, CoA, and NADP+, whereas its 3 products are (S)-3-hydroxy-3-methylglutaryl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in biosynthesis of steroids including cholesterol. The statin class of anticholesterol drugs act through inhibiting this enzyme.
Nomenclature
The systematic name of this enzyme class is (R)-mevalonate:NADP+ oxidoreductase (CoA-acylating). Other names in common use include:
hydroxymethylglutaryl coenzyme A reductase (reduced nicotinamide
adenine dinucleotide phosphate), 3-hydroxy-3-methylglutaryl-CoA reductase
β-hydroxy-β-methylglutaryl coenzyme A reductase
hydroxymethylglutaryl CoA reductase (NADPH)
S-3-hydroxy-3-methylglutaryl-CoA reductase
NADPH-hydroxymethylglutaryl-CoA reductase
HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating-CoA)
3-hydroxy-3-methylglutaryl CoA reductase (NADPH)
hydroxymethylglutaryl-CoA reductase (NADPH2).
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known stru |
https://en.wikipedia.org/wiki/Hydroxyphenylpyruvate%20reductase | In enzymology, a hydroxyphenylpyruvate reductase () is an enzyme that catalyzes the chemical reaction
3-(4-hydroxyphenyl)lactate + NAD+ 3-(4-hydroxyphenyl)pyruvate + NADH + H+
Thus, the two substrates of this enzyme are 3-(4-hydroxyphenyl)lactate and NAD+, whereas its 3 products are 3-(4-hydroxyphenyl)pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxyphenyllactate:NAD+ oxidoreductase. This enzyme is also called HPRP. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Hydroxypyruvate%20reductase | In enzymology, a hydroxypyruvate reductase () is an enzyme that catalyzes the chemical reaction
D-glycerate + NAD(P)+ hydroxypyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are D-glycerate, NAD+, and NADP+, whereas its 4 products are hydroxypyruvate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glycerate:NADP+ 2-oxidoreductase. Other names in common use include beta-hydroxypyruvate reductase, NADH:hydroxypyruvate reductase, and D-glycerate dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.
See also
Oxidoreductases
Enzymes
Enzyme Commission number (EC number)
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Indanol%20dehydrogenase | In enzymology, an indanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
indan-1-ol + NAD(P)+ indanone + NAD(P)H + H+
The 3 substrates of this enzyme are indan-1-ol, NAD+, and NADP+, whereas its 4 products are indanone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is indan-1-ol:NAD(P)+ 1-oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indole-3-acetaldehyde%20reductase%20%28NADH%29 | In enzymology, an indole-3-acetaldehyde reductase (NADH) () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)ethanol + NAD+ (indol-3-yl)acetaldehyde + NADH + H+
Thus, the two substrates of this enzyme are (indol-3-yl)ethanol and NAD+, whereas its 3 products are (indol-3-yl)acetaldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (indol-3-yl)ethanol:NAD+ oxidoreductase. Other names in common use include indoleacetaldehyde reductase, indole-3-acetaldehyde reductase (NADH), and indole-3-ethanol:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
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