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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 |
https://en.wikipedia.org/wiki/Indole-3-acetaldehyde%20reductase%20%28NADPH%29 | In enzymology, an indole-3-acetaldehyde reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)ethanol + NADP+ (indol-3-yl)acetaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are (indol-3-yl)ethanol and NADP+, whereas its 3 products are (indol-3-yl)acetaldehyde, 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 (indol-3-yl)ethanol:NADP+ oxidoreductase. Other names in common use include indoleacetaldehyde (reduced nicotinamide adenine dinucleotide, phosphate) reductase, indole-3-acetaldehyde reductase (NADPH), and indole-3-ethanol:NADP+ oxidoreductase. This enzyme participates in tryptophan metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indolelactate%20dehydrogenase | In enzymology, an indolelactate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(indol-3-yl)lactate + NAD+ (indol-3-yl)pyruvate + NADH + H+
Thus, the two substrates of this enzyme are (indol-3-yl)lactate and NAD+, whereas its 3 products are (indol-3-yl)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 (indol-3-yl)lactate:NAD+ oxidoreductase. This enzyme is also called indolelactate:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-Hydroxycyclohexanecarboxylate%20dehydrogenase | In enzymology, a 4-hydroxycyclohexanecarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
trans-4-hydroxycyclohexanecarboxylate + NAD+ 4-oxocyclohexanecarboxylate + NADH + H+
Thus, the two substrates of this enzyme are trans-4-hydroxycyclohexanecarboxylate and NAD+, whereas its 3 products are 4-oxocyclohexanecarboxylate, 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-4-hydroxycyclohexanecarboxylate:NAD+ 4-oxidoreductase. This enzyme is also called trans-4-hydroxycyclohexanecarboxylate dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol%202-dehydrogenase | In enzymology, an inositol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
myo-inositol + NAD+ 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Thus, the two substrates of this enzyme are myo-inositol and NAD+, whereas its 3 products are 2,4,6/3,5-pentahydroxycyclohexanone, 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 myo-inositol:NAD+ 2-oxidoreductase. Other names in common use include myo-inositol 2-dehydrogenase, myo-inositol:NAD+ oxidoreductase, inositol dehydrogenase, and myo-inositol dehydrogenase. This enzyme participates in inositol metabolism and inositol phosphate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-%28hydroxymethyl%29benzenesulfonate%20dehydrogenase | In enzymology, a 4-(hydroxymethyl)benzenesulfonate dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-(hydroxymethyl)benzenesulfonate + NAD+ 4-formylbenzenesulfonate + NADH + H+
Thus, the two substrates of this enzyme are 4-(hydroxymethyl)benzenesulfonate and NAD+, whereas its 3 products are 4-formylbenzenesulfonate, 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-(hydroxymethyl)benzenesulfonate:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxythreonine-4-phosphate%20dehydrogenase | In enzymology, a 4-hydroxythreonine-4-phosphate dehydrogenase () is an enzyme that catalyzes the chemical reaction
4-phosphonooxy-L-threonine + NAD+ (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+
Thus, the two substrates of this enzyme are 4-phosphonooxy-L-threonine and NAD+, whereas its 3 products are (2S)-2-amino-3-oxo-4-phosphonooxybutanoate, 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-phosphonooxy-L-threonine:NAD+ oxidoreductase. Other names in common use include NAD+-dependent threonine 4-phosphate dehydrogenase, L-threonine 4-phosphate dehydrogenase, 4-(phosphohydroxy)-L-threonine dehydrogenase, PdxA, and 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase. This enzyme participates in vitamin B6 metabolism.
Structural studies
As of late 2007, 6 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/Isopiperitenol%20dehydrogenase | In enzymology, an isopiperitenol dehydrogenase () is an enzyme that catalyzes the chemical reaction
(-)-trans-isopiperitenol + NAD+ (-)-isopiperitenone + NADH + H+
Thus, the two substrates of this enzyme are (-)-trans-isopiperitenol and NAD+, whereas its 3 products are (-)-isopiperitenone, 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-isopiperitenol:NAD+ oxidoreductase. This enzyme participates in monoterpenoid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-oxoproline%20reductase | In enzymology, a 4-oxoproline reductase () is an enzyme that catalyzes the chemical reaction
4-oxo-L-proline + NADH + H+ cis-4-hydroxy-L-proline + NAD+
Thus, the three substrates of this enzyme are 4-oxo-L-proline, NADH, and H+, whereas its two products are cis-4-hydroxy-L-proline and NAD+.
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-hydroxy-L-proline:NAD+ oxidoreductase. This enzyme is also called hydroxy-L-proline oxidase. This enzyme was originally thought to participate in the metabolism of arginine and proline. However, recent data show that it is unlikely since neither 4-oxo-L-proline nor cis-4-hydroxy-L-proline are metabolites of these metabolic pathways.
Gene
The gene encoding 4-oxo-L-proline reductase was identified as 3-hydroxybutyrate dehydrogenase 2 (BDH2) by Sebastian Kwiatkowski and co-workers in 2022. The enzyme is a member of the Short-chain Dehydrogenases/Reductases (SDR) family of enzymes.
References
Further reading
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isopropanol%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Isopropanol dehydrogenase (NADP+)}}
In enzymology, an isopropanol dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
propan-2-ol + NADP+ acetone + NADPH + H+
Thus, the two substrates of this enzyme are propan-2-ol and NADP+, whereas its 3 products are acetone, 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 propan-2-ol:NADP+ oxidoreductase. This enzyme is also called isopropanol dehydrogenase (NADP+). This enzyme participates in propanoate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Ketol-acid%20reductoisomerase | In enzymology, a ketol-acid reductoisomerase () is an enzyme that catalyzes the chemical reaction
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+ (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH + H+
Thus, the two substrates of this enzyme are (R)-2,3-dihydroxy-3-methylbutanoate and NADP+, whereas its 3 products are (S)-2-hydroxy-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 (R)-2,3-dihydroxy-3-methylbutanoate:NADP+ oxidoreductase (isomerizing). Other names in common use include dihydroxyisovalerate dehydrogenase (isomerizing), acetohydroxy acid isomeroreductase, ketol acid reductoisomerase, alpha-keto-beta-hydroxylacyl reductoisomerase, 2-hydroxy-3-keto acid reductoisomerase, acetohydroxy acid reductoisomerase, acetolactate reductoisomerase, dihydroxyisovalerate (isomerizing) dehydrogenase, isomeroreductase, and reductoisomerase. This enzyme participates in valine, leucine and isoleucine biosynthesis and pantothenate and coa 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 |
https://en.wikipedia.org/wiki/4-phosphoerythronate%20dehydrogenase | In enzymology, a 4-phosphoerythronate dehydogenase () is an enzyme that catalyzes the chemical reaction
4-phospho-D-erythronate + NAD+ (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH + H+
Thus, the two substrates of this enzyme are 4-phospho-D-erythronate and NAD+, whereas its 3 products are (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate, 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-phospho-D-erythronate:NAD+ 2-oxidoreductase. Other names in common use include PdxB, PdxB 4PE dehydrogenase, and 4-O-phosphoerythronate dehydrogenase. This enzyme participates in vitamin B6 metabolism.
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/Lactaldehyde%20reductase | In enzymology, a lactaldehyde reductase () is an enzyme that catalyzes the chemical reaction
(R)[or (S)]-propane-1,2-diol + NAD+ (R)[or (S)]-lactaldehyde + NADH + H+
The 3 substrates of this enzyme are (R)-propane-1,2-diol, (S)-propane-1,2-diol, and NAD+, whereas its 4 products are (R)-lactaldehyde, (S)-lactaldehyde, 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)[or (S)]-propane-1,2-diol:NAD+ oxidoreductase. Other names in common use include propanediol:nicotinamide adenine dinucleotide (NAD+) oxidoreductase, and L-lactaldehyde:propanediol oxidoreductase. 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
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lactaldehyde%20reductase%20%28NADPH%29 | In enzymology, a lactaldehyde reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
propane-1,2-diol + NADP+ L-lactaldehyde + NADPH + H+
Thus, the two substrates of this enzyme are 1,2-propanediol and NADP+, whereas its 3 products are L-lactaldehyde, 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 propane-1,2-diol:NADP+ oxidoreductase. Other names in common use include lactaldehyde (reduced nicotinamide adenine dinucleotide phosphate), reductase, NADP+-1,2-propanediol dehydrogenase, propanediol dehydrogenase, 1,2-propanediol:NADP+ oxidoreductase, and lactaldehyde reductase (NADPH).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-arabinitol%202-dehydrogenase | In enzymology, a L-arabinitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-arabinitol + NAD+ L-ribulose + NADH + H+
Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-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 L-arabinitol:NAD+ 2-oxidoreductase (L-ribulose-forming). Other names in common use include L-arabinitol dehydrogenase (ribulose-forming), and L-arabinitol (ribulose-forming) 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/L-arabinitol%204-dehydrogenase | In enzymology, a L-arabinitol 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-arabinitol + NAD+ L-xylulose + NADH + H+
Thus, the two substrates of this enzyme are L-arabinitol and NAD+, whereas its 3 products are L-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 L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming). Other names in common use include pentitol-DPN dehydrogenase, and L-arabitol 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/L-arabinose%201-dehydrogenase | In enzymology, a L-arabinose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-arabinose + NAD+ L-arabinono-1,4-lactone + NADH + H+
Thus, the two substrates of this enzyme are L-arabinose and NAD+, whereas its 3 products are L-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 L-arabinose:NAD+ 1-oxidoreductase. 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/L-glycol%20dehydrogenase | In enzymology, a L-glycol dehydrogenase () is an enzyme that catalyzes the chemical reaction
an L-glycol + NAD(P)+ a 2-hydroxycarbonyl compound + NAD(P)H + H+
The 3 substrates of this enzyme are L-glycol, NAD+, and NADP+, whereas its 4 products are 2-hydroxycarbonyl compound, 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 L-glycol:NAD(P)+ oxidoreductase. Other names in common use include glycol (nicotinamide adenine dinucleotide (phosphate)), dehydrogenase, L-(+)-glycol:NAD(P)+ oxidoreductase, and L-glycol:NAD(P)+ dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-gulonate%203-dehydrogenase | In enzymology, a L-gulonate 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-gulonate + NAD+ 3-dehydro-L-gulonate + NADH + H+
Thus, the two substrates of this enzyme are L-gulonate and NAD+, whereas its 3 products are 3-dehydro-L-gulonate, 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-gulonate:NAD+ 3-oxidoreductase. Other names in common use include L-3-aldonate dehydrogenase, L-3-aldonic dehydrogenase, L-gulonic acid dehydrogenase, L-beta-hydroxyacid dehydrogenase, L-beta-hydroxy-acid-NAD+-oxidoreductase, and L-3-hydroxyacid dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
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/L-iditol%202-dehydrogenase | In enzymology, a L-iditol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-iditol + NAD+ L-sorbose + NADH + H+
Thus, the two substrates of this enzyme are L-iditol and NAD+, whereas its 3 products are L-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 L-iditol:NAD+ 2-oxidoreductase. Other names in common use include polyol dehydrogenase, sorbitol dehydrogenase, L-iditol:NAD+ 5-oxidoreductase, L-iditol (sorbitol) dehydrogenase, glucitol dehydrogenase, L-iditol:NAD+ oxidoreductase, NAD+-dependent sorbitol dehydrogenase, NAD+-dependent sorbitol dehydrogenase, and NAD+-sorbitol dehydrogenase. This enzyme participates in fructose and mannose metabolism.
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
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-idonate%205-dehydrogenase | In enzymology, a L-idonate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-idonate + NAD(P)+ 5-dehydrogluconate + NAD(P)H + H+
The 3 substrates of this enzyme are L-idonate, NAD+, and NADP+, whereas its 4 products are 5-dehydrogluconate, 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 L-idonate:NAD(P)+ oxidoreductase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-alcohol%20dehydrogenase | In enzymology, a long-chain-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
a long-chain alcohol + 2 NAD+ + H2O a long-chain carboxylate + 2 NADH + 2 H+
The 3 substrates of this enzyme are long-chain alcohol, NAD+, and H2O, whereas its 3 products are long-chain 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 long-chain-alcohol:NAD+ oxidoreductase. Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This enzyme participates in fatty acid metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-rhamnose%201-dehydrogenase | In enzymology, a L-rhamnose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-rhamnofuranose + NAD+ L-rhamno-1,4-lactone + NADH + H+
Thus, the two substrates of this enzyme are L-rhamnofuranose and NAD+, whereas its 3 products are L-rhamno-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 L-rhamnofuranose:NAD+ 1-oxidoreductase. 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/L-threonate%203-dehydrogenase | In enzymology, a L-threonate 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-threonate + NAD+ 3-dehydro-L-threonate + NADH + H+
Thus, the two substrates of this enzyme are L-threonate and NAD+, whereas its 3 products are 3-dehydro-L-threonate, 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-threonate:NAD+ 3-oxidoreductase. Other names in common use include threonate dehydrogenase, and L-threonic acid 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/L-threonine%203-dehydrogenase | In enzymology, a L-threonine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-threonine + NAD+ L-2-amino-3-oxobutanoate + NADH + H+
Thus, the two substrates of this enzyme are L-threonine and NAD+, whereas its 3 products are L-2-amino-3-oxobutanoate, 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-threonine:NAD+ oxidoreductase. Other names in common use include L-threonine dehydrogenase, threonine 3-dehydrogenase, and threonine dehydrogenase. This enzyme participates in glycine, serine and threonine 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
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-xylose%201-dehydrogenase | In enzymology, a L-xylose 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-xylose + NADP+ L-xylono-1,4-lactone + NADPH + H+
Thus, the two substrates of this enzyme are L-xylose and NADP+, whereas its 3 products are L-xylono-1,4-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-xylose:NADP+ 1-oxidoreductase. Other names in common use include L-xylose dehydrogenase, and NADPH-xylose reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malate%20dehydrogenase%20%28decarboxylating%29 | Malate dehydrogenase (decarboxylating) () or NAD-malic enzyme (NAD-ME) is an enzyme that catalyzes the chemical reaction
(S)-malate + NAD+ pyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are (S)-malate and NAD+, whereas its three products are pyruvate, CO2, and NADH. Malate is oxidized to pyruvate and CO2, and NAD+ is reduced to NADH.
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. The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in pyruvate metabolism and carbon fixation. NAD-malic enzyme is one of three decarboxylation enzymes used in the inorganic carbon concentrating mechanisms of C4 and CAM plants. The others are NADP-malic enzyme and PEP carboxykinase.
References
EC 1.1.1
NADH-dependent enzymes |
https://en.wikipedia.org/wiki/Malate%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Malate dehydrogenase (NADP+)}}
In enzymology, a malate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(S)-malate + NADP+ oxaloacetate + NADPH + H+
Thus, the two substrates of this enzyme are (S)-malate and NADP+, whereas its 3 products are oxaloacetate, 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 (S)-malate:NADP+ oxidoreductase. Other names in common use include NADP+-malic enzyme, NADP+-malate dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), malate NADP+ dehydrogenase, NADP+ malate dehydrogenase, NADP+-linked malate dehydrogenase, and malate dehydrogenase (NADP+). This enzyme participates in pyruvate metabolism and carbon fixation. This enzyme has at least one effector, hn.
Structural studies
As of late 2007, two 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/Malate%20dehydrogenase%20%28oxaloacetate-decarboxylating%29 | In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) () is an enzyme that catalyzes the chemical reaction below
(S)-malate + NAD+ pyruvate + CO2 + NADH
Thus, the two substrates of this enzyme are (S)-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 donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating). Other names in common use include malic enzyme, pyruvic-malic carboxylase, NAD+-specific malic enzyme, NAD+-malic enzyme, and NAD+-linked malic enzyme. This enzyme participates in pyruvate metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
See also
ME2 (gene)
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Malate%20dehydrogenase%20%28oxaloacetate-decarboxylating%29%20%28NADP%2B%29 | {{DISPLAYTITLE:Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)}}
Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) () or NADP-malic enzyme (NADP-ME) is an enzyme that catalyzes the chemical reaction in the presence of a bivalent metal ion:
(S)-malate + NADP+ pyruvate + CO2 + NADPH
Thus, the two substrates of this enzyme are (S)-malate and NADP+, whereas its 3 products are pyruvate, CO2, and NADPH. Malate is oxidized to pyruvate and CO2, and NADP+ is reduced to NADPH.
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. The systematic name of this enzyme class is (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating). This enzyme participates in pyruvate metabolism and carbon fixation. NADP-malic enzyme is one of three decarboxylation enzymes used in the inorganic carbon concentrating mechanisms of C4 and CAM plants. The others are NAD-malic enzyme and PEP carboxykinase. Although often one of the three photosynthetic decarboxylases predominate, the simultaneous operation of all three is also shown to exist.
Enzyme structure
Based on crystallography data of homologous NADP-dependent malic enzymes of mammalian origin, a 3D model for C4 pathway NADP-ME in plants has been developed, identifying the key residues involved in substrate-binding or catalysis. Dinucleotide binding involves two glycine-rich GXGXXG motifs, a hydrophobic groove involving at least si |
https://en.wikipedia.org/wiki/Mannitol-1-phosphate%205-dehydrogenase | In enzymology, a mannitol-1-phosphate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-mannitol 1-phosphate + NAD+ D-fructose 6-phosphate + NADH + H+
Thus, the two substrates of this enzyme are D-mannitol 1-phosphate and NAD+, whereas its 3 products are 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-mannitol-1-phosphate:NAD+ 2-oxidoreductase. Other names in common use include hexose reductase, mannitol 1-phosphate dehydrogenase, D-mannitol-1-phosphate dehydrogenase, and fructose 6-phosphate reductase. This enzyme participates in fructose and mannose metabolism.
See also
D-Mannitol
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Mannitol%202-dehydrogenase | In enzymology, a mannitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-mannitol + NAD+ D-fructose + NADH + H+
Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-fructose, 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-mannitol:NAD+ 2-oxidoreductase. Other names in common use include D-mannitol dehydrogenase, and mannitol dehydrogenase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, two 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/Mannitol%202-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Mannitol 2-dehydrogenase (NADP+)}}
In enzymology, a mannitol 2-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-mannitol + NADP+ D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are D-mannitol and NADP+, whereas its 3 products are 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-mannitol:NADP+ 2-oxidoreductase. This enzyme is also called mannitol 2-dehydrogenase (NADP+). This enzyme participates in fructose and mannose metabolism.
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/Mannitol%20dehydrogenase | In enzymology, a mannitol dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-mannitol + NAD+ D-mannose + NADH + H+
Thus, the two substrates of this enzyme are D-mannitol and NAD+, whereas its 3 products are D-mannose, 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 mannitol:NAD+ 1-oxidoreductase. Other names in common use include MTD, and NAD+-dependent mannitol dehydrogenase.
References
See also
D-Mannitol
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannose-6-phosphate%206-reductase | In enzymology, a mannose-6-phosphate 6-reductase () is an enzyme that catalyzes the chemical reaction
D-mannitol 1-phosphate + NADP+ D-mannose 6-phosphate + NADPH + H+
Thus, the two substrates of this enzyme are D-mannitol 1-phosphate and NADP+, whereas its 3 products are D-mannose 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-mannitol-1-phosphate:NADP+ 6-oxidoreductase. Other names in common use include NADPH-dependent mannose 6-phosphate reductase, mannose-6-phosphate reductase, 6-phosphomannose reductase, NADP+-dependent mannose-6-P:mannitol-1-P oxidoreductase, NADPH-dependent M6P reductase, and NADPH-mannose-6-P reductase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannuronate%20reductase | In enzymology, a mannuronate reductase () is an enzyme that catalyzes the chemical reaction
D-mannonate + NAD(P)+ D-mannuronate + NAD(P)H + H+
The 3 substrates of this enzyme are D-mannonate, NAD+, and NADP+, whereas its 4 products are D-mannuronate, 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-mannonate:NAD(P)+ 6-oxidoreductase. Other names in common use include mannonate dehydrogenase, mannonate (nicotinamide adenine dinucleotide, (phosphate))dehydrogenase, mannonate dehydrogenase, mannuronate reductase, mannonate dehydrogenase (NAD(P)+), D-mannonate:nicotinamide adenine dinucleotide (phosphate, and oxidoreductase (D-mannuronate-forming)).
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methanol%20dehydrogenase | In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:
CH3OH CH2O + 2 electrons + 2H+
How the electrons are captured and transported depends upon the kind of methanol dehydrogenase. There are three main types of MDHs: NAD+-dependent MDH, pyrrolo-quinoline quinone dependent MDH, and oxygen-dependent alcohol oxidase.
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 methanol:NAD+ oxidoreductase. This enzyme participates in methane metabolism.
Classes of Methanol Dehydrogenase
NAD+ Dependent MDH
A common electron acceptor in biological systems is nicotinamide adenine dinucleotide (NAD+); some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate (NADP+). An NAD+-dependent methanol dehydrogenase() was first reported in a Gram-positive methylotroph and is an enzyme that catalyzes the chemical reaction:
CH3OH + NAD+ CH2O + NADH + H+
Thus, the two substrates of this enzyme are methanol and NAD+, whereas its 3 products are formaldehyde (CH2O), NADH, and H+. This can be performed under both aerobic and anaerobic conditions.
NAD+ -dependent MDHs are found in thermophilic, Gram positive methlyotrophs, but can also been obtained from some non-methylotrophic bacteria. NAD+-dependent MDHs have so far been found in Bacillus sp., Lysinibacillus sp.,and Cupriavidus sp.
PQQ-Depen |
https://en.wikipedia.org/wiki/Methylglyoxal%20reductase%20%28NADH-dependent%29 | In enzymology, a methylglyoxal reductase (NADH-dependent) () is an enzyme that catalyzes the chemical reaction
(R)-lactaldehyde + NAD+ methylglyoxal + NADH + H+
Thus, the two substrates of this enzyme are (R)-lactaldehyde and NAD+, whereas its 3 products are methylglyoxal, 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)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include methylglyoxal reductase, and D-lactaldehyde dehydrogenase. This enzyme participates in pyruvate metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylglyoxal%20reductase%20%28NADPH-dependent%29 | In enzymology, a methylglyoxal reductase (NADPH-dependent) () is an enzyme that catalyzes the chemical reaction
lactaldehyde + NADP+ methylglyoxal + NADPH + H+
Thus, the two substrates of this enzyme are lactaldehyde and NADP+, whereas its 3 products are methylglyoxal, 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 lactaldehyde:NADP+ oxidoreductase. Other names in common use include lactaldehyde dehydrogenase (NADP+), and Gre2.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mevaldate%20reductase | In enzymology, a mevaldate reductase () is an enzyme that catalyzes the chemical reaction
(R)-mevalonate + NAD+ mevaldate + NADH + H+
Thus, the two substrates of this enzyme are (R)-mevalonate and NAD+, whereas its 3 products are mevaldate, 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)-mevalonate:NAD+ oxidoreductase. This enzyme is also called mevalonic dehydrogenase.
References
External links
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mevaldate%20reductase%20%28NADPH%29 | In enzymology, a mevaldate reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
(R)-mevalonate + NADP+ mevaldate + NADPH + H+
Thus, the two substrates of this enzyme are (R)-mevalonate and NADP+, whereas its 3 products are mevaldate, 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)-mevalonate:NADP+ oxidoreductase. Other names in common use include mevaldate (reduced nicotinamide adenine dinucleotide phosphate), reductase, and mevaldate reductase (NADPH).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Morphine%206-dehydrogenase | In enzymology, a morphine 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
morphine + NAD(P)+ morphinone + NAD(P)H + H+
The 3 substrates of this enzyme are morphine, NAD+, and NADP+, whereas its 4 products are morphinone, 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 morphine:NAD(P)+ 6-oxidoreductase. Other names in common use include naloxone reductase, and reductase, naloxone. This enzyme participates in alkaloid biosynthesis i. This enzyme has at least one effector, Mercaptoethanol.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylhexosamine%201-dehydrogenase | In enzymology, a N-acetylhexosamine 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-acetyl-D-glucosamine + NAD+ N-acetyl-D-glucosaminate + NADH + H+
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and NAD+, whereas its 3 products are N-acetyl-D-glucosaminate, 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 N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase. Other names in common use include N-acetylhexosamine dehydrogenase, and N-acetyl-D-hexosamine dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acylmannosamine%201-dehydrogenase | In enzymology, a N-acylmannosamine 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-mannosamine + NAD+ N-acyl-D-mannosaminolactone + NADH + H+
Thus, the two substrates of this enzyme are N-acyl-D-mannosamine and NAD+, whereas its 3 products are N-acyl-D-mannosaminolactone, 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 N-acyl-D-mannosamine:NAD+ 1-oxidoreductase. Other names in common use include N-acylmannosamine dehydrogenase, N-acetyl-D-mannosamine dehydrogenase, N-acyl-D-mannosamine dehydrogenase, and N-acylmannosamine dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Octanol%20dehydrogenase | In enzymology, an octanol dehydrogenase () is an enzyme that catalyzes the chemical reaction
1-octanol + NAD+ 1-octanal + NADH + H+
Thus, the two substrates of this enzyme are 1-octanol and NAD+, whereas its 3 products are 1-octanal, 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 octanol:NAD+ oxidoreductase. This enzyme is also called 1-octanol dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Omega-hydroxydecanoate%20dehydrogenase | In enzymology, an omega-hydroxydecanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
10-hydroxydecanoate + NAD+ ⇌ 10-oxodecanoate + NADH + H+
Thus, the two substrates of this enzyme are 10-hydroxydecanoate and NAD+, whereas its 3 products are 10-oxodecanoate, 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 10-hydroxydecanoate:NAD+ 10-oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oxaloglycolate%20reductase%20%28decarboxylating%29 | In enzymology, an oxaloglycolate reductase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
D-glycerate + NAD(P)+ + CO2 2-hydroxy-3-oxosuccinate + NAD(P)H + 2 H+
The 4 substrates of this enzyme are D-glycerate, NAD+, NADP+, and CO2, whereas its 4 products are 2-hydroxy-3-oxosuccinate, 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:NAD(P)+ oxidoreductase (carboxylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pantoate%204-dehydrogenase | In enzymology, a pantoate 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
(R)-pantoate + NAD+ (R)-4-dehydropantoate + NADH + H+
Thus, the two substrates of this enzyme are (R)-pantoate and NAD+, whereas its 3 products are (R)-4-dehydropantoate, 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)-pantoate:NAD+ 4-oxidoreductase. Other names in common use include pantoate dehydrogenase, pantothenase, and D-pantoate:NAD+ 4-oxidoreductase. This enzyme participates in pantothenate and coa biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Perillyl-alcohol%20dehydrogenase | In enzymology, a perillyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction
perillyl alcohol + NAD+ perillyl aldehyde + NADH + H+
Thus, the two substrates of this enzyme are perillyl alcohol and NAD+, whereas its 3 products are perillyl 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 perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
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