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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 |
https://en.wikipedia.org/wiki/Phosphogluconate%20dehydrogenase%20%28decarboxylating%29 | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
6-phospho-D-gluconate + NADP+ D-ribulose 5-phosphate + CO2 + NADPH
Thus, the two substrates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH.
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 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating). Other names in common use include phosphogluconic acid dehydrogenase, 6-phosphogluconic dehydrogenase, 6-phosphogluconic carboxylase, 6-phosphogluconate dehydrogenase (decarboxylating), and 6-phospho-D-gluconate dehydrogenase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, manganese.
Enzyme Structure
The general structure, as well as several critical residues, on 6-phosphogluconate dehydrogenase appear to be well conserved over various species. The enzyme is a dimer, with each subunit containing three domains. The N-terminal coenzyme binding domain contains a Rossmann fold with additional α/β units. The second domain consists of a number of alpha helical structures, and the C-terminal domain consists of a short tail. The tails of the two subunits interact with each other to form a mobile lid on the enzyme's active site.
As of late 2007, 11 structures have been solved fo |
https://en.wikipedia.org/wiki/Prostaglandin-E2%209-reductase | {{DISPLAYTITLE:Prostaglandin-E2 9-reductase}}
In enzymology, a prostaglandin-E2 9-reductase () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate and NADP+, whereas its 3 products are (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate, 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 (5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP+ 9-oxidoreductase. Other names in common use include PGE2-9-OR, reductase, 15-hydroxy-9-oxoprostaglandin, 9-keto-prostaglandin E2 reductase, 9-ketoprostaglandin reductase, PGE-9-ketoreductase, PGE2 9-oxoreductase, PGE2 reductase-9-ketoreductase, prostaglandin 9-ketoreductase, prostaglandin E 9-ketoreductase, and prostaglandin E2 reductase-9-oxoreductase. This enzyme participates in arachidonic acid 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/Pterocarpin%20synthase | In enzymology, a pterocarpin synthase () is an enzyme that catalyzes the chemical reaction
medicarpin + NADP+ + H2O vestitone + NADPH + H+
The 3 substrates of this enzyme are medicarpin, NADP+, and H2O, whereas its 3 products are vestitone, 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 medicarpin:NADP+ 2'-oxidoreductase. This enzyme is also called pterocarpan synthase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/Pyridoxal%204-dehydrogenase | In enzymology, a pyridoxal 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
pyridoxal + NAD+ 4-pyridoxolactone + NADH + H+
Thus, the two substrates of this enzyme are pyridoxal and NAD+, whereas its 3 products are 4-pyridoxolactone, 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 pyridoxal:NAD+ 4-oxidoreductase. This enzyme is also called pyridoxal dehydrogenase. This enzyme participates in vitamin B6 metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pyridoxine%204-dehydrogenase | In enzymology, a pyridoxine 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
pyridoxine + NADP+ pyridoxal + NADPH + H+
Thus, the two substrates of this enzyme are pyridoxine and NADP+, whereas its 3 products are pyridoxal, 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 pyridoxine:NADP+ 4-oxidoreductase. Other names in common use include pyridoxin dehydrogenase, pyridoxol dehydrogenase, and pyridoxine dehydrogenase. This enzyme participates in vitamin B6 metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinate%20dehydrogenase | In enzymology, a quinate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-quinate + NAD+ 3-dehydroquinate + NADH + H+
Thus, the two substrates of this enzyme are L-quinate and NAD+, whereas its 3 products are 3-dehydroquinate, 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-quinate:NAD+ 3-oxidoreductase. Other names in common use include quinic dehydrogenase, quinate:NAD oxidoreductase, quinate 5-dehydrogenase, and quinate:NAD+ 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Retinol%20dehydrogenase | In enzymology, a retinol dehydrogenase (RDH) () is an enzyme that catalyzes the chemical reaction
retinol + NAD+ retinal + NADH + H+
Sometimes, in addition to or along with NAD+, NADP+ can act as a preferred cofactor in the reaction as well. The substrate of the enzyme can be all-trans- or -cis- retinol. There are at least over 20 different isolated enzymes with RDH activity to date. Thus, the two substrates of this enzyme are retinol and NAD+, whereas its 3 products are retinal, NADH (or NADPH in the case where NADP+ is a cofactor), 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 retinol:NAD+ oxidoreductase. Other names in common use include retinol (vitamin A1) dehydrogenase, MDR, microsomal retinol dehydrogenase, all-trans retinol dehydrogenase, retinal reductase, and retinene reductase. This enzyme participates in retinol metabolism. Occasionally, the literature refers to retinol dehydrogenase as an enzyme that oxidizes retinol in general, such as class IV alcohol dehydrogenase (ADH4), which reportedly is the most efficient retinol oxidation in the human alcohol dehydrogenase (ADH) family.
Structure
As one of the most important RDH, 11-cis-retinol dehydrogenase catalyzes the 11-cis retinaldehyde (the most common visual pigments in higher animals) formation. The enzyme is mainly expressed in the retinal pigment epithelium (R |
https://en.wikipedia.org/wiki/Ribitol%202-dehydrogenase | In enzymology, a ribitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
ribitol + NAD+ D-ribulose + NADH + H+
Thus, the two substrates of this enzyme are ribitol and NAD+, whereas its 3 products are D-ribulose, NADH, and H+.
This enzyme participates in pentose and glucuronate interconversions.
Nomenclature
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 ribitol:NAD+ 2-oxidoreductase. Other names in common use include adonitol dehydrogenase, ribitol dehydrogenase A (wild type), ribitol dehydrogenase B (mutant enzyme with different properties), and ribitol dehydrogenase D (mutant enzyme with different properties).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribitol-5-phosphate%202-dehydrogenase | In enzymology, a ribitol-5-phosphate 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-ribitol 5-phosphate + NAD(P)+ D-ribulose 5-phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are D-ribitol 5-phosphate, NAD+, and NADP+, whereas its 4 products are D-ribulose 5-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 D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase. This enzyme is also called dehydrogenase, ribitol 5-phosphate. This enzyme participates in pentose and glucuronate interconversions.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Testosterone%2017b-dehydrogenase%20%28NADP%2B%29 | Testosterone 17beta-dehydrogenase (NADP+) (, 17-ketoreductase, NADP-dependent testosterone-17beta-oxidoreductase, testosterone 17beta-dehydrogenase (NADP)) is an enzyme with systematic name 17beta-hydroxysteroid:NADP+ 17-oxidoreductase. This enzyme catalyses the following chemical reaction
testosterone + NADP+ androstenedione + NADPH + H+
Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
References
External links
EC 1.1.1
Steroid hormone biosynthesis |
https://en.wikipedia.org/wiki/Ribose%201-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Ribose 1-dehydrogenase (NADP+)}}
In enzymology, a ribose 1-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
D-ribose + NADP+ + H2O D-ribonate + NADPH + H+
The three substrates of this enzyme are D-ribose, NADP+, and H2O, whereas its 3 products are D-ribonate, 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-ribose:NADP+ 1-oxidoreductase. Other names in common use include D-ribose dehydrogenase (NADP+), NADP+-pentose-dehydrogenase, and ribose 1-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Salutaridine%20reductase%20%28NADPH%29 | In enzymology, a salutaridine reductase (NADPH) () is an enzyme that catalyzes the chemical reaction
salutaridinol + NADP+ salutaridine + NADPH + H+
Thus, the two substrates of this enzyme are salutaridinol and NADP+, whereas its 3 products are salutaridine, 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 salutaridinol:NADP+ 7-oxidoreductase. This enzyme participates in alkaloid biosynthesis i.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sepiapterin%20reductase | Sepiapterin reductase is an enzyme that in humans is encoded by the SPR gene.
Function
Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase; EC 1.1.1.153) catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines, and belongs to a group of enzymes called aldo-keto reductases. SPR plays an important role in the biosynthesis of tetrahydrobiopterin.
Reaction
Sepiapterin reductase (SPR) catalyzes the chemical reaction
L-erythro-7,8-dihydrobiopterin + NADP+ sepiapterin + NADPH + H+
Thus, the two substrates of this enzyme are L-erythro-7,8-dihydrobiopterin and NADP+, whereas its three products are sepiapterin, NADPH, and a single hydrogen ion (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. The systematic name of this enzyme class is 7,8-dihydrobiopterin:NADP+ oxidoreductase. This enzyme participates in folate biosynthesis.
Clinical significance
Mutations of the SPR gene may cause sepiapterin reductase deficiency, a rare disease. The clinical phenotype can include progressive psychomotor retardation, altered tone, seizures, choreoathetosis, temperature instability, hypersalivation, microcephaly, and irritability. Patients with sepiapterin reductase deficiency also manifest dystonia with diurnal variation, oculogyric crises, tremor, hypersomnolence, oculomotor apraxia, and weakness. Response to treatment is var |
https://en.wikipedia.org/wiki/S-%28hydroxymethyl%29glutathione%20dehydrogenase | In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase () is an enzyme that catalyzes the chemical reaction
S-(hydroxymethyl)glutathione + NAD(P)+ S-formylglutathione + NAD(P)H + H+
The 3 substrates of this enzyme are S-(hydroxymethyl)glutathione, NAD+, and NADP+, whereas its 4 products are S-formylglutathione, 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 S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include NAD-linked formaldehyde dehydrogenase (incorrect), formaldehyde dehydrogenase (incorrect), formic dehydrogenase (incorrect), class III alcohol dehydrogenase, ADH3, &chi, -ADH, FDH (incorrect), formaldehyde dehydrogenase (glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent formaldehyde dehydrogenase, GD-FALDH, and NAD- and glutathione-dependent formaldehyde dehydrogenase. This enzyme participates in methane 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
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Sorbose%205-dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:Sorbose 5-dehydrogenase (NADP+)}}
In enzymology, a sorbose 5-dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
L-sorbose + NADP+ 5-dehydro-D-fructose + NADPH + H+
Thus, the two substrates of this enzyme are L-sorbose 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 L-sorbose:NADP+ 5-oxidoreductase. Other names in common use include 5-ketofructose reductase, 5-keto-D-fructose reductase, sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase, reduced nicotinamide adenine dinucleotide phosphate-linked, reductase, and sorbose 5-dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sorbose%20reductase | In enzymology, a sorbose reductase () is an enzyme that catalyzes the chemical reaction
D-glucitol + NADP+ L-sorbose + NADPH + H+
Thus, the two substrates of this enzyme are D-glucitol and NADP+, whereas its 3 products are L-sorbose, 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-glucitol:NADP+ oxidoreductase. This enzyme is also called Sou1p.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sterol-4alpha-carboxylate%203-dehydrogenase%20%28decarboxylating%29 | In enzymology, a sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) () is an enzyme that catalyzes the chemical reaction
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H
The 3 substrates of this enzyme are 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate, NAD+, and NADP+, whereas its 4 products are 4alpha-methyl-5alpha-cholest-7-en-3-one, CO2, NADH, and NADPH.
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 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate:NAD(P)+ 3-oxidoreductase (decarboxylating). Other names in common use include 3beta-hydroxy-4beta-methylcholestenecarboxylate 3-dehydrogenase, (decarboxylating), 3beta-hydroxy-4beta-methylcholestenoate dehydrogenase, 3beta-hydroxy-4beta-methylcholestenoate dehydrogenase, and sterol 4alpha-carboxylic decarboxylase. This enzyme participates in biosynthesis of steroids.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulcatone%20reductase | In enzymology, a sulcatone reductase () is an enzyme that catalyzes the chemical reaction
sulcatol + NAD+ sulcatone + NADH + H+
Thus, the two substrates of this enzyme are sulcatol and NAD+, whereas its 3 products are sulcatone, 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 sulcatol:NAD+ oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tagaturonate%20reductase | Tagaturonate reductase () is an enzyme that catalyzes the chemical reaction
D-altronate + NAD+ D-tagaturonate + NADH + H+
Thus, the two substrates of this enzyme are D-altronate and NAD+, whereas its 3 products are D-tagaturonate, 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-altronate:NAD+ 3-oxidoreductase. Other names in common use include altronic oxidoreductase, altronate oxidoreductase, TagUAR, altronate dehydrogenase, and D-tagaturonate reductase. 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/Tartrate%20dehydrogenase | In enzymology, a tartrate dehydrogenase () is an enzyme that catalyzes the chemical reaction
tartrate + NAD+ oxaloglycolate + NADH + H+
Thus, the two substrates of this enzyme are tartrate and NAD+, whereas its 3 products are oxaloglycolate, 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 tartrate:NAD+ oxidoreductase. This enzyme is also called mesotartrate dehydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, manganese.
References
EC 1.1.1
NADH-dependent enzymes
Manganese enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Testosterone%2017beta-dehydrogenase | In enzymology, a testosterone 17beta-dehydrogenase is an enzyme that catalyzes the chemical reaction between testosterone and androst-4-ene-3,17-dione. 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 17beta-hydroxysteroid:NAD+ 17-oxidoreductase. Other names in common use include 17-ketoreductase and 17beta-HSD. This enzyme participates in androgen and estrogen metabolism.
Variants
There are two variants of the enzyme, one that uses NAD+ as a substrate, and one that uses NADP+ as acceptor.
NAD+
This variant of testosterone 17beta-dehydrogenase () catalyzes the reaction
testosterone + NAD+ androst-4-ene-3,17-dione + NADH + H+
Thus, the two substrates of this enzyme are testosterone and NAD+, whereas its 3 products are androst-4-ene-3,17-dione, NADH, and H+.
NADP+
This variant of testosterone 17beta-dehydrogenase () catalyzes the reaction
testosterone + NADP+ androst-4-ene-3,17-dione + NADPH + H+
Thus, the two substrates of this enzyme are testosterone and NADP+, whereas its 3 products are androst-4-ene-3,17-dione, NADPH, and H+.
References
External links
Testodren - Testosterone Booster
EC 1.1.1
Testosterone
NADH-dependent enzymes
NADPH-dependent enzymes
Enzymes of known structure
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydroxynaphthalene%20reductase | In enzymology, a tetrahydroxynaphthalene reductase () is an enzyme that catalyzes the chemical reaction
scytalone + NADP+ 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+
Thus, the two substrates of this enzyme are scytalone and NADP+, whereas its 3 products are 1,3,6,8-tetrahydroxynaphthalene, 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 scytalone:NADP+ Delta5-oxidoreductase.
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/Tropinone%20reductase%20I | In enzymology, a tropinone reductase I () is an enzyme that catalyzes the chemical reaction
tropine + NADP+ tropinone + NADPH + H+
Thus, the two substrates of this enzyme are tropine and NADP+, whereas its 3 products are tropinone, 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 tropine:NADP+ 3alpha-oxidoreductase. Other names in common use include tropine dehydrogenase, tropinone reductase (ambiguous), and TR-I. This enzyme participates in alkaloid biosynthesis ii.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tropinone%20reductase%20II | In enzymology, a tropinone reductase II () is an enzyme that catalyzes the chemical reaction
pseudotropine + NADP+ tropinone + NADPH + H+
Thus, the two substrates of this enzyme are pseudotropine and NADP+, whereas its 3 products are tropinone, 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 pseudotropine:NADP+ 3-oxidoreductase. Other names in common use include tropinone (psi-tropine-forming) reductase, pseudotropine forming tropinone reductase, tropinone reductase (ambiguous), and TR-II. This enzyme participates in alkaloid biosynthesis ii.
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
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-glucose%206-dehydrogenase | UDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the UGDH gene.
The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia.
This enzyme participates in 4 metabolic pathways: pentose and glucuronate interconversions, ascorbate and aldarate metabolism, starch and sucrose metabolism, and nucleotide sugars metabolism.
Loss of UGDH has recently been implicated in epileptic encephalopathy in humans
Nomenclature
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 UDP-glucose:NAD+ 6-oxidoreductase.
Other names in common use include:
UDP-glucose dehydrogenase,
uridine diphosphoglucose dehydrogenase,
UDPG dehydrogenase,
UDPG:NAD oxidoreductase,
UDP-alpha-D-glucose:NAD oxidoreductase,
UDP-glucose:NAD+ oxidoreductase,
uridine diphosphate glucose dehydrogenase,
UDP-D-glucose dehydrogenase, and
uridine diphosphate D-glucose dehydrogenase.
Biochemistry
In enzymology, a UDP-glucose 6-dehy |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%206-dehydrogenase | In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+
The 3 substrates of this enzyme are UDP-N-acetyl-D-glucosamine, NAD+, and H2O, whereas its 3 products are UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate, 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 UDP-N-acetyl-D-glucosamine:NAD+ 6-oxidoreductase. Other names in common use include uridine diphosphoacetylglucosamine dehydrogenase, UDP-acetylglucosamine dehydrogenase, UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase, and UDP-GlcNAc dehydrogenase. This enzyme participates in aminosugars metabolism.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramate%20dehydrogenase | In enzymology, an UDP-N-acetylmuramate dehydrogenase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-alpha-D-muramate + NADP+ UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
Thus, the two substrates of this enzyme are UDP-N-acetyl-alpha-D-muramate and NADP+, whereas its 3 products are UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-N-acetyl-alpha-D-muramate:NADP+ oxidoreductase. Other names in common use include MurB reductase, UDP-N-acetylenolpyruvoylglucosamine reductase, UDP-N-acetylglucosamine-enoylpyruvate reductase, UDP-GlcNAc-enoylpyruvate reductase, uridine diphosphoacetylpyruvoylglucosamine reductase, uridine diphospho-N-acetylglucosamine-enolpyruvate reductase, uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase. This enzyme participates in aminosugars metabolism. It employs one cofactor, FAD.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 1.3.1
NADPH-dependent enzymes
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/RMI%20Corporation | RMI Corporation, formerly Raza Microelectronics, Inc., was a privately held fabless semiconductor company headquartered in Cupertino, California, which specialized in designing system-on-a-chip processors for computer networking (known as network processors) and consumer media applications.
History
Saiyed Atiq Raza founded NexGen, which was acquired by AMD in 1995. Raza was AMD's president and chief operating officer in the late 1990s after the NexGen acquisition.
He left AMD in 1999 and founded Raza Microelectronics, Inc. in 2002.
In 2003, SandCraft Inc folded, and Raza acquired the rights to its intellectual property.
Behrooz Abdi became president and CEO in November 2007, and Raza Microelectronics changed its name to RMI Corporation in December 2007.
In January 2008 Raza settled with the US Securities and Exchange Commission over an allegation of insider trading during 2006.
RMI was not affiliated with Foundries Holdings, LLC, formerly known as Raza Foundries, Inc.
Most of RMI's revenue came from its multi-core processor product line, which had major customers from China including Huawei, ZTE, and H3C. The China business of RMI was built from scratch by its co-founder Sunny Siu. In 2008, RMI merged with NetLogic Microsystems, which was acquired by Broadcom in 2012.
Product lines
RMI had four product lines: three developed internally and one acquired.
The XLR (introduced circa 2005) was a multicore, multithreaded CPU used for network processing. XLR integrated circ |
https://en.wikipedia.org/wiki/Ureidoglycolate%20dehydrogenase | In enzymology, an ureidoglycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-ureidoglycolate + NAD(P)+ oxalurate + NAD(P)H + H+
The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalurate, 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 (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine 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
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Uronate%20dehydrogenase | In enzymology, an uronate dehydrogenase () is an enzyme that catalyzes the chemical reaction
D-galacturonate + NAD+ + H2O + NADH + H+
The 3 substrates of this enzyme are D-galacturonate, NAD+, and H2O, whereas its 3 products are (the lactone of D-galactarate), 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 uronate:NAD+ 1-oxidoreductase. Other names in common use include uronate: NAD-oxidoreductase, and uronic acid dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/12alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 12alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+ 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, 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 12alpha-hydroxysteroid:NADP+ 12-oxidoreductase. Other names in common use include 12alpha-hydroxy steroid dehydrogenase, 12alpha-hydroxy steroid dehydrogenase, NAD+-dependent 12alpha-hydroxysteroid dehydrogenase, and NADP+-12alpha-hydroxysteroid dehydrogenase. This enzyme is involved in a metabolic pathway that degrades bile acids into cholesterol.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/12beta-hydroxysteroid%20dehydrogenase | In enzymology, a 12beta-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP+ 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate + NADPH + H+
Thus, the two substrates of this enzyme are 3alpha,7alpha,12beta-trihydroxy-5beta-cholanate and NADP+, whereas its 3 products are 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate, 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 12beta-hydroxysteroid:NADP+ 12-oxidoreductase. Other names in common use include 12beta-hydroxy steroid (nicotinamide adenine dinucleotide phosphate), and dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1%2C3-propanediol%20dehydrogenase | In enzymology, a 1,3-propanediol dehydrogenase () is an enzyme that catalyzes the chemical reaction
propane-1,3-diol + NAD+ 3-hydroxypropanal + NADH + H+
Thus, the two substrates of this enzyme are propane-1,3-diol and NAD+, whereas its 3 products are 3-hydroxypropanal, 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-1,3-diol:NAD+ 1-oxidoreductase. Other names in common use include 3-hydroxypropionaldehyde reductase, 1,3-PD:NAD+ oxidoreductase, 1,3-propanediol:NAD+ oxidoreductase, and 1,3-propanediol dehydrogenase. This enzyme participates in ether lipid metabolism as a step in glycerolipid biosynthesis.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1%2C5-anhydro-D-fructose%20reductase | In enzymology, a 1,5-anhydro-D-fructose reductase () is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-glucitol + NADP 1,5-anhydro-D-fructose + NADPH + H
Thus, the two substrates of this enzyme are 1,5-anhydro-D-glucitol and NADP, whereas its 3 products are 1,5-anhydro-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 1,5-anhydro-D-glucitol:NADP oxidoreductase.
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/1%2C5-anhydro-D-fructose%20reductase%20%281%2C5-anhydro-D-mannitol-forming%29 | In enzymology, a 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) () is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-mannitol + NADP 1,5-anhydro-D-fructose + NADPH + H
Thus, the two substrates of this enzyme are 1,5-anhydro-D-mannitol and NADP, whereas its 3 products are 1,5-anhydro-D-fructose, NADPH, and H.
This enzyme belongs to the common family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 1,5-anhydro-D-mannitol:NADP oxidoreductase. Other names in common use include 1,5-anhydro-D-fructose reductase (ambiguous), and AFR.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-hydroxyicosatetraenoate%20dehydrogenase | In enzymology, a 15-hydroxyicosatetraenoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H + H+
The 3 substrates of this enzyme are 15-Hydroxyicosatetraenoic acid (i.e. 15(S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate), NAD+, and NADP+, whereas its 4 products are 15-oxo-5,8,11-cis-13-trans-icosatetraenoate, 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 (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate:NAD(P)+ 15-oxidoreductase. This enzyme is also called 15-hydroxyeicosatetraenoate dehydrogenase. This enzyme participates in arachidonic acid metabolism.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin-D%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin-D dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin-D dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate and NADP+, whereas its 3 products are (5Z,13E)-9alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate, 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 (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate:NADP+ 15-oxidoreductase. Other names in common use include prostaglandin-D 15-dehydrogenase (NADP+), dehydrogenase, prostaglandin D2, NADP+-PGD2 dehydrogenase, dehydrogenase, 15-hydroxyprostaglandin (nicotinamide adenine, dinucleotide phosphate), 15-hydroxy PGD2 dehydrogenase, 15-hydroxyprostaglandin dehydrogenase (NADP+), NADP+-dependent 15-hydroxyprostaglandin dehydrogenase, prostaglandin D2 dehydrogenase, NADP+-linked 15-hydroxyprostaglandin dehydrogenase, NADP+-specific 15-hydroxyprostaglandin dehydrogenase, NADP+-linked prostaglandin D2 dehydrogenase, and 15-hydroxyprostaglandin-D dehydrogenase (NADP+). This enzyme participates in arachidonic acid metabolism.
References
EC 1.1.1
NADPH-depende |
https://en.wikipedia.org/wiki/15-hydroxyprostaglandin%20dehydrogenase%20%28NAD%2B%29 | Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase (NAD+), (), is an enzyme that catalyzes the following chemical reaction:
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+
Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NAD+, whereas its 3 products are (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, 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 (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase. Other names in common use include NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I), PGDH, 11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, 15-OH-PGDH, 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostanoic dehydrogenase, NAD+-specific 15-hydroxyprostaglandin dehydrogenase, prostaglandin dehydrogenase, and 15-hydroxyprostaglandin dehydrogenase (NAD+).
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/15-hydroxyprostaglandin%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+
Thus, the two substrates of this enzyme are (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NADP+, whereas its 3 products are (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, 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 (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NADP+ 15-oxidoreductase. Other names in common use include NADP+-dependent 15-hydroxyprostaglandin dehydrogenase, NADP+-linked 15-hydroxyprostaglandin dehydrogenase, NADP+-specific 15-hydroxyprostaglandin dehydrogenase, type II 15-hydroxyprostaglandin dehydrogenase, and 15-hydroxyprostaglandin dehydrogenase (NADP+).
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/15-hydroxyprostaglandin-I%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:15-hydroxyprostaglandin-I dehydrogenase (NADP+)}}
In enzymology, a 15-hydroxyprostaglandin-I dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- dienoate + NADP+ (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
The 3 substrates of this enzyme are (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-, dienoate, and NADP+, whereas its 3 products are (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate, 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 (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoa te:NADP+ 15-oxidoreductase. Other names in common use include prostacyclin dehydrogenase, PG I2 dehydrogenase, prostacyclin dehydrogenase, NADP+-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase, NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase, and 15-hydroxyprostaglandin-I dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/16-alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 16alpha-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 16alpha-hydroxysteroid + NAD(P)+ a 16-oxosteroid + NAD(P)H + H+
The 3 substrates of this enzyme are 16alpha-hydroxysteroid, NAD+, and NADP+, whereas its 4 products are 16-oxosteroid, 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 16alpha-hydroxysteroid:NAD(P)+ 16-oxidoreductase. This enzyme is also called 16alpha-hydroxy steroid dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/20alpha-hydroxysteroid%20dehydrogenase | In enzymology, a 20-α-hydroxysteroid dehydrogenase () is an enzyme that catalyzes the chemical reaction
17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ 17alpha-hydroxyprogesterone + NAD(P)H + H+
The 3 substrates of this enzyme are 17alpha,20alpha-dihydroxypregn-4-en-3-one, NAD+, and NADP+, whereas its 4 products are 17-alpha-hydroxyprogesterone, 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 20alpha-hydroxysteroid:NAD(P)+ 20-oxidoreductase. Other names in common use include 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxy steroid dehydrogenase, 20alpha-HSD, and 20alpha-HSDH. This enzyme participates in c21-steroid hormone metabolism.
20alpha-HSD has been initially described as a progesterone metabolizing enzyme of the ovary. On a functional level, ovarian 20alpha-HSD is actively involved in the control of progesterone homeostasis in pregnancy of rats and mice. While 20alpha-HSD expression and activity is downregulated in the corpus luteum of pregnancy, 24 hrs prior to parturition ovarian 20alpha-HSD activity is acutely stimulated. Accordingly, in mice with targeted deletion of the 20alpha-HSD gene, progesterone blood concentration remain high throughout pregnancy which results in a delay of 2–4 days in parturition. Indicating that expression of 20alpha-HSD activity is mandatory for the induction of parturi |
https://en.wikipedia.org/wiki/21-hydroxysteroid%20dehydrogenase%20%28NAD%2B%29 | {{DISPLAYTITLE:21-hydroxysteroid dehydrogenase (NAD+)}}
In enzymology, a 21-hydroxysteroid dehydrogenase (NAD+) () is an enzyme that catalyzes the chemical reaction
pregnan-21-ol + NAD+ pregnan-21-al + NADH + H+
Thus, the two substrates of this enzyme are pregnan-21-ol and NAD+, whereas its 3 products are pregnan-21-al, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 21-hydroxysteroid:NAD+ 21-oxidoreductase. This enzyme is also called 21-hydroxysteroid dehydrogenase (NAD+).
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/21-hydroxysteroid%20dehydrogenase%20%28NADP%2B%29 | {{DISPLAYTITLE:21-hydroxysteroid dehydrogenase (NADP+)}}
In enzymology, a 21-hydroxysteroid dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
pregnan-21-ol + NADP+ pregnan-21-al + NADPH + H+
Thus, the two substrates of this enzyme are pregnan-21-ol and NADP+, whereas its 3 products are pregnan-21-al, 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 21-hydroxysteroid:NADP+ 21-oxidoreductase. Other names in common use include 21-hydroxy steroid dehydrogenase, 21-hydroxy steroid (nicotinamide adenine dinucleotide phosphate), dehydrogenase, 21-hydroxy steroid dehydrogenase (nicotinamide adenine dinucleotide, phosphate), NADP+-21-hydroxysteroid dehydrogenase, and 21-hydroxysteroid dehydrogenase (NADP+).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C5-didehydrogluconate%20reductase | In enzymology, a 2,5-didehydrogluconate reductase () is an enzyme that catalyzes the chemical reaction
2-dehydro-D-gluconate + NADP+ 2,5-didehydro-D-gluconate + NADPH + H+
Thus, the two substrates of this enzyme are 2-dehydro-D-gluconate and NADP+, whereas its 3 products are 2,5-didehydro-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 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase. Other names in common use include 2,5-diketo-D-gluconate reductase, and YqhE 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
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-alkyn-1-ol%20dehydrogenase | In enzymology, a 2-alkyn-1-ol dehydrogenase () is an enzyme that catalyzes the chemical reaction below:
2-butyne-1,4-diol + NAD+ 4-hydroxy-2-butynal + NADH + H+
The two substrates of this enzyme are 2-butyne-1,4-diol and NAD+, whereas its 3 products are 4-hydroxy-2-butynal, 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 2-butyne-1,4-diol:NAD+ 1-oxidoreductase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20dehydrogenase%20%28NAD%28P%29%2B%29 | {{DISPLAYTITLE:Glycerol-3-phosphate dehydrogenase (NAD(P)+)}}
In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + NAD(P)+ glycerone phosphate + NAD(P)H + H+
The 3 substrates of this enzyme are sn-glycerol 3-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-3-phosphate:NAD(P)+ 2-oxidoreductase. Other names in common use include L-glycerol-3-phosphate:NAD(P)+ oxidoreductase, glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide, (phosphate)), glycerol 3-phosphate dehydrogenase (NADP+), and glycerol-3-phosphate dehydrogenase [NAD(P)+]. This enzyme participates in glycerophospholipid 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
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxy-D-gluconate%205-dehydrogenase | In enzymology, a 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-dehydro-3-deoxy-D-gluconate + NAD+ (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+
Thus, the two substrates of this enzyme are 2-dehydro-3-deoxy-D-gluconate and NAD+, whereas its 3 products are (4S)-4,6-dihydroxy-2,5-dioxohexanoate, NADH, and H+.
This enzyme participates in pentose and glucuronate interconversions.
Nomenclature
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-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase. Other names in common use include 2-keto-3-deoxygluconate 5-dehydrogenase, 2-keto-3-deoxy-D-gluconate dehydrogenase, 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide, (phosphate)) dehydrogenase, 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic, and acid) dehydrogenase.
References
EC 1.1.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydro-3-deoxy-D-gluconate%206-dehydrogenase | In enzymology, a 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-dehydro-3-deoxy-D-gluconate + NADP+ (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+
Thus, the two substrates of this enzyme are 2-dehydro-3-deoxy-D-gluconate and NADP+, whereas its 3 products are (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate, 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-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase. Other names in common use include 2-keto-3-deoxy-D-gluconate dehydrogenase, and 2-keto-3-deoxygluconate dehydrogenase.
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydropantoate%202-reductase | In enzymology, a 2-dehydropantoate 2-reductase () is an enzyme that catalyzes the chemical reaction
(R)-pantoate + NADP+ 2-dehydropantoate + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantoate and NADP+, whereas its 3 products are 2-dehydropantoate, 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)-pantoate:NADP+ 2-oxidoreductase. Other names in common use include 2-oxopantoate reductase, 2-ketopantoate reductase, 2-ketopantoic acid reductase, ketopantoate reductase, and ketopantoic acid reductase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-dehydropantolactone%20reductase%20%28A-specific%29 | In enzymology, a 2-dehydropantolactone reductase (A-specific) () is an enzyme that catalyzes the chemical reaction
(R)-pantolactone + NADP+ 2-dehydropantolactone + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantolactone and NADP+, whereas its 3 products are 2-dehydropantolactone, 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)-pantolactone:NADP+ oxidoreductase (A-specific). Other names in common use include 2-oxopantoyl lactone reductase, ketopantoyl lactone reductase, 2-ketopantoyl lactone reductase, and 2-dehydropantoyl-lactone reductase (A-specific).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-dehydropantolactone%20reductase%20%28B-specific%29 | In enzymology, a 2-dehydropantolactone reductase (B-specific) () is an enzyme that catalyzes the chemical reaction
(R)-pantolactone + NADP+ 2-dehydropantolactone + NADPH + H+
Thus, the two substrates of this enzyme are (R)-pantolactone and NADP+, whereas its 3 products are 2-dehydropantolactone, 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)-pantolactone:NADP+ oxidoreductase (B-specific). Other names in common use include 2-oxopantoyl lactone reductase, 2-ketopantoyl lactone reductase, ketopantoyl lactone reductase, and 2-dehydropantoyl-lactone reductase (B-specific).
References
EC 1.1.1
NADPH-dependent enzymes
Enzymes of unknown structure |
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