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13900359 | Glycerol-3-phosphate dehydrogenase (NAD+) | In enzymology, a glycerol-3-phosphate dehydrogenase (NAD+) (EC 1.1.1.8) is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + NAD+ formula_0 glycerone phosphate + NADH + H+
The two substrates of this enzyme are sn-glycerol 3-phosphate and NAD+, whereas its 3 products are glycerone phosphate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase. Other names in common use include alpha-glycerol phosphate dehydrogenase (NAD+), alpha-glycerophosphate dehydrogenase (NAD+), glycerol 1-phosphate dehydrogenase, glycerol phosphate dehydrogenase (NAD+), glycerophosphate dehydrogenase (NAD+), hydroglycerophosphate dehydrogenase, L-alpha-glycerol phosphate dehydrogenase, L-alpha-glycerophosphate dehydrogenase, L-glycerol phosphate dehydrogenase, L-glycerophosphate dehydrogenase, NAD+-alpha-glycerophosphate dehydrogenase, NAD+-dependent glycerol phosphate dehydrogenase, NAD+-dependent glycerol-3-phosphate dehydrogenase, NAD+-L-glycerol-3-phosphate dehydrogenase, NAD+-linked glycerol 3-phosphate dehydrogenase, NADH-dihydroxyacetone phosphate reductase, and glycerol-3-phosphate dehydrogenase (NAD+). This enzyme participates in glycerophospholipid metabolism.
Structural studies.
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1EVY, 1EVZ, 1JDJ, 1M66, 1M67, 1N1E, 1N1G, 1WPQ, 1X0V, 1X0X, 1YJ8, and 1Z82.
References.
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13900389 | Glycerol dehydrogenase (NADP+) | In enzymology, a glycerol dehydrogenase (NADP+) (EC 1.1.1.72) is an enzyme that catalyzes the chemical reaction
glycerol + NADP+ formula_0 D-glyceraldehyde + NADPH + H+
Thus, the two substrates of this enzyme are glycerol and NADP+, whereas its 3 products are D-glyceraldehyde, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycerol:NADP+ oxidoreductase. This enzyme is also called glycerol dehydrogenase (NADP+). This enzyme participates in glycerolipid metabolism.
References.
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13900414 | Glyoxylate reductase (NADP+) | In enzymology, a glyoxylate reductase (NADP+) (EC 1.1.1.79) is an enzyme that catalyzes the chemical reaction
glycolate + NADP+ formula_0 glyoxylate + NADPH + H+
Thus, the two substrates of this enzyme are glycolate and NADP+, whereas its 3 products are glyoxylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glycolate:NADP+ oxidoreductase. Other names in common use include NADPH-glyoxylate reductase, and glyoxylate reductase (NADP+). This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2GCG, 2H1S, and 2Q50.
References.
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13900436 | Hexadecanol dehydrogenase | Enzyme
In enzymology, a hexadecanol dehydrogenase (EC 1.1.1.164) is an enzyme that catalyzes the chemical reaction
hexadecanol + NAD+ formula_0 hexadecanal + NADH + H+
Thus, the two substrates of this enzyme are hexadecanol and NAD+, whereas its 3 products are hexadecanal, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanol:NAD+ oxidoreductase.
References.
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13900450 | Histidinol dehydrogenase |
In enzymology, histidinol dehydrogenase (HIS4) (HDH) (EC 1.1.1.23) is an enzyme that catalyzes the chemical reaction
-histidinol + 2 NAD+ formula_0 -histidine + 2 NADH + 2 H+
Thus, the two substrates of this enzyme are L-histidinol and NAD+, whereas its 3 products are L-histidine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD+ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase.
Structure.
In bacteria, HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyses three different steps of histidine biosynthesis; and in plants it is expressed as a nuclear encoded protein precursor which is exported to the chloroplast.
Active site.
Histidinol is held inside the active site thanks to a zinc ion, but the zinc ion does not participate in the catalysis otherwise. The zinc ion is held in place by His262, Gln259, Asp360 and His419 (which, in homodimeric histidinol dehydrogenases, comes from the other monomer). Histidinol itself is held in place by His327 and His367 from one moment unit and Glu414 from the other monomer unit.
A Cys residue has been implicated in the catalytic mechanism of the second oxidative step. However, according to newer studies with histidinol dehydrogenase from "E. coli", the mechanism is catalyzed by four bases, B1-B4. His327 acts as the first base, deprotonating histidinol's hydroxyl group. Concomitantly, hydride is abstracted from histidinol by NAD+, which is then exchanged for a second NAD+ molecule. Glu325 acts as the second base, deprotonating a molecule of water, which then attacks histidinol. At the same time, His327 (now protonated) donates a proton to the aldehydic oxygen, which results in a gem-diol. After then, His327 again deprotonates one of the hydroxyl groups and NAD+ abstracts a proton from the reactive carbon atom. This series of steps oxidizes the hydroxyl group to a carboxylic acid.
Function.
Histidinol dehydrogenase catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of -histidinol to histidine.
In 4-electron dehydrogenases, a single active site catalyses 2 separate oxidation steps: oxidation of the substrate alcohol to an intermediate aldehyde; and oxidation of the aldehyde to the product acid, in this case His. The reaction proceeds via a tightly- or covalently-bound intermediate, and requires the presence of 2 NAD molecules. By contrast with most dehydrogenases, the substrate is bound before the NAD coenzyme.
Co-regulation of the gene.
Histodinol dehydrogenase gene ("HIS4") has been shown co-regulating the adjacent gene while it is under amino acids selective pressure.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1K75, 1KAE, 1KAH, and 1KAR. | [
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13900469 | Homoisocitrate dehydrogenase | Enzyme
In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ formula_0 2-oxoadipate + CO2 + NADH + H+
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1X0L.
References.
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13900486 | Hydroxycyclohexanecarboxylate dehydrogenase | In enzymology, a hydroxycyclohexanecarboxylate dehydrogenase (EC 1.1.1.166) is an enzyme that catalyzes the chemical reaction
(1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD+ formula_0 (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH + H+
Thus, the two substrates of this enzyme are (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate and NAD+, whereas its 3 products are (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate:NAD+ 3-oxidoreductase. Other names in common use include dihydroxycyclohexanecarboxylate dehydrogenase, and (−)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate-NAD+ oxidoreductase.
References.
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13900495 | Hydroxymalonate dehydrogenase | In enzymology, a hydroxymalonate dehydrogenase (EC 1.1.1.167) is an enzyme that catalyzes the chemical reaction
hydroxymalonate + NAD+ formula_0 oxomalonate + NADH + H+
Thus, the two substrates of this enzyme are hydroxymalonate and NAD+, whereas its 3 products are oxomalonate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydroxymalonate:NAD+ oxidoreductase.
References.
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13900511 | Hydroxymethylglutaryl-CoA reductase (NADPH) | In enzymology, a hydroxymethylglutaryl-CoA reductase (NADPH) (EC 1.1.1.34) is an enzyme that catalyzes the chemical reaction
("R")-mevalonate + CoA + 2 NADP+ formula_0 ("S")-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
The 3 substrates of this enzyme are ("R")-mevalonate, CoA, and NADP+, whereas its 3 products are ("S")-3-hydroxy-3-methylglutaryl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in biosynthesis of steroids including cholesterol. The statin class of anticholesterol drugs act through inhibiting this enzyme.
Nomenclature.
The systematic name of this enzyme class is (R)-mevalonate:NADP+ oxidoreductase (CoA-acylating). Other names in common use include:
Structural studies.
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1DQ8, 1DQ9, 1DQA, 1HW8, 1HW9, 1HWI, 1HWJ, 1HWK, 1HWL, 2Q1L, 2Q6B, and 2Q6C.
References.
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13900527 | Hydroxyphenylpyruvate reductase | In enzymology, a hydroxyphenylpyruvate reductase (EC 1.1.1.237) is an enzyme that catalyzes the chemical reaction
3-(4-hydroxyphenyl)lactate + NAD+ formula_0 3-(4-hydroxyphenyl)pyruvate + NADH + H+
Thus, the two substrates of this enzyme are 3-(4-hydroxyphenyl)lactate and NAD+, whereas its 3 products are 3-(4-hydroxyphenyl)pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-hydroxyphenyllactate:NAD+ oxidoreductase. This enzyme is also called HPRP. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
References.
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13900543 | Hydroxypyruvate reductase | In enzymology, a hydroxypyruvate reductase (EC 1.1.1.81) is an enzyme that catalyzes the chemical reaction
D-glycerate + NAD(P)+ formula_0 hydroxypyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are D-glycerate, NAD+, and NADP+, whereas its 4 products are hydroxypyruvate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glycerate:NADP+ 2-oxidoreductase. Other names in common use include beta-hydroxypyruvate reductase, NADH:hydroxypyruvate reductase, and D-glycerate dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.
References.
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13900553 | Indanol dehydrogenase | In enzymology, an indanol dehydrogenase (EC 1.1.1.112) is an enzyme that catalyzes the chemical reaction
indan-1-ol + NAD(P)+ formula_0 indanone + NAD(P)H + H+
The 3 substrates of this enzyme are indan-1-ol, NAD+, and NADP+, whereas its 4 products are indanone, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is indan-1-ol:NAD(P)+ 1-oxidoreductase.
References.
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13900570 | Indole-3-acetaldehyde reductase (NADH) | Enzyme
In enzymology, an indole-3-acetaldehyde reductase (NADH) (EC 1.1.1.190) is an enzyme that catalyzes the chemical reaction
(indol-3-yl)ethanol + NAD+ formula_0 (indol-3-yl)acetaldehyde + NADH + H+
Thus, the two substrates of this enzyme are (indol-3-yl)ethanol and NAD+, whereas its 3 products are (indol-3-yl)acetaldehyde, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (indol-3-yl)ethanol:NAD+ oxidoreductase. Other names in common use include indoleacetaldehyde reductase, indole-3-acetaldehyde reductase (NADH), and indole-3-ethanol:NAD+ oxidoreductase. This enzyme participates in tryptophan metabolism.
References.
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13900578 | Indole-3-acetaldehyde reductase (NADPH) | Class of enzymes
In enzymology, an indole-3-acetaldehyde reductase (NADPH) (EC 1.1.1.191) is an enzyme that catalyzes the chemical reaction
(indol-3-yl)ethanol + NADP+ formula_0 (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.
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13900591 | Indolelactate dehydrogenase | In enzymology, an indolelactate dehydrogenase (EC 1.1.1.110) is an enzyme that catalyzes the chemical reaction
(indol-3-yl)lactate + NAD+ formula_0 (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.
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13900594 | 4-Hydroxycyclohexanecarboxylate dehydrogenase | Class of enzymes
In enzymology, a 4-hydroxycyclohexanecarboxylate dehydrogenase (EC 1.1.1.226) is an enzyme that catalyzes the chemical reaction
trans-4-hydroxycyclohexanecarboxylate + NAD+ formula_0 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.
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13900611 | Inositol 2-dehydrogenase | In enzymology, an inositol 2-dehydrogenase (EC 1.1.1.18) is an enzyme that catalyzes the chemical reaction
myo-inositol + NAD+ formula_0 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.
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13900612 | 4-(hydroxymethyl)benzenesulfonate dehydrogenase | Class of enzymes
In enzymology, a 4-(hydroxymethyl)benzenesulfonate dehydrogenase (EC 1.1.1.257) is an enzyme that catalyzes the chemical reaction
4-(hydroxymethyl)benzenesulfonate + NAD+ formula_0 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.
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13900628 | 4-hydroxythreonine-4-phosphate dehydrogenase | Protein family
In enzymology, a 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) is an enzyme that catalyzes the chemical reaction
4-phosphonooxy-L-threonine + NAD+ formula_0 (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 1PS6, 1PS7, 1PTM, 1R8K, 1YXO, and 2HI1.
References.
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13900630 | Isopiperitenol dehydrogenase | Class of enzymes
In enzymology, an isopiperitenol dehydrogenase (EC 1.1.1.223) is an enzyme that catalyzes the chemical reaction
(-)-trans-isopiperitenol + NAD+ formula_0 (-)-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.
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13900645 | 4-oxoproline reductase | Class of enzymes
In enzymology, a 4-oxoproline reductase (EC 1.1.1.104) is an enzyme that catalyzes the chemical reaction
4-oxo-L-proline + NADH + H+ formula_0 "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.
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Further reading.
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13900647 | Isopropanol dehydrogenase (NADP+) | Class of enzymes
In enzymology, an isopropanol dehydrogenase (NADP+) (EC 1.1.1.80) is an enzyme that catalyzes the chemical reaction
propan-2-ol + NADP+ formula_0 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.
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13900668 | Ketol-acid reductoisomerase | Class of enzymes
In enzymology, a ketol-acid reductoisomerase (EC 1.1.1.86) is an enzyme that catalyzes the chemical reaction
(R)-2,3-dihydroxy-3-methylbutanoate + NADP+ formula_0 (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 1NP3, 1QMG, 1YRL, and 1YVE.
References.
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| https://en.wikipedia.org/wiki?curid=13900668 |
13900674 | 4-phosphoerythronate dehydrogenase | InterPro Family
In enzymology, a 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction
4-phospho-D-erythronate + NAD+ formula_0 (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 2O4C.
References.
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| https://en.wikipedia.org/wiki?curid=13900674 |
13900686 | Lactaldehyde reductase | In enzymology, a lactaldehyde reductase (EC 1.1.1.77) is an enzyme that catalyzes the chemical reaction
(R)[or (S)]-propane-1,2-diol + NAD+ formula_0 (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 1RRM, 2BI4, and 2BL4.
References.
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| https://en.wikipedia.org/wiki?curid=13900686 |
13900702 | Lactaldehyde reductase (NADPH) | Enzyme class
In enzymology, a lactaldehyde reductase (NADPH) (EC 1.1.1.55) is an enzyme that catalyzes the chemical reaction
propane-1,2-diol + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900702 |
13900717 | L-arabinitol 2-dehydrogenase | In enzymology, a L-arabinitol 2-dehydrogenase (EC 1.1.1.13) is an enzyme that catalyzes the chemical reaction
L-arabinitol + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900717 |
13900732 | L-arabinitol 4-dehydrogenase | In enzymology, a L-arabinitol 4-dehydrogenase (EC 1.1.1.12) is an enzyme that catalyzes the chemical reaction
L-arabinitol + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900732 |
13900747 | L-arabinose 1-dehydrogenase | In enzymology, a L-arabinose 1-dehydrogenase (EC 1.1.1.46) is an enzyme that catalyzes the chemical reaction
L-arabinose + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900747 |
13900763 | L-glycol dehydrogenase | In enzymology, a L-glycol dehydrogenase (EC 1.1.1.185) is an enzyme that catalyzes the chemical reaction
an L-glycol + NAD(P)+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900763 |
13900775 | L-gulonate 3-dehydrogenase | In enzymology, a L-gulonate 3-dehydrogenase (EC 1.1.1.45) is an enzyme that catalyzes the chemical reaction
L-gulonate + NAD+ formula_0 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 2DPO.
References.
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| https://en.wikipedia.org/wiki?curid=13900775 |
13900816 | L-idonate 5-dehydrogenase | In enzymology, a L-idonate 5-dehydrogenase (EC 1.1.1.264) is an enzyme that catalyzes the chemical reaction
L-idonate + NAD(P)+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900816 |
13900831 | Long-chain-alcohol dehydrogenase | In enzymology, a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction
a long-chain alcohol + 2 NAD+ + H2O formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900831 |
13900844 | L-rhamnose 1-dehydrogenase | Enzyme
In enzymology, a L-rhamnose 1-dehydrogenase (EC 1.1.1.173) is an enzyme that catalyzes the chemical reaction
L-rhamnofuranose + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900844 |
13900855 | L-threonate 3-dehydrogenase | In enzymology, a L-threonate 3-dehydrogenase (EC 1.1.1.129) is an enzyme that catalyzes the chemical reaction
L-threonate + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900855 |
13900871 | L-threonine 3-dehydrogenase | Class of enzymes
In enzymology, a L-threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction
L-threonine + NAD+ formula_0 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 2D8A, 2DFV, and 2DQ4.
References.
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| https://en.wikipedia.org/wiki?curid=13900871 |
13900893 | L-xylose 1-dehydrogenase | In enzymology, a L-xylose 1-dehydrogenase (EC 1.1.1.113) is an enzyme that catalyzes the chemical reaction
L-xylose + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900893 |
13900909 | Malate dehydrogenase (decarboxylating) | Enzyme
Malate dehydrogenase (decarboxylating) (EC 1.1.1.39) or NAD-malic enzyme (NAD-ME) is an enzyme that catalyzes the chemical reaction
(S)-malate + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13900909 |
13901061 | Malate dehydrogenase (NADP+) | Enzyme class
In enzymology, a malate dehydrogenase (NADP+) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction
(S)-malate + NADP+ formula_0 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 1CIV and 7MDH.
References.
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| https://en.wikipedia.org/wiki?curid=13901061 |
13901078 | Malate dehydrogenase (oxaloacetate-decarboxylating) | Class of enzymes
In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction below
(S)-malate + NAD+ formula_0 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 1DO8, 1EFK, 1EFL, 1GZ3, 1LLQ, 1O0S, 1PJ2, 1PJ3, 1PJ4, 1PJL, 1QR6, 1WW8, and 2DVM.
References.
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| https://en.wikipedia.org/wiki?curid=13901078 |
13901085 | Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) | Enzyme
Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) 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+ formula_0 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 six amino acid residues, and a negatively charged residue at the end of the βB-strand. The primary sequence of the first motif, 240GLGDLG245, is a consensus marker for phosphate binding, evidencing involvement with NADP binding, while the other glycine rich motif adopts a classical Rossmann fold—also a typical marker for NADP cofactor binding. Mutagenesis experiments in maize NADP-ME have supported the current model. Valine substitution for glycine in either motif region rendered the enzyme completely inactive while spectral analysis indicated no major changes from wild-type form. The data is suggestive of direct impairment at a key residue involved in binding or catalysis rather than an inter-domain residue influencing conformational stability.
Additionally, a key arginine residue at site 237 has been shown to interact both with malate and NADP+ substrates, forming key favorable electrostatic interactions to the negatively charged carboxylic-acid and phosphate group respectively. Elucidation of whether the residue plays a role in substrate binding or substrate positioning for catalysis has yet to be determined.
Lysine residue 255 has been implicated as a catalytic base for the enzymes reactivity; however, further studies are still required to conclusively establish its biochemical role.
Structural studies.
As of 2007[ [update]], 3 structures have been solved for this class of enzymes, with PDB accession codes 1GQ2, 1GZ4, and 2AW5.
Biological function.
In a broader context, malic enzymes are found within a wide range of eukaryotic organisms, from fungi to mammals, and beyond that, are shown to localize in range of subcellular locations, including the cytosol, mitochondria, and chloroplast. C4 NADP-ME, specifically, is in plants localized in bundle sheath chloroplasts.
During C4 photosynthesis, an evolved pathway to increase localized CO2 concentrations under the threat of enhanced photorespiration, CO2 is captured within mesophyll cells, fixed as oxaloacetate, converted into malate and released internally within bundle sheath cells to directly feed RuBisCO activity. This release of fixed CO2, triggered by the favorable decarboxylation of malate into pyruvate, is mediated by NADP-dependent malic enzyme. In fact, the significance of NADP-ME activity in CO2 conservation is evidenced by a study performed with transgenic plants exhibiting a NADP-ME loss of function mutation. Plants with the mutation experienced 40% the activity of wild-type NADP-ME and achieved significantly reduced CO2 uptake even at high intercellular levels of CO2, evidencing the biological importance of NADP-ME at regulating carbon flux towards the Calvin cycle.
Enzyme regulation.
NADP-ME expression has been shown to be regulated by abiotic stress factors. For CAM plants, drought conditions cause stoma to largely remain shut to avoid water loss by evapotranspiration, which unfortunately leads to CO2 starvation. In compensation, closed stoma activates the translation of NADP-ME to reinforce high efficiency of CO2 assimilation during the brief intervals of CO2 intake, allowing for carbon fixation to continue.
In addition to regulation at the longer time scale by means of expression control, regulation at the short-time scale can occur through allosteric mechanisms. C4 NADP-ME has been shown to be partially inhibited by its substrate, malate, suggesting two independent binding sites: one at the active site and one at an allosteric site. However, the inhibitory effect exhibits pH-dependence – existent at a pH of 7 but not a pH of 8. The control of enzyme activity due to pH changes align with the hypothesis that NADP-ME is most active while photosynthesis is in progress: Active light reactions leads to a rise in basicity within the chloroplast stroma, the location of NADP-ME, leading to a diminished inhibitory effect of malate on NADP-ME and thereby promoting a more active state. Conversely, slowed light reactions leads to a rise in acidity within the stroma, promoting the inhibition of NADP-ME by malate. Because the high energy products of the light reactions, NADPH and ATP, are required for the Calvin cycle to proceed, a buildup of CO2 without them is not useful, explaining the need for the regulatory mechanism.
This protein may use the morpheein model of allosteric regulation.
Evolution.
NADP-malic enzyme, as all other C4 decarboxylases, did not evolve de novo for CO2 pooling to aid RuBisCO. Rather, NADP-ME was directly transformed from a C3 species in photosynthesis, and even earlier origins from an ancient cystolic ancestor. In the cytosol, the enzyme existed as a series of housekeeping isoforms purposed towards a variety of functions including malate level maintenance during hypoxia, microspore separation, and pathogen defense. In regards to the mechanism of evolution, the C4 functionality is thought to have stemmed from gene duplication error both within promoter regions, triggering overexpression in bundle-sheath cells, and within the coding region, generating neofunctionalization. Selection for CO2 preservation function as well as enhanced water and nitrogen utilization under stressed conditions was then shaped by natural pressures.
References.
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| https://en.wikipedia.org/wiki?curid=13901085 |
13901104 | Mannitol-1-phosphate 5-dehydrogenase | In enzymology, a mannitol-1-phosphate 5-dehydrogenase (EC 1.1.1.17) is an enzyme that catalyzes the chemical reaction
D-mannitol 1-phosphate + NAD+ formula_0 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.
References.
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| https://en.wikipedia.org/wiki?curid=13901104 |
13901126 | Mannitol 2-dehydrogenase | In enzymology, a mannitol 2-dehydrogenase (EC 1.1.1.67) is an enzyme that catalyzes the chemical reaction
D-mannitol + NAD+ formula_0 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 1LJ8 and 1M2W.
References.
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| https://en.wikipedia.org/wiki?curid=13901126 |
13901145 | Mannitol 2-dehydrogenase (NADP+) | In enzymology, a mannitol 2-dehydrogenase (NADP+) (EC 1.1.1.138) is an enzyme that catalyzes the chemical reaction
D-mannitol + NADP+ formula_0 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 1H5Q.
References.
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| https://en.wikipedia.org/wiki?curid=13901145 |
13901157 | Mannitol dehydrogenase | In enzymology, a mannitol dehydrogenase (EC 1.1.1.255) is an enzyme that catalyzes the chemical reaction
D-mannitol + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901157 |
13901169 | Mannose-6-phosphate 6-reductase | In enzymology, a mannose-6-phosphate 6-reductase (EC 1.1.1.224) is an enzyme that catalyzes the chemical reaction
D-mannitol 1-phosphate + NADP+ formula_0 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.
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13901184 | Mannuronate reductase | In enzymology, a mannuronate reductase (EC 1.1.1.131) is an enzyme that catalyzes the chemical reaction
D-mannonate + NAD(P)+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901184 |
13901205 | Methanol dehydrogenase | In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:
CH3OH formula_0 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(EC 1.1.1.244) was first reported in a Gram-positive methylotroph and is an enzyme that catalyzes the chemical reaction:
CH3OH + NAD+ formula_0 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-Dependent MDH.
For Gram-negative bacteria, methanol oxidation occurs in the periplasmic space, facilitated by PQQ-dependent MDH. PQQ-dependent MDHs contain a PQQ prosthetic group, which has the role of capturing electrons from methanol oxidation and passing them to the cytochrome.
MxaFI and XoxF are the genes that encode for PQQ-dependent MDHs. In MxaFI-type MDH, calcium (Ca2+) is encoded as the cofactor for PQQ-dependent methylotrophy. XoxF-type MDHs use lanthanides (Ln3+) as cofactors and are highly selective towards early lanthanides (typically La-Nd). Sm3+, Eu3+, and Gd3+ can support some XoxF-type organisms, but less effectively. Pm3+ and Tb-Lu have shown no evidence of utilization so far.
Many methylotrophs encode both MxaFI and XoxF, but those that encode only one will encode exclusively for XoxF.
O2-Dependent Alcohol Oxidase.
Oxygen-dependent alcohol oxidase (AOX) can be obtained from eukaryotic methylotrophs in the peroxisome of yeasts. Formaldehyde and hydrogen peroxide (H2O2) are formed through the oxidation of methanol. Dihydroxyacetone synthase (DAS) and catalase (CTA) must then transform these toxic chemicals into non-toxic forms to protect the cell. In this process, electrons from methanol are not captured as usable energy by the cell, and are thus lost.
References.
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Further reading.
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13901215 | Methylglyoxal reductase (NADH-dependent) | In enzymology, a methylglyoxal reductase (NADH-dependent) (EC 1.1.1.78) is an enzyme that catalyzes the chemical reaction
(R)-lactaldehyde + NAD+ formula_0 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.
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13901228 | Methylglyoxal reductase (NADPH-dependent) | In enzymology, a methylglyoxal reductase (NADPH-dependent) (EC 1.1.1.283) is an enzyme that catalyzes the chemical reaction
lactaldehyde + NADP+ formula_0 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.
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13901241 | Mevaldate reductase | In enzymology, a mevaldate reductase (EC 1.1.1.32) is an enzyme that catalyzes the chemical reaction
(R)-mevalonate + NAD+ formula_0 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.
In 2022, this entry was deleted from the Enzyme Classification, and is now included in with the entry for Alcohol dehydrogenase.
References.
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| https://en.wikipedia.org/wiki?curid=13901241 |
13901253 | Mevaldate reductase (NADPH) | In enzymology, a mevaldate reductase (NADPH) (EC 1.1.1.33) is an enzyme that catalyzes the chemical reaction
(R)-mevalonate + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901253 |
13901271 | Morphine 6-dehydrogenase | In enzymology, a morphine 6-dehydrogenase (EC 1.1.1.218) is an enzyme that catalyzes the chemical reaction
morphine + NAD(P)+ formula_0 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.
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13901280 | N-acetylhexosamine 1-dehydrogenase | In enzymology, a N-acetylhexosamine 1-dehydrogenase (EC 1.1.1.240) is an enzyme that catalyzes the chemical reaction
N-acetyl-D-glucosamine + NAD+ formula_0 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.
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13901297 | N-acylmannosamine 1-dehydrogenase | In enzymology, a N-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) is an enzyme that catalyzes the chemical reaction
N-acyl-D-mannosamine + NAD+ formula_0 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.
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13901312 | Octanol dehydrogenase | In enzymology, an octanol dehydrogenase (EC 1.1.1.73) is an enzyme that catalyzes the chemical reaction
1-octanol + NAD+ formula_0 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.
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13901334 | Oxaloglycolate reductase (decarboxylating) | In enzymology, an oxaloglycolate reductase (decarboxylating) (EC 1.1.1.92) is an enzyme that catalyzes the chemical reaction
D-glycerate + NAD(P)+ + CO2 formula_0 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.
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13901344 | Pantoate 4-dehydrogenase | In enzymology, a pantoate 4-dehydrogenase (EC 1.1.1.106) is an enzyme that catalyzes the chemical reaction
(R)-pantoate + NAD+ formula_0 (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.
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13901355 | Perillyl-alcohol dehydrogenase | In enzymology, a perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction
perillyl alcohol + NAD+ formula_0 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.
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13901387 | Phosphogluconate dehydrogenase (decarboxylating) | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction
6-phospho-D-gluconate + NADP+ formula_0 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 for this class of enzymes, with PDB accession codes 1PGJ, 1PGN, 1PGO, 1PGP, 1PGQ, 2IYO, 2IYP, 2IZ0, 2IZ1, 2P4Q, and 2PGD.
Enzyme Mechanism.
The conversion of 6-phosphogluconate and NADP to ribulose 5-phosphate, carbon dioxide, and NADPH is believed to follow a sequential mechanism with ordered product release. 6-phosphogluconate is first oxidized to 3-keto-6-phosphogluconate and NADPH is formed and released. Then, the intermediate is decarboxylated, yielding a 1,2-enediol of ribulose 5-phosphate, which tautomerizes to form ribulose 5-phosphate. High levels of NADPH are believed to inhibit the enzyme, while 6-phosphogluconate acts to activate the enzyme.
Biological Function.
6-phosphogluconate dehydrogenase is involved in the production of ribulose 5-phosphate, which is used in nucleotide synthesis, and functions in the pentose phosphate pathway as the main generator of cellular NADPH.
Disease Relevance.
Since NADPH is required by both thioredoxin reductase and glutathione reductase to reduce oxidized thioredoxin and glutathionine, 6-phosphogluconate dehydrogenase is believed to be involved in protecting cells from oxidative damage. Several studies have linked oxidative stress to diseases such as Alzheimer's disease, as well as cancer, These studies have found phosphogluconate dehydrogenase activity to be up-regulated, both in tumor cells and in relevant cortical regions of Alzheimer's patient brains, most likely as a compensatory reaction to highly oxidative environments.
Recently, phosphogluconate dehydrogenase has been posited as a potential drug target for African sleeping sickness (trypanosomiasis). The pentose phosphate pathway protects the trypanosomes from oxidative stress via the generation of NADPH and provides carbohydrate intermediates used in nucleotide synthesis. Structural differences between mammalian and trypanosome 6-phosphogluconate dehydrogenase have allowed for the development of selective inhibitors of the enzyme. Phosphorylated carbohydrate substrate and transition state analogues, non-carbohydrate substrate analogues and triphenylmethane-based compounds are currently being explored.
References.
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13901412 | Prostaglandin-E2 9-reductase | In enzymology, a prostaglandin-E2 9-reductase (EC 1.1.1.189) is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ formula_0 (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 1Q13, 1Q5M, and 2PFG.
References.
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13901449 | Pterocarpin synthase | In enzymology, a pterocarpin synthase (EC 1.1.1.246) is an enzyme that catalyzes the chemical reaction
medicarpin + NADP+ + H2O formula_0 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.
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13901466 | Pyridoxal 4-dehydrogenase | In enzymology, a pyridoxal 4-dehydrogenase (EC 1.1.1.107) is an enzyme that catalyzes the chemical reaction
pyridoxal + NAD+ formula_0 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.
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13901487 | Pyridoxine 4-dehydrogenase | In enzymology, a pyridoxine 4-dehydrogenase (EC 1.1.1.65) is an enzyme that catalyzes the chemical reaction
pyridoxine + NADP+ formula_0 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 donors with NAD+ or NADP+ as acceptors. 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.
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13901509 | Quinate dehydrogenase | In enzymology, a quinate dehydrogenase (EC 1.1.1.24) is an enzyme that catalyzes the chemical reaction
L-quinate + NAD+ formula_0 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.
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13901526 | Retinol dehydrogenase | In enzymology, a retinol dehydrogenase (RDH) (EC 1.1.1.105) is an enzyme that catalyzes the chemical reaction
retinol + NAD+ formula_0 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 (RPE) and is part of short-chain dehydrogenase (SDR) / reductase superfamily. The integral membrane enzyme is anchored to the membranes by its two hydrophobic chains. The catalytic domain of 11-"cis"-retinol dehydrogenase is restricted to the lumenal compartment, suggesting its origin from compartmentalized process. 11-"cis"-retinol dehydrogenase is also mainly associated to the smooth endoplasmic reticulum of RPE cells. The 32-kDa integral membrane protein protein (p32) was found to act as the stereospecific 11-"cis"-retinol dehydrogenase in the presence of NAD+ cofactor, and p32 catalyzes the biosynthesis of 11-"cis" retinal commonly found visual chromophore.
One of the widely studied genes of retinol dehydrogenase "RDH12", which encodes retinol dehydrogenase is part of the superfamily of short-chained alcohol dehydrogenases and reductases. "RDH12" is mainly expressed in neuroretina and is composed of 7 exons encoding a 360-amino acid peptide.
Zinc molecules serve as the ligand cofactor with the cofactor NAD. The retinol will interact with the enzyme at the area between those two cofactors.
However, not all retinol dehydrogenases in visual cycle are identified, and this remains challenging to scientists due to the overlapping expressions and activity redundancy among two large RDH and RDH-like producing classes: microsomal short-chain dehydrogenase/reductase and cytosolic medium-chain alcohol dehydrogenases.
In Bovine, retinol dehydrogenase is found as a part of retinal rod outer segments and shows difficulty when separating from membrane. Its Stokes radius is 8.5 nm in Lubrol 12A9 mixed micelle.
Function.
Retinoid dehydrogenases/reductases (oxidoreductases), including retinol dehydrogenase, catalyze the key oxidation-reduction reactions in the visual cycle, converting vitamin A to 11-"cis" retinal, which is the chromophore of the rod and cone photoreceptors. It is believed that RDHs at rod and cone are different, but related and can catalyze the same reaction. RDH12 is the primary enzyme that reduces all-"trans" retinal released from bleached photopigments during recovery phase in the visual cycle. The RDH12 enzyme can use either "cis" or "trans" retinoid isomers as substrates and can also function as both dehydrogenase (i.e. retinol to retinal) and reductase (i.e. retinal to retinol).
The conversion of retinol to retinal is the rate-limiting step in the retinoic acid biosynthesis. In vertebrates, the retinoic acid is the ligand that controls nuclear receptor signaling pathway, which is responsible for growth and development as well as epithelial maintenance, therefore can be used for cancer and acne treatment. In human, ADH4 can exhibit at least 10 folds higher Vmax/Km than other ADH.
Some retinol dehydrogenases are in extra-ocular tissues, such as human retinol dehydrogenase-4 (RoDH-4), which converts retinol and 1-"cis"-retinol to different aldehydes in liver and skin. It was also found that 13-"cis"-retinoic acid (isotretinoin), 3,4-didehydroretinoic acid, and 3,4-didehydroretinol can act as competitive inhibitor of the 3α-hydroxysteroid dehydrogenase oxidative activity of the enzyme. This can potentially explain how isotretinoin, the active ingredient is Roaccutane (Accutane), can suppress sebaceous glands and be used for severe acne treatment.
Disease relevance.
The missense mutation in gene "rdh5", which codes for microsomal 11-"cis"-retinol dehydrogenase (RDH5), causes fundus albipunctatus, whose symptoms include retinal white-spot accumulation, stationary night blindness caused by delay in cone and rod photopigment regeneration, and elderly cone dystrophy.
At least 20 mutations in "rdh12" gene, which encodes retinol dehydrogenase, can be associated to diseases, including severe and early-onset autosomal recessive retinal dystrophy (arRD), or Leber congenital amaurosis. Patients suffer from cone and rod malfunction since childhood and develop legal blindness when reaching adulthood. This suggests that RDH12 might play a central role in the visual cycle and can be a promising therapeutic target. A possible mechanism of the accelerated degradation among RDH12 mutants is the polyubiquitination by cytosolic ubiquitin ligases and subsequent degradation by proteosome. Its conformation aberration provokes the aforementioned accelerated degradation.
References.
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13901541 | Ribitol 2-dehydrogenase | In enzymology, a ribitol 2-dehydrogenase (EC 1.1.1.56) is an enzyme that catalyzes the chemical reaction
ribitol + NAD+ formula_0 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.
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13901554 | Ribitol-5-phosphate 2-dehydrogenase | In enzymology, a ribitol-5-phosphate 2-dehydrogenase (EC 1.1.1.137) is an enzyme that catalyzes the chemical reaction
D-ribitol 5-phosphate + NAD(P)+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901554 |
13901570 | Testosterone 17b-dehydrogenase (NADP+) | Testosterone 17beta-dehydrogenase (NADP+) (EC 1.1.1.64, "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+ formula_0 androstenedione + NADPH + H+
Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital.
References.
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13901583 | Ribose 1-dehydrogenase (NADP+) | In enzymology, a ribose 1-dehydrogenase (NADP+) (EC 1.1.1.115) is an enzyme that catalyzes the chemical reaction
D-ribose + NADP+ + H2O formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901583 |
13901598 | Salutaridine reductase (NADPH) | In enzymology, a salutaridine reductase (NADPH) (EC 1.1.1.248) is an enzyme that catalyzes the chemical reaction
salutaridinol + NADP+ formula_0 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.
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13901617 | Sepiapterin reductase | Mammalian protein found in Homo sapiens
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+ formula_0 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 variable and the long-term and functional outcome is unknown. To provide a basis for improving the understanding of the epidemiology, genotype/phenotype correlation and outcome of these diseases their impact on the quality of life of patients, and for evaluating diagnostic and therapeutic strategies a patient registry was established by the noncommercial International Working Group on Neurotransmitter Related Disorders (iNTD).
References.
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Further reading.
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13901637 | S-(hydroxymethyl)glutathione dehydrogenase | In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction
S-(hydroxymethyl)glutathione + NAD(P)+ formula_0 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 2FZE and 2FZW.
References.
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13901656 | Sorbose 5-dehydrogenase (NADP+) | In enzymology, a sorbose 5-dehydrogenase (NADP+) (EC 1.1.1.123) is an enzyme that catalyzes the chemical reaction
L-sorbose + NADP+ formula_0 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.
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13901668 | Sorbose reductase | In enzymology, a sorbose reductase (EC 1.1.1.289) is an enzyme that catalyzes the chemical reaction
D-glucitol + NADP+ formula_0 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.
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13901684 | Sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) | In enzymology, a sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) (EC 1.1.1.170) is an enzyme that catalyzes the chemical reaction
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ formula_0 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.
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13901703 | Sulcatone reductase | In enzymology, a sulcatone reductase (EC 1.1.1.260) is an enzyme that catalyzes the chemical reaction
sulcatol + NAD+ formula_0 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.
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13901719 | Tagaturonate reductase | Enzyme
Tagaturonate reductase (EC 1.1.1.58) is an enzyme that catalyzes the chemical reaction
D-altronate + NAD+ formula_0 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.
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13901735 | Tartrate dehydrogenase | In enzymology, a tartrate dehydrogenase (EC 1.1.1.93) is an enzyme that catalyzes the chemical reaction
tartrate + NAD+ formula_0 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.
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13901753 | Testosterone 17beta-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.
Names.
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 (EC 1.1.1.239) catalyzes the reaction
testosterone + NAD+ formula_0 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 (EC 1.1.1.64) catalyzes the reaction
testosterone + NADP+ formula_0 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.
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13901786 | Tetrahydroxynaphthalene reductase | In enzymology, a tetrahydroxynaphthalene reductase (EC 1.1.1.252) is an enzyme that catalyzes the chemical reaction
scytalone + NADP+ formula_0 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 1DOH, 1G0N, and 1G0O.
References.
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13901804 | Tropinone reductase I | In enzymology, a tropinone reductase I (EC 1.1.1.206) is an enzyme that catalyzes the chemical reaction
tropine + NADP+ formula_0 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.
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13901822 | Tropinone reductase II | In enzymology, a tropinone reductase II (EC 1.1.1.236) is an enzyme that catalyzes the chemical reaction
pseudotropine + NADP+ formula_0 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 1AE1, 1IPE, 1IPF, 1XHL, 2AE1, and 2AE2.
References.
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13901839 | UDP-glucose 6-dehydrogenase | Mammalian protein found in humans
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:
Biochemistry.
In enzymology, a UDP-glucose 6-dehydrogenase (EC 1.1.1.22) is an enzyme that catalyzes the chemical reaction
UDP-glucose + 2 NAD+ + H2O formula_0 UDP-glucuronate + 2 NADH + 2 H+
The 3 substrates of this enzyme are UDP-glucose, NAD+, and H2O, whereas its 3 products are UDP-glucuronate, NADH, and H+
References:
References.
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Further reading.
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13901849 | UDP-N-acetylglucosamine 6-dehydrogenase | Class of enzymes
In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase (EC 1.1.1.136) is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O formula_0 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.
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13901862 | UDP-N-acetylmuramate dehydrogenase | Class of enzymes
In enzymology, an UDP-N-acetylmuramate dehydrogenase (EC 1.3.1.98) is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-alpha-D-muramate + NADP+ formula_0 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 1HSK, 1MBB, 1MBT, 1UXY, 2GQT, 2GQU, 2MBR, and 2Q85.
References.
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13901872 | Ureidoglycolate dehydrogenase | Class of enzymes
In enzymology, an ureidoglycolate dehydrogenase (EC 1.1.1.154) is an enzyme that catalyzes the chemical reaction
(S)-ureidoglycolate + NAD(P)+ formula_0 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 1WTJ and 1XRH.
References.
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13901889 | Uronate dehydrogenase | Class of enzymes
In enzymology, an uronate dehydrogenase (EC 1.1.1.203) is an enzyme that catalyzes the chemical reaction
D-galacturonate + NAD+ + H2O formula_0 D-galactaro-1,5-lactone + NADH + H+
The 3 substrates of this enzyme are D-galacturonate, NAD+, and H2O, whereas its 3 products are D-galactaro-1,5-lactone (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.
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| https://en.wikipedia.org/wiki?curid=13901889 |
13901997 | 12alpha-hydroxysteroid dehydrogenase | Class of enzymes
In enzymology, a 12alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13901997 |
13902007 | 12beta-hydroxysteroid dehydrogenase | Class of enzymes
In enzymology, a 12beta-hydroxysteroid dehydrogenase (EC 1.1.1.238) is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12beta-trihydroxy-5beta-cholanate + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13902007 |
13902025 | 1,3-propanediol dehydrogenase | Class of enzymes
In enzymology, a 1,3-propanediol dehydrogenase (EC 1.1.1.202) is an enzyme that catalyzes the chemical reaction
propane-1,3-diol + NAD+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13902025 |
13902037 | 1,5-anhydro-D-fructose reductase | Class of enzymes
In enzymology, a 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-glucitol + NADP+ formula_0 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 2GLX.
References.
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| https://en.wikipedia.org/wiki?curid=13902037 |
13902054 | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) | Enzyme in the family of oxidoreductases
In enzymology, a 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) (EC 1.1.1.292) is an enzyme that catalyzes the chemical reaction
1,5-anhydro-D-mannitol + NADP+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13902054 |
13902069 | 15-hydroxyicosatetraenoate dehydrogenase | Class of enzymes
In enzymology, a 15-hydroxyicosatetraenoate dehydrogenase (EC 1.1.1.232) is an enzyme that catalyzes the chemical reaction
(15"S")-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)+ formula_0 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 (15"S")-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.
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| https://en.wikipedia.org/wiki?curid=13902069 |
13902077 | 15-hydroxyprostaglandin-D dehydrogenase (NADP+) | Class of enzymes
In enzymology, a 15-hydroxyprostaglandin-D dehydrogenase (NADP+) (EC 1.1.1.196) is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP+ formula_0 (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.
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| https://en.wikipedia.org/wiki?curid=13902077 |
13902087 | 15-hydroxyprostaglandin dehydrogenase (NAD+) | Class of enzymes
Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase (NAD+), (EC 1.1.1.141), is an enzyme that catalyzes the following chemical reaction:
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ formula_0 (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 2GDZ.
References.
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| https://en.wikipedia.org/wiki?curid=13902087 |
13902100 | 15-hydroxyprostaglandin dehydrogenase (NADP+) | Enzyme
In enzymology, a 15-hydroxyprostaglandin dehydrogenase (NADP+) (EC 1.1.1.197) is an enzyme that catalyzes the chemical reaction
(13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ formula_0 (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 2PFG.
References.
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| https://en.wikipedia.org/wiki?curid=13902100 |
13902113 | 15-hydroxyprostaglandin-I dehydrogenase (NADP+) | Class of enzymes
In enzymology, a 15-hydroxyprostaglandin-I dehydrogenase (NADP+) (EC 1.1.1.231) is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13- dienoate + NADP+ formula_0 (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.
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| https://en.wikipedia.org/wiki?curid=13902113 |
13902128 | 16-alpha-hydroxysteroid dehydrogenase | Class of enzymes
In enzymology, a 16alpha-hydroxysteroid dehydrogenase (EC 1.1.1.147) is an enzyme that catalyzes the chemical reaction
a 16alpha-hydroxysteroid + NAD(P)+ formula_0 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.
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| https://en.wikipedia.org/wiki?curid=13902128 |
13902134 | 20alpha-hydroxysteroid dehydrogenase | Class of enzymes
In enzymology, a 20-α-hydroxysteroid dehydrogenase (EC 1.1.1.149) is an enzyme that catalyzes the chemical reaction
17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ formula_0 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 parturition through reduction of progesterone blood concentration. In mice, 20alpha-HSD is also expressed in the adrenals, kidneys, brain, thymus, T cells and bone marrow. Its induction in hematopoietic cells was used as an assay for the identification of T cell derived factor interleukin-3. In addition, the enzyme reduces and inactivates 17-deoxycorticosterone, the precursor of aldosterone and corticosterone.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1MRQ (AKR1C1), 1Q13, and 1Q5M.
AKR1C1, AKR1C2, and AKR1C3
Enzymes.
AKR1C1 has high catalytic efficiency as a 20α-HSD and AKR1C2 and AKR1C3 efficiently catalyze this reaction as well.
References.
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Further reading.
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| https://en.wikipedia.org/wiki?curid=13902134 |
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