Hydroxypyruvate reductase

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In enzymology, a hydroxypyruvate reductase (EC 1.1.1.81) is an enzyme that catalyzes the chemical reaction

D-glycerate + NAD(P)+ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.1.1.81
BRENDA references for 1.1.1.81 (Recommended.)
PubMed references for 1.1.1.81
PubMed Central references for 1.1.1.81
Google Scholar references for 1.1.1.81
Kleczkowski LA and Edwards GE (1989). "Identification of hydroxypyruvate and glyoxylate reductases in maize leaves". Plant Physiol. 91: 278–286.
Kleczkowski LA, Randall DD (1988). "Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases". Biochem. J. 250: 145–52. PMID 3281657.
Kohn LD, Jakoby WB (1968). "Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase)". J. Biol. Chem. 243: 2494–9. PMID 4385077.