Hydroxypyruvate reductase

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

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

See also

• Oxidoreductases
• Enzymes
• Enzyme Commission number (EC number)

References

• Kleczkowski LA; Edwards GE (1989). "Identification of hydroxypyruvate and glyoxylate reductases in maize leaves". Plant Physiol. 91 (1): 278–286. doi:10.1104/pp.91.1.278. PMC 1061987. PMID 16667010.
• 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 (1): 145–52. doi:10.1042/bj2500145. PMC 1148826. PMID 3281657.
• Kohn LD, Jakoby WB (1968). "Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase)". J. Biol. Chem. 243 (10): 2494–9. PMID 4385077.

This page was last edited on 26 August 2023, at 14:31