In
enzymology, a
hydroxypyruvate reductase is an
enzyme that
catalyzes the
chemical reaction- D-glycerate + NAD(P)+ hydroxypyruvate + NAD(P)H + H+
The 3 substrates of this enzyme are D-glycerate, NAD+, and NADP+, whereas its 4 products are hydroxypyruvate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glycerate:NADP+ 2-oxidoreductase. Other names in common use include beta-hydroxypyruvate reductase, NADH:hydroxypyruvate reductase, and D-glycerate dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.
References
- Kleczkowski LA and Edwards GE "Identification of hydroxypyruvate and glyoxylate reductases in maize leaves". Plant Physiol. 91 278–286.
- Kleczkowski LA, Randall DD "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.
- Kohn LD, Jakoby WB "Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase)". J. Biol. Chem. 243 2494–9.
External links
- The CAS registry number for this enzyme class is .
Gene Ontology (GO) codes