Glycerate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a glycerate dehydrogenase (EC 1.1.1.29) is an enzyme that catalyzes the chemical reaction

(R)-glycerate + NAD⁺ $\rightleftharpoons$ hydroxypyruvate + NADH + H⁺

Thus, the two substrates of this enzyme are (R)-glycerate and NAD⁺, whereas its 3 products are hydroxypyruvate, 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)-glycerate:NAD+ oxidoreductase. Other names in common use include D-glycerate dehydrogenase, and hydroxypyruvate reductase. This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1GDH.

[edit] References

IUBMB entry for 1.1.1.29
BRENDA references for 1.1.1.29 (Recommended.)
PubMed references for 1.1.1.29
PubMed Central references for 1.1.1.29
Google Scholar references for 1.1.1.29
HOLZER H, HOLLDORF A (1957). "[Isolation of D-glycerate dehydrogenase, some properties of the enzyme and its application to the enzymic-optic determination of hydroxypyruvate in presence of pyruvate.]". Biochem. Z. 329: 292–312. PMID 13522707.
STAFFORD HA, MAGALDI A, VENNESLAND B (1954). "The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants". J. Biol. Chem. 207: 621–9. PMID 13163046.