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Glycerate dehydrogenase

Glycerate Dehydrogenase
Glyoxylate Reductase Hydroxypyruvate Reductase.png
Glyoxylate Reductase/Hydroxypyruvate Reductase. Quaternary structure of 2 homodimers of GRHPR bound to NADPH and (D)-glycerate.
Identifiers
EC number 1.1.1.29
CAS number 9028-37-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

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

Thus, the two substrates of this enzyme are (R)-glycerate and NAD+, whereas its 3 products are hydroxypyruvate, NADH, and H+. However, in nature these enzymes have the ability to catalyze the reverse reaction as well. That is, hydroxypyruvate, NADH, and H+ can act as the substrates while (R)-glycerate and NAD+ are formed as products. Additionally, NADPH can take the place of NADH in this reaction.

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 (due to the reversibility of the reaction). This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism.

This class of enzyme is part of a larger superfamily of enzymes known as D-2-hydroxy-acid dehydrogenases. Many organisms from Hyphomicrobium methylovorum to humans have some form of the glycerate dehydrogenase protein. There are currently several structures that have been solved for this class of enzyme including those for the two mentioned above with PDB access code 1GDH, D-glycerate dehydrogenase, and the human homolog Glyoxylate Reductase/Hydroxypyruvate Reductase(GRHPR), 2WWR.


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Wikipedia

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