EC - Phosphoglycerate dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
phosphoglycerate dehydrogenase
Other names:
3-phosphoglycerate dehydrogenase
3-phosphoglyceric acid dehydrogenase
α-phosphoglycerate dehydrogenase
D-3-phosphoglycerate dehydrogenase
D-3-phosphoglycerate:NAD+ oxidoreductase
glycerate 3-phosphate dehydrogenase
glycerate-1,3-phosphate dehydrogenase
phosphoglycerate oxidoreductase
phosphoglyceric acid dehydrogenase
3-phosphoglycerate:NAD+ 2-oxidoreductase
SerA 3PG dehydrogenase
3PHP reductase
αKG reductase
D- and L-HGA
Systematic name:
3-phospho-D-glycerate:NAD+ 2-oxidoreductase



This enzyme catalyses the first committed step in the phosphoserine pathway of serine biosynthesis in Escherichia coli [2,3]. Reaction (1) occurs predominantly in the reverse direction and is inhibited by serine and glycine. The enzyme is unusual in that it also acts as a D- and L-2-hydroxyglutarate dehydrogenase (with the D-form being the better substrate) and as a 2-oxoglutarate reductase [3]. It has been postulated [3] that the cellular 2-oxoglutarate concentration may regulate serine biosynthesis and one-carbon metabolism directly by modulating the activity of this enzyme.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00063
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004617
CAS Registry Number: 9075-29-0
UniProtKB/Swiss-Prot: (29) [show] [UniProt]


  1. Sugimoto, E. and Pizer, L.I.
    The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase.
    J. Biol. Chem. 243: 2081-1089 (1968). [PMID: 4384871]
  2. Pizer, L.I.
    The pathway and control of serine biosynthesis in Escherichia coli.
    J. Biol. Chem. 238: 3934-3944 (1963). [PMID: 14086727]
  3. Zhao, G. and Winkler, M.E.
    A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria.
    J. Bacteriol. 178: 232-239 (1996). [PMID: 8550422]
  4. Schuller, D.J., Grant, G.A. and Banaszak, L.J.
    The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
    Nat. Struct. Biol. 2: 69-76 (1995). [PMID: 7719856]

[EC created 1972, modified 2006]