The Enzyme Database

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EC 1.1.1.95     
Accepted name: phosphoglycerate dehydrogenase
Reaction: (1) 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH + H+
(2) 2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
For diagram of the phosphoserine pathway of serine biosynthesis, click here
Other name(s): D-3-phosphoglycerate:NAD+ oxidoreductase; α-phosphoglycerate dehydrogenase; 3-phosphoglycerate dehydrogenase; 3-phosphoglyceric acid dehydrogenase; D-3-phosphoglycerate dehydrogenase; glycerate 3-phosphate dehydrogenase; glycerate-1,3-phosphate dehydrogenase; phosphoglycerate oxidoreductase; phosphoglyceric acid dehydrogenase; SerA; 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
Comments: 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: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-29-0
References:
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 (1968) 2081. [PMID: 4384871]
2.  Pizer, L.I. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238 (1963) 3934–3944. [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 (1996) 232–239. [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 (1995) 69–76. [PMID: 7719856]
[EC 1.1.1.95 created 1972, modified 2006]
 
 


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