Enzyme - Phosphoglycerate dehydrogenase

Alternative Name(s)
  • 3-phosphoglycerate dehydrogenase.
  • D-3-phosphoglycerate dehydrogenase.
  • Glycerate 3-phosphate dehydrogenase.
  • Phosphoglycerate oxidoreductase.
  • Glycerate-1,3-phosphate dehydrogenase.
  • Phosphoglyceric acid dehydrogenase.
  • 3PHP reductase.
  • Alpha-KG reductase.
  • PGDH.
  • Alpha-phosphoglycerate dehydrogenase.
  • 3-phosphoglyceric acid dehydrogenase.

Catalytic Activity

(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH


There are no Cofactors for this Enzyme

Reaction Mechanism

    3-phosphoglycerate dehydrogenase catalyses the oxidation of D-3-phosphoglycerate to 3-phosphohydroxypyruvate with concurrent reduction of NAD+ to NADH. This reaction is the first committed step in serine biosynthesis. In the following steps transamination of 3-phosphohydroxypyruvate with glutamate yields phosphoserine and the action of a phosphatase completes the biosynthesis. In prokaryotes and plants 3-phosphoglycerate dehydrogenase is inhibited by serine in an allosteric fashion.

    3-phosphoglycerate utilises a charge-relay system involving His 292 and Glu 269. His 292 deprotonates the C2 hydroxyl group of 3-phosphoglycerate as a hydride ion is transferred from C2 to NAD+. Glu 269 functions to modify the pKa of His 292, allowing it to carry out its catalytic role.
    Catalytic Residues
    AA Uniprot Uniprot Resid PDB PDB Resid
    His P0A9T0 292 1psd 291
    Glu P0A9T0 269 1psd 268
    Step Components

    inferred reaction step, hydride transfer, aromatic bimolecular nucleophilic addition, proton transfer, native state of enzyme regenerated, overall reactant used, overall product formed

    Step 1.

    His292 depronates the hydroxyl group of 3-phosphoglycerate. This is facilitated by Glu269. A hydride from the hydroxyl carbon of 3-phosphoglycerate is transferred to NAD+ in an aromatic bimolecular nucleophilic addition reaction.

    Step 2.

    In an inferred step His292 is deprotonated to regenerate the native state of the enzyme.


    The products of the reaction.

Reaction Parameters

  • Kinetic Parameters
    Organism KM Value [mM] Substrate Comment
    Arabidopsis thaliana 0.000017 2-oxoglutarate pH 6.0, 25°C
    Mycobacterium tuberculosis 0.14 2-oxoglutarate mutant enzyme R72L, pH 7.0, temperature not specified in the publication
    Entamoeba histolytica 0.216 3-phospho-D-glycerate mutant enzyme K263A, at pH 9.0 and 25°C
    Escherichia coli 0.5 3-phospho-D-glycerate pH and temperature not specified in the publication
    Marchantia polymorpha 51 3-phospho-D-glycerate pH 9.0, temperature not specified in the publication
  • Temperature
    Organism Temperature Range Comment
    Bombyx mori 20 - 50 at temperatures of 20-50°C, the activity of the enzyme is greater than 80% of maximal activity
  • pH
    Organism pH Range Comment
    Bombyx mori 4 - 9 pH 4.0: about 82% of maximal activity, pH 9.0: about 80% of maximal activity
    Glycine max 5 - 7.8 about 50% of activity maximum at pH 5 and 7.8, NADH oxidation
    Mycobacterium tuberculosis 5.2 - 5.7 at approximately pH 5.7 the activity starts increasing again and reaches a new optimum at approximately pH 5.2 before decreasing once again
    Escherichia coli 5.5 - 8.5 Tris buffer and phosphate buffer
    Entamoeba histolytica 6.5 - 8 enzymatic activity decreases below pH 6.5

Associated Proteins

Protein name Organism
D-3-phosphoglycerate dehydrogenase 2, chloroplastic Mouse-ear cress
D-3-phosphoglycerate dehydrogenase 1, chloroplastic Mouse-ear cress
D-3-phosphoglycerate dehydrogenase 3, chloroplastic Mouse-ear cress
Putative D-3-phosphoglycerate dehydrogenase Fission yeast
D-3-phosphoglycerate dehydrogenase 1 Baker's yeast