Serine-pyruvate transaminase

Serine-pyruvate transaminase

In enzymology, a serine-pyruvate transaminase is an enzyme that catalyzes the chemical reaction

L-serine + pyruvate rightleftharpoons 3-hydroxypyruvate + L-alanine

Thus, the two substrates of this enzyme are L-serine and pyruvate, whereas its two products are 3-hydroxypyruvate and L-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:pyruvate aminotransferase. Other names in common use include SPT, and hydroxypyruvate:L-alanine transaminase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

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


  • Cheung GP, Rosenblum IY, Sallach HJ "Comparative studies of enzymes related to serine metabolism in higher plants". Plant. Physiol. 43 1813–20.
  • Kretovich VL and Stepanovich KM "[The synthesis of serine from hydroxypyruvate in plants.]". Dokl. Akad. Nauk S.S.S.R. 139 488–490.
  • Sallach HJ "Formation of serine from hydroxypyruvate and L-alanine". J. Biol. Chem. 223 1101–1108.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes

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