Serine-pyruvate transaminase

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In enzymology, a serine-pyruvate transaminase (EC 2.6.1.51) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1J04.

[edit] References

IUBMB entry for 2.6.1.51
BRENDA references for 2.6.1.51 (Recommended.)
PubMed references for 2.6.1.51
PubMed Central references for 2.6.1.51
Google Scholar references for 2.6.1.51
Cheung GP, Rosenblum IY, Sallach HJ (1968). "Comparative studies of enzymes related to serine metabolism in higher plants". Plant. Physiol. 43: 1813–20. PMID 5699148.
Kretovich VL and Stepanovich KM (1961). "[The synthesis of serine from hydroxypyruvate in plants.]". Dokl. Akad. Nauk S.S.S.R. 139: 488–490.
Sallach HJ (1956). "Formation of serine from hydroxypyruvate and L-alanine". J. Biol. Chem. 223: 1101–1108.