Serine—pyruvate transaminase
| serine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.51 | ||||||||
| CAS number | 9030-88-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a serine-pyruvate transaminase (EC 2.6.1.51) is an enzyme that catalyzes the chemical reaction
- L-serine + pyruvate 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 1J04.
References
- Cheung GP, Rosenblum IY, Sallach HJ (1968). "Comparative studies of enzymes related to serine metabolism in higher plants". Plant. Physiol. 43 (11): 1813–20. doi:10.1104/pp.43.11.1813. PMC 1087083
. PMID 5699148. - Kretovich, V. L.; K. M. Stepanovich (1961). Синтез серина из оксипировнногратной кислоты в растениях [The synthesis of serine from hydroxypyruvate in plants]. Doklady Akademii Nauk SSSR (in Russian). 139: 488–490.
- Sallach HJ (1956). "Formation of serine from hydroxypyruvate and L-alanine". J. Biol. Chem. 223: 1101–1108.
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