Serine—pyruvate transaminase
| serine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Serine-pyruvate transaminase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.51 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1J04.
References
[edit]- 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 (2): 1101–1108. doi:10.1016/S0021-9258(18)65108-7.
