Beta-alanine—pyruvate transaminase
| beta-alanine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.18 | ||||||||
| CAS number | 9030-47-1 | ||||||||
| 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 | ||||||||
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In enzymology, a beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the chemical reaction
- L-alanine + 3-oxopropanoate pyruvate + beta-alanine
Thus, the two substrates of this enzyme are L-alanine and 3-oxopropanoate, whereas its two products are pyruvate and beta-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-alanine:3-oxopropanoate aminotransferase. Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. This enzyme participates in 4 metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
References
- HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S (1961). "Enzymatic studies on the metabolism of beta-alanine". J. Biol. Chem. 236: 781–90. PMID 13712439.
- Stinson RA, Spencer MS (1969). "Beta alanine aminotransferase (s) from a plant source". Biochem. Biophys. Res. Commun. 34 (1): 120–7. doi:10.1016/0006-291X(69)90537-3. PMID 5762452.