Beta-alanine—pyruvate transaminase
| Beta-alanine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Beta-alanine-pyruvate transaminase homotetramer, Pseudomonas aeruginosa | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.18 | ||||||||
| CAS no. | 9030-47-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the reversible chemical reaction
The two substrates of this enzyme first characterised from Pseudomonas fluorescens are L-alanine and 3-oxopropanoic acid. Its products are pyruvic acid and β-alanine.[1][2]
This enzyme is a transferase, specifically a transaminase, 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. It participates in four metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It uses pyridoxal phosphate as a cofactor.[3]
References
- ↑ Hayaishi, Osamu; Nishizuka, Yasutomi; Tatibana, Masamiti; Takeshita, Masazumi; Kuno, Sigeru (1961). "Enzymatic Studies on the Metabolism of β-Alanine". Journal of Biological Chemistry. 236 (3): 781–790. doi:10.1016/S0021-9258(18)64309-1. PMID 13712439.
- ↑ Stinson, Robert A.; Spencer, Mary S. (1969). "Β-Alanine aminotransferase(s) from a plant source". Biochemical and Biophysical Research Communications. 34 (1): 120–127. doi:10.1016/0006-291X(69)90537-3. PMID 5762452.
- ↑ Enzyme 2.6.1.18 at KEGG Pathway Database.