Taurine—pyruvate aminotransferase
| taurine-pyruvate aminotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.77 | ||||||||
| 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 taurine-pyruvate aminotransferase (EC 2.6.1.77) is an enzyme that catalyzes the chemical reaction
- taurine + pyruvate L-alanine + 2-sulfoacetaldehyde
Thus, the two substrates of this enzyme are taurine and pyruvate, whereas its two products are L-alanine and 2-sulfoacetaldehyde.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is taurine:pyruvate aminotransferase. This enzyme is also called Tpa. This enzyme participates in taurine and hypotaurine metabolism.
References
- Laue H, Cook AM (2000). "Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia". Eur. J. Biochem. 267 (23): 6841–8. doi:10.1046/j.1432-1033.2000.01782.x. PMID 11082195.
- Cook AM, Denger K (2002). "Dissimilation of the C2 sulfonates". Arch. Microbiol. 179 (1): 1–6. doi:10.1007/s00203-002-0497-0. PMID 12471498.
- Masepohl B, Fuhrer F, Klipp W (2001). "Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source". FEMS Microbiol. Lett. 205 (1): 105–11. doi:10.1111/j.1574-6968.2001.tb10932.x. PMID 11728723.
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