Taurine-pyruvate aminotransferase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 2.6.1.77
- BRENDA references for 2.6.1.77 (Recommended.)
- PubMed references for 2.6.1.77
- PubMed Central references for 2.6.1.77
- Google Scholar references for 2.6.1.77
- Laue H, Cook AM (2000). "Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia". Eur. J. Biochem. 267: 6841–8. doi:. PMID 11082195.
- Cook AM, Denger K (2002). "Dissimilation of the C2 sulfonates". Arch. Microbiol. 179: 1–6. doi:. 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: 105–11. doi:. PMID 11728723.

