The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.6.1.77     
Accepted name: taurine—pyruvate aminotransferase
Reaction: taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
For diagram of reaction, click here
Glossary: taurine = 2-aminoethanesulfonate
hypotaurine = 2-aminoethanesulfinate
2-sulfoacetaldehyde = 2-oxoethanesulfonate
2-sulfinoacetaldehyde = 2-oxoethanesulfinate
Other name(s): Tpa
Systematic name: taurine:pyruvate aminotransferase
Comments: The enzyme from the bacterium Bilophila wadsworthia requires pyridoxal 5′-phosphate as a cofactor, and catalyses a reversible reaction that starts an anaerobic taurine degradation pathway. β-Alanine is also a significant amino group donor. The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyses to sulfite and acetaldehyde. Unlike, EC 2.6.1.55, taurine—2-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51901-18-9
References:
1.  Laue, H. and Cook, A.M. Biochemical and molecular characterization of taurine:pyruvate transaminase from the anaerobe Bilophila wadsworthia. Eur. J. Biochem. 267 (2000) 6841–6848. [DOI] [PMID: 11082195]
2.  Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1–6. [DOI] [PMID: 12471498]
3.  Masepohl, B., Fuhrer, F. and Klipp, W. Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source. FEMS Microbiol. Lett. 205 (2001) 105–111. [DOI] [PMID: 11728723]
4.  Felux, A.K., Denger, K., Weiss, M., Cook, A.M. and Schleheck, D. Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination followed by spontaneous desulfination to yield acetaldehyde and, finally, acetate for growth. J. Bacteriol. 195 (2013) 2921–2930. [DOI] [PMID: 23603744]
[EC 2.6.1.77 created 2003]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald