| EC |
2.6.1.77 |
| Accepted name: |
taurine—pyruvate aminotransferase |
| Reaction: |
taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde |
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For diagram of reaction, click here |
| Glossary: |
2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate |
| Other name(s): |
Tpa |
| Systematic name: |
taurine:pyruvate aminotransferase |
| Comments: |
The enzyme from Bilophila wadsworthia requires pyridoxal 5′-phosphate as a cofactor, is reversible, and catalyses the first step of anaerobic taurine degradation. Hypotaurine (i.e. 2-aminoethanesulfinate) and β-alanine are also significant donors of an amino group. Unlike, EC 2.6.1.55, taurine—2-oxoglutarate transaminase, 2-oxoglutarate is not an acceptor of amino groups. |
| Links to other databases: |
BRENDA, EXPASY, IUBMB, KEGG, 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. [PMID: 11082195] |
| 2. |
Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1–6. [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. [PMID: 11728723] |
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| [EC 2.6.1.77 created 2003] |
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