EC - Taurine—pyruvate aminotransferase

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IntEnz Enzyme Nomenclature


Accepted name:
taurine—pyruvate aminotransferase
Other name:
Systematic name:
taurine:pyruvate aminotransferase




The enzyme from 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, taurine—2-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00519
Structural data: CSA , EC2PDB
Gene Ontology: GO:0031299


  1. Laue, H. and Cook, A.M.
    Biochemical and molecular characterization of taurine:pyruvate transaminase from the anaerobe Bilophila wadsworthia.
    Eur. J. Biochem. 267 : 6841-6848 (2000). [PMID: 11082195]
  2. Cook, A.M. and Denger, K.
    Dissimilation of the C2 sulfonates.
    Arch. Microbiol. 179 : 1-6 (2002). [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 : 105-111 (2001). [PMID: 11728723]
  4. Felux, A. K., Denger, K., Weiss, M., Cook, A. M., Schleheck, D.
    Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination followed by spontaneous desulfination to yield acetaldehyde and, finally, acetate for growth.
    J. Bacteriol. 195 : 2921-2930 (2013). [PMID: 23603744]

[EC created 2003]