|Gene:||tpa||Accession Number: G-2101 (MetaCyc)|
Synonyms: taurine:pyruvate transaminase
Species: Bilophila wadsworthia RZATAU
Taurine:pyruvate aminotransferase from Bilophila wadsworthia is a homotetramer [Laue00]. The tetrameric structure is similar to that of ω-amino acid:pyruvate aminotransferase from Pseudomonas putida with its native molecular mass of 172 kDa and a 49 kDa subunit [Laue00].
Molecular Weight of Polypeptide: 49.7 kD (from nucleotide sequence), 51 kD (experimental)
Molecular Weight of Multimer: 197 kD (experimental)
Relationship Links: InterPro:IN-FAMILY:IPR005814 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , Panther:IN-FAMILY:PTHR11986 , Pfam:IN-FAMILY:PF00202 , Prosite:IN-FAMILY:PS00600
|Cellular Component:||GO:0005829 - cytosol|
Enzymatic reaction of: taurine:pyruvate aminotransferase
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
This reaction is reversible.
Taurine:pyruvate aminotransferase catalyzes the initial step in taurine degradation in the anaerobic bacterium, Bilophila wadsworthia [Laue00]. Tpa from Bilophila wadsworthia was partially purified and characterized [Laue00]. Pyridoxal 5'-phosphate was required in all of the buffers in order to purify an active enzyme [Laue00]. UV/Vis spectra of Tpa were reported in [Laue00] and support the presence of pyridoxal 5'-phosphate [Laue00].
The pH optimum was 9.0 [Laue00].
The apparent KM for taurine, pyruvate, and hypotaurine were determined to be 7.1, 0.82, and 8.1 mM [Laue00].
The deduced amino acid sequence of Tpa was 33%, 32%, and 31% identical to those of the diaminopelargonate-aminotransferase from Bacillus subtilis, ω-amino acid:pyruvate aminotransferase from Pseudomonas putida, and acetylornithine aminotransferase from E. coli [Laue00].
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493