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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Enzyme: taurine:pyruvate aminotransferase

Gene: tpa Accession Number: G-2101 (MetaCyc)

Synonyms: taurine:pyruvate transaminase

Species: Bilophila wadsworthia RZATAU

Subunit composition of taurine:pyruvate aminotransferase = [Tpa]4
         taurnine:pyruvate aminotransferase subunit = Tpa

Summary:
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].

Locations: cytosol

Molecular Weight of Polypeptide: 49.7 kD (from nucleotide sequence), 51 kD (experimental)

Molecular Weight of Multimer: 197 kD (experimental)

Unification Links: ModBase:Q9APM5 , Protein Model Portal:Q9APM5 , Swiss-Model:Q9APM5 , UniProt:Q9APM5

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

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol


Enzymatic reaction of: taurine:pyruvate aminotransferase

Synonyms: Tpa

EC Number: 2.6.1.77

pyruvate + taurine <=> L-alanine + sulfoacetaldehyde

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.

Alternative Substrates for pyruvate: oxaloacetate [Laue00 ] , 2-oxobutanoate [Laue00 ]

Alternative Substrates for taurine: β-alanine [Laue00 ] , hypotaurine [Laue00 ]

In Pathways: superpathway of taurine degradation , taurine degradation I

Summary:
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].

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Laue00]


References

Laue00: Laue H, Cook AM (2000). "Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia." Eur J Biochem 267(23);6841-8. PMID: 11082195


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc12.