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Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia

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2000

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Laue, Heike
Cook, Alasdair M.

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European Journal of Biochemistry. 2000, 267(23), pp. 6841-6848. eISSN 0014-2956. Available under: doi: 10.1046/j.1432-1033.2000.01782.x

Zusammenfassung

Bilophila wadsworthia RZATAU is a Gram-negative bacterium which converts the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and sulfide in an anaerobic respiration. Taurine:pyruvate aminotransferase (Tpa) catalyses the initial metabolic reaction yielding alanine and sulfoacetaldehyde. We purified Tpa 72-fold to apparent homogeneity with an overall yield of 89%. The purified enzyme did not require addition of pyridoxal 5'-phosphate, but highly active enzyme was only obtained by addition of pyridoxal 5'-phosphate to all buffers during purification. SDS/PAGE revealed a single protein band with a molecular mass of 51 kDa. The apparent molecular mass of the native enzyme was 197 kDa as determined by gel filtration, which indicates a homotetrameric structure. The kinetic constants for taurine were: Km = 7.1 mm, Vmax = 1.20 nmol·s-1, and for pyruvate: Km = 0.82 mm, Vmax = 0.17 nmol·s-1. The purified enzyme was able to transaminate hypotaurine (2-aminosulfinate), taurine, beta-alanine and with low activity cysteine and 3-aminopropanesulfonate. In addition to pyruvate, 2-ketobutyrate and oxaloacetate were utilized as amino group acceptors. We have sequenced the encoding gene (tpa). It encoded a 50-kDa peptide, which revealed 33% identity to diaminopelargonate aminotransferase from Bacillus subtilis.

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570 Biowissenschaften, Biologie

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aminotransferase, Bilophila wadsworthia, taurine, anaerobic metabolism, pyridoxal 5'-phosphate

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ISO 690LAUE, Heike, Alasdair M. COOK, 2000. Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia. In: European Journal of Biochemistry. 2000, 267(23), pp. 6841-6848. eISSN 0014-2956. Available under: doi: 10.1046/j.1432-1033.2000.01782.x
BibTex
@article{Laue2000Bioch-7868,
  year={2000},
  doi={10.1046/j.1432-1033.2000.01782.x},
  title={Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia},
  number={23},
  volume={267},
  journal={European Journal of Biochemistry},
  pages={6841--6848},
  author={Laue, Heike and Cook, Alasdair M.}
}
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    <dcterms:abstract xml:lang="eng">Bilophila wadsworthia RZATAU is a Gram-negative bacterium which converts the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and sulfide in an anaerobic respiration. Taurine:pyruvate aminotransferase (Tpa) catalyses the initial metabolic reaction yielding alanine and sulfoacetaldehyde. We purified Tpa 72-fold to apparent homogeneity with an overall yield of 89%. The purified enzyme did not require addition of pyridoxal 5'-phosphate, but highly active enzyme was only obtained by addition of pyridoxal 5'-phosphate to all buffers during purification. SDS/PAGE revealed a single protein band with a molecular mass of 51 kDa. The apparent molecular mass of the native enzyme was 197 kDa as determined by gel filtration, which indicates a homotetrameric structure. The kinetic constants for taurine were: Km = 7.1 mm, Vmax = 1.20 nmol·s-1, and for pyruvate: Km = 0.82 mm, Vmax = 0.17 nmol·s-1. The purified enzyme was able to transaminate hypotaurine (2-aminosulfinate), taurine, beta-alanine and with low activity cysteine and 3-aminopropanesulfonate. In addition to pyruvate, 2-ketobutyrate and oxaloacetate were utilized as amino group acceptors. We have sequenced the encoding gene (tpa). It encoded a 50-kDa peptide, which revealed 33% identity to diaminopelargonate aminotransferase from Bacillus subtilis.</dcterms:abstract>
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