Publications

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

  Laue H., Cook A.M.

  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 sulfoacetaldehy ... >> More

  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. << Less

  Eur. J. Biochem. 267:6841-6848(2000) [PubMed] [EuropePMC]

• Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source.

  Masepohl B., Fuhrer F., Klipp W.

  Rhodobacter capsulatus was shown to grow efficiently with taurine as sole source of sulfur. We identified a gene region exhibiting similarity to the Escherichia coli tauABC genes coding for a taurine-specific ABC transporter. The R. capsulatus tauABC genes were flanked by two putative operons (orf ... >> More

  Rhodobacter capsulatus was shown to grow efficiently with taurine as sole source of sulfur. We identified a gene region exhibiting similarity to the Escherichia coli tauABC genes coding for a taurine-specific ABC transporter. The R. capsulatus tauABC genes were flanked by two putative operons (orf459-484-590 and cysE-srpI-nifS2) both reading in opposite direction relative to tauABC. Orf459 shows strong similarity to taurine:pyruvate aminotransferase (Tpa) from Bilophila wadsworthia catalyzing the initial transamination during anaerobic taurine degradation, and Orf590 exhibits clear similarity to sulfoacetaldehyde sulfo-lyase from Desulfonispora thiosulfatigenes probably catalyzing the step following the taurine:pyruvate aminotransferase (Tpa) reaction, whereas nifS2 might code for a putative cysteine desulfurase. Expression of R. capsulatus tauABC and nifS2 was inhibited by sulfate, suggesting that tauABC and nifS2 might belong to the same regulon. In contrast, transcription of orf459 was not inhibited by sulfate but was induced by taurine. A tauAB deletion mutant showed significantly reduced growth compared to the wild-type with taurine as sole sulfur source in the presence of serine as a nitrogen source, whereas normal growth was observed in the presence of taurine and ammonium. Deletion of orf459-484-590 completely abolished growth with taurine/serine. Single mutations in any of the three genes resulted in the same phenotype, indicating that all three genes of this putative operon are essential for taurine sulfur utilization in the presence of serine. A model for anaerobic taurine sulfur assimilation in R. capsulatus is discussed. << Less

  FEMS Microbiol Lett 205:105-111(2001) [PubMed] [EuropePMC]

• Dissimilation of the C2 sulfonates.

  Cook A.M., Denger K.

  Organosulfonates are widespread in the environment, both as natural products and as xenobiotics; and they generally share the property of chemical stability. A wide range of phenomena has evolved in microorganisms able to utilize the sulfur or the carbon moiety of these compounds; and recent work ... >> More

  Organosulfonates are widespread in the environment, both as natural products and as xenobiotics; and they generally share the property of chemical stability. A wide range of phenomena has evolved in microorganisms able to utilize the sulfur or the carbon moiety of these compounds; and recent work has centered on bacteria. This Mini-Review centers on bacterial catabolism of the carbon moiety in the C2-sulfonates and the fate of the sulfonate group. Five of the six compounds examined are subject to catabolism, but information on the molecular nature of transport and regulation is based solely on sequencing data. Two mechanisms of desulfonation have been established. First, there is the specific monooxygenation of ethanesulfonate or ethane-1,2-disulfonate. Second, the oxidative, reductive and fermentative modes of catabolism tend to yield the intermediate sulfoacetaldehyde, which is now known to be desulfonated to acetyl phosphate by a thiamin-diphosphate-dependent acetyltransferase. This enzyme is widespread and at least three subgroups can be recognized, some of them in genomic sequencing projects. These data emphasize the importance of acetyl phosphate in bacterial metabolism. A third mechanism of desulfonation is suggested: the hydrolysis of sulfoacetate. << Less

  Arch Microbiol 179:1-6(2002) [PubMed] [EuropePMC]

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