Taurine-reduction Powers Rapid Growth of Bilophila wadsworthia: A Liquid Minimal-salts Medium for Clinical Research?

Laue, Heike; Schumacher, Ulrike; Cook, Alasdair M.

doi:10.1006/anae.1999.0210

Cited by 3 publications

(2 citation statements)

References 8 publications

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“…Desulfonation reactions in anaerobic bacteria have been discovered only recently (Seitz & Leadbetter, 1995 ;Cook, 1998), but it is already clear that the first recognized dissimilatory reaction, reduction of sulfonates in respirations, is widespread in sulfate-reducing bacteria (Lie et al, 1996(Lie et al, , 1998 and in Bilophila wadsworthia in the normal human gut flora (Laue et al, , 1999. Much less was known about the second recognized class of dissimilatory reactions in anaerobes, the oxidations, where only one organism has been examined in any detail, though others were detected .…”

Section: Discussionmentioning

confidence: 99%

Anaerobic oxidations of cysteate: degradation via L-cysteate: 2-oxoglutarate aminotransferase in Paracoccus pantotrophus

Mikosch¹,

Denger²,

Schäfer³

et al. 1999

Microbiology

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Anoxic, fresh-water enrichment cultures to oxidize different organosulfonates were set up with nitrate, ferric iron or sulfate as electron acceptors. Pure cultures were easily obtained with two naturally occurring sulfonates, cysteate (2-amino-3-sulfopropionate) and taurine (2-aminoethane~uIfonate)~ under nitrate-reducing conditions. These two sulfonates were also oxidized during reduction of iron(lll), though isolation of pure cultures was not successful. One nitrate-reducing cysteate-oxidizing bacterium, strain NKNCYSA, was studied in detail. It was identified as Paracoccus pantotrophus. Eighteen sulfonates were tested, and the organism degraded cysteate, taurine, isethionate (2-hydroxyethane~uIfonate)~ sulfoacetate or 3-aminopropanesulfonate with concomitant reduction of nitrate, presumably to molecular nitrogen. The carbon skeleton of these substrates was converted to cell material and, presumably, CO, . The amino group was released as ammonia and the sulfono moiety was recovered as sulfate. Cell-free extracts of P. pantotrophus NKNCYSA contained constitutive L-cysteate : 2-oxoglutarate aminotransferase (EC 2.6.1 .-) and glutamate dehydrogenase (EC 1.4.1.4). Taurine : pyruvate aminotransferase, in contrast, was inducible.

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Section: Discussionmentioning

confidence: 99%

Anaerobic oxidations of cysteate: degradation via L-cysteate: 2-oxoglutarate aminotransferase in Paracoccus pantotrophus

Mikosch¹,

Denger²,

Schäfer³

et al. 1999

Microbiology

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“…At least six enzymes are involved in the formation of the metabolic end products (ammonium, acetate and sulphide ions) during the degradation of taurine by B. wadsworthia (Laue et al, , 1999. Taurine-pyruvate aminotransferase (Tpa) [EC 2.6.1.77] catalyzes transamination of taurine to sulphoacetaldehyde and alanine (Laue & Cook, 2000b).…”

Section: Introductionmentioning

confidence: 99%

Identification ofBilophila wadsworthiaby specific PCR which targets the taurine:pyruvate aminotransferase gene

Laue

Smits

Schumacher

et al. 2006

FEMS Microbiology Letters

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The bile-resistant, strictly anaerobic bacterium Bilophila wadsworthia is found in human faecal flora, in human infections and in environmental samples. A specific PCR primer set for the gene encoding the first metabolic enzyme in the degradative pathway for taurine in B. wadsworthia, taurine:pyruvate aminotransferase (tpa), was developed and tested. In addition, enrichment cultures were started from faecal samples of primates and felines and shown to contain B. wadsworthia. These were subcultured on agar media and then identified by PCR fingerprinting. PCR for tpa was successful in all positive enrichment cultures and showed no amplification signal in a variety of other bacterial species. Therefore, this PCR method could be a promising tool for rapid detection of B. wadsworthia in biological samples.

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Microbial desulfonation

Cook¹,

Laue²,

Junker³

1998

FEMS Microbiol Rev

149

106

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Organosulfonates are widespread compounds, be they natural products of low or high molecular weight, or xenobiotics. Many commonly found compounds are subject to desulfonation, even if it is not certain whether all the corresponding enzymes are widely expressed in nature. Sulfonates require transport systems to cross the cell membrane, but few physiological data and no biochemical data on this topic are available, though the sequences of some of the appropriate genes are known. Desulfonative enzymes in aerobic bacteria are generally regulated by induction, if the sulfonate is serving as a carbon and energy source, or by a global network for sulfur scavenging (sulfate-starvation-induced (SSI) stimulon) if the sulfonate is serving as a source of sulfur. It is unclear whether an SSI regulation is found in anaerobes. The anaerobic bacteria examined can express the degradative enzymes constitutively, if the sulfonate is being utilized as a carbon source, but enzyme induction has also been observed. At least three general mechanisms of desulfonation are recognisable or postulated in the aerobic catabolism of sulfonates: (1) activate the carbon neighboring the C-SO3- bond and release of sulfite assisted by a thiamine pyrophosphate cofactor; (2) destabilize the C-SO3- bond by addition of an oxygen atom to the same carbon, usually directly by oxygenation, and loss of the good leaving group, sulfite; (3) an unidentified, formally reductive reaction. Under SSIS control, different variants of mechanism (2) can be seen. Catabolism of sulfonates by anaerobes was discovered recently, and the degradation of taurine involves mechanism (1). When anaerobes assimilate sulfonate sulfur, there is one common, unknown mechanism to desulfonate the inert aromatic compounds and another to desulfonate inert aliphatic compounds; taurine seems to be desulfonated by mechanism (1).

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Taurine-reduction Powers Rapid Growth of Bilophila wadsworthia: A Liquid Minimal-salts Medium for Clinical Research?

Cited by 3 publications

References 8 publications

Anaerobic oxidations of cysteate: degradation via L-cysteate: 2-oxoglutarate aminotransferase in Paracoccus pantotrophus

Anaerobic oxidations of cysteate: degradation via L-cysteate: 2-oxoglutarate aminotransferase in Paracoccus pantotrophus

Identification ofBilophila wadsworthiaby specific PCR which targets the taurine:pyruvate aminotransferase gene

Microbial desulfonation

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