No abstract

Genes thought to encode (a) the regulator of taurine catabolism under carbon-limiting or nitrogen-limiting conditions and (b) taurine dehydrogenase were found in the genome of Rhodopseudomonas palustris. The organism utilized taurine quantitatively as a sole source of nitrogen (but not of carbon) for aerobic and photoheterotrophic growth. No sulfate was released, and the C-sulfonate bond was recovered stoichiometrically as sulfoacetate, which was identified by mass spectrometry. An inducible sulfoacetaldehyde dehydrogenase was detected. R. palustris thus contains a pathway to generate a natural product that was previously believed to be formed solely from sulfoquinovose.

Data from the genome sequence of the aerobic, marine bacterium Roseovarius nubinhibens ISM were interpreted such that 3-sulfolactate would be degraded as a sole source of carbon and energy for growth via a novel bifurcated pathway including two known desulfonative enzymes, sulfoacetaldehyde acetyltransferase (EC 2.3.3.15) (Xsc) and cysteate sulfo-lyase (EC 4.4.1.25) (CuyA). Strain ISM utilized sulfolactate quantitatively with stoichiometric excretion of the sulfonate sulfur as sulfate. A combination of enzyme assays, analytical chemistry, enzyme purification, peptide mass fingerprinting, and reverse transcription-PCR data supported the presence of an inducible, tripartite sulfolactate uptake system (SlcHFG), and a membrane-bound sulfolactate dehydrogenase (SlcD) which generated 3-sulfopyruvate, the point of bifurcation. 3-Sulfopyruvate was in part decarboxylated by 3-sulfopyruvate decarboxylase (EC 4.1.1.79) (ComDE), which was purified. The sulfoacetaldehyde that was formed was desulfonated by Xsc, which was identified, and the acetyl phosphate was converted to acetyl-coenzyme A by phosphate acetyltransferase (Pta). The other portion of the 3-sulfopyruvate was transaminated to (S)-cysteate, which was desulfonated by CuyA, which was identified. The sulfite that was formed was presumably exported by CuyZ (TC 9.B.7.1.1 in the transport classification system), and a periplasmic sulfite dehydrogenase is presumed. Bioinformatic analyses indicated that transporter SlcHFG is rare but that SlcD is involved in three different combinations of pathways, the bifurcated pathway shown here, via CuyA alone, and via Xsc alone. This novel pathway involves ComDE in biodegradation, whereas it was discovered in the biosynthesis of coenzyme M. The different pathways of desulfonation of sulfolactate presumably represent final steps in the biodegradation of sulfoquinovose (and exudates derived from it) in marine and aquatic environments.Sulfolactate (Fig. 1A) is a widespread natural product, which contains the stable C-SO 3 Ϫ bond. The compound is known to be (i) a component (5% of dry weight) of bacterial endospores (5), (ii) an intermediate in the biosynthesis of coenzyme M in archaea (55), (iii) in equilibrium with (S)-cysteate in mammals (54), (iv) involved in the metabolism of sulfoquinovose (6-deoxy-6-sulfo-D-glucopyranose, the polar moiety of the plant sulfolipid) in plants and algae (e.g., see reference 48), and (v) an intermediate in the bacterial degradation of sulfoquinovose (44).Research on the biodegradation of organosulfonates has concentrated on compounds containing one to four carbon atoms (C 1 , C 2 , C 3 , or C 4 sulfonates), because where appropriate, larger molecules all seemed to be processed via one of the five desulfonative reactions that have been elucidated. Pathways from (i) sulfoquinovose yield, e.g., sulfoacetate or sulfolactate and 2,3-dihydroxy-1-sulfopropane (36, 44), (ii) taurocholate and N-acetyltaurine yield taurine (37, 43), and (iii) N-methyltaurine yield sulfoacetaldehyde (52). The five desulfonatio...

Eighteen enrichment cultures with taurine (2-aminoethanesulfonate) as the sole source of combined nitrogen under aerobic conditions were all successful, and 24 pure cultures were obtained. Only three of the cultures yielded an inorganic product, sulfate, from the sulfonate moiety of taurine, and the others were presumed to yield organosulfonates. Sulfoacetate, known from Rhodopseudomonas palustris CGA009 under these conditions, was not detected in any culture, but sulfoacetaldehyde (as a hydrazone derivative) was tentatively detected in the outgrown medium of nine isolates. The compound was stable under these conditions and the identification was confirmed by MALDI-TOF-MS. Most sulfoacetaldehyde-releasing isolates were determined to be strains of Acinetobacter calcoaceticus, and a representative organism, strain SW1, was chosen for further work. A quantitative enzymic determination of sulfoacetaldehyde and its bisulfite addition complex was developed: it involved the NAD-coupled sulfoacetaldehyde dehydrogenase from R. palustris. A. calcoaceticus SW1 utilized taurine quantitatively and concomitantly with growth in, for example, an adipate-salts medium, and the release of sulfoacetaldehyde was stoichiometric. The deamination reaction involved a taurine dehydrogenase. Enrichment cultures to explore the possible release of organophosphonates from the analogous substrate, 2-aminoethanephosphonate, led to 33 isolates, all of which released inorganic phosphate quantitatively.

Taurine (2-aminoethanesulfonate) is a widespread natural product whose nitrogen moiety was recently shown to be assimilated by bacteria, usually with excretion of an organosulfonate via undefined novel pathways; other data involve transcriptional regulator TauR in taurine metabolism. A screen of genome sequences for TauR with the BLAST algorithm allowed the hypothesis that the marine gammaproteobacterium Neptuniibacter caesariensis MED92 would inducibly assimilate taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter (TauABC), taurine:pyruvate aminotransferase (Tpa), a novel sulfoacetaldehyde dehydrogenase (SafD) and exporter(s) of sulfoacetate (SafE) (DUF81). Ten candidate genes in two clusters involved three sets of paralogues (for TauR, Tpa and SafE). Inducible Tpa and SafD were detected in cell extracts. SafD was purified 600-fold to homogeneity in two steps. The monomer had a molecular mass of 50 kDa (SDS-PAGE); data from gel filtration chromatography indicated a tetrameric native protein. SafD was specific for sulfoacetaldehyde with a K m -value of 0.12 mM. The N-terminal amino acid sequence of SafD confirmed the identity of the safD gene. The eight pathway genes were transcribed inducibly, which indicated expression of the whole hypothetical pathway. We presume that this pathway is one source of sulfoacetate in nature, where this compound is dissimilated by many bacteria.