Sulfoacetate generated by Rhodopseudomonas palustris from taurine

Denger, Karin; Weinitschke, Sonja; Hollemeyer, Klaus; Cook, Alasdair M.

doi:10.1007/s00203-004-0678-0

Cited by 35 publications

(50 citation statements)

References 28 publications

(39 reference statements)

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“…However, S. Weinitschke (unpublished data) has now observed that the addition of separated cytochrome c (from extracts of taurine-grown R. palustris) to the apparently inactive crude extract from R. palustris allows oxidation of taurine to sulfoacetaldehyde. This tends to confirm the hypothesis of Denger et al (2004b) that a native cytochrome c is sometimes essential for activity of taurine dehydrogenase. Correspondingly, characterization of taurine dehydrogenase will require not only pure protein (not attained elsewhere; Brüggemann et al, 2004) but also its native cytochrome c.…”

Section: Discussionsupporting

confidence: 82%

“…The (N-methyl)taurine dehydrogenase from A. faecalis MT1 showed a much higher activity with the artificial electron acceptor, DCPIP, than with equine cytochrome c, as observed with some other taurine dehydrogenases (Brüggemann et al, 2004). One taurine dehydrogenase, postulated from the presence of the tauXY genes in Rhodopseudomonas palustris CGA009, is inactive with both DCPIP and equine cytochrome c (Denger et al, 2004b), which is itself an artificial substrate in bacterial extracts. However, S. Weinitschke (unpublished data) has now observed that the addition of separated cytochrome c (from extracts of taurine-grown R. palustris) to the apparently inactive crude extract from R. palustris allows oxidation of taurine to sulfoacetaldehyde.…”

Section: Discussionmentioning

confidence: 99%

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The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

et al. 2006

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Selective enrichments yielded bacterial cultures able to utilize the osmolyte N-methyltaurine as sole source of carbon and energy or as sole source of fixed nitrogen for aerobic growth. Strain MT1, which degraded N-methyltaurine as a sole source of carbon concomitantly with growth, was identified as a strain of Alcaligenes faecalis. Stoichiometric amounts of methylamine, whose identity was confirmed by matrix-assisted, laser-desorption ionization time-of-flight mass spectrometry, and of sulfate were released during growth. Inducible N-methyltaurine dehydrogenase, sulfoacetaldehyde acetyltransferase (Xsc) and a sulfite dehydrogenase could be detected. Taurine dehydrogenase was also present and it was hypothesized that taurine dehydrogenase has a substrate range that includes N-methyltaurine. Partial sequences of a tauY-like gene (encoding the putative large component of taurine dehydrogenase) and an xsc gene were obtained by PCR with degenerate primers. Strain N-MT utilized N-methyltaurine as a sole source of fixed nitrogen for growth and could also utilize the compound as sole source of carbon. This bacterium was identified as a strain of Paracoccus versutus. This organism also expressed inducible (N-methyl)taurine dehydrogenase, Xsc and a sulfite dehydrogenase. The presence of a gene cluster with high identity to a larger cluster from Paracoccus pantotrophus NKNCYSA, which is now known to dissimilate N-methyltaurine via Xsc, allowed most of the overall pathway, including transport and excretion, to be defined. N-Methyltaurine is thus another compound whose catabolism is channelled directly through sulfoacetaldehyde. INTRODUCTIONTaurine (2-aminoethanesulfonate) is widespread in the biosphere, whether as the free ampholyte or in derivatized form. Mammals usually contain about 8 mM taurine, which they cannot desulfonate (Huxtable, 1992), and which they excrete largely in urine (e.g. Stipanuk, 2004). We presume that this steady supply of taurine to the environment explains the considerable diversity of microbial taurine metabolism, which includes utilizing the compound as a sole source of carbon, nitrogen or sulfur for aerobic growth, as a source of, or as a sink for, electrons for anaerobes, or as a fermentative substrate .One of the few undisputed functions of free taurine in many animals is its role as an osmolyte (Huxtable, 1992;Yancey et al., 2002). One widespread derivative of taurine, Nmethyltaurine (Allen & Garrett, 1971), has now been recognized as an osmolyte in some deep-sea worms, where it can be present at concentrations in excess of 250 mM (Yin et al., 2000). The fate of this compound was unknown until now.The bacterial catabolism of taurine and of the structurally related compounds isethionate (2-hydroxyethanesulfonate), sulfoacetate and ethane-1,2-disulfonate converges at sulfoacetaldehyde (Cook & Denger, 2002). We were interested to see whether N-methyltaurine would be degradable, and if so, whether sulfoacetaldehyde acetyltransferase (Xsc) (EC 2.3.3.15) was involved as well (Fig. 1). Xsc catalyses...

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

et al. 2006

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“…The sulfur content of leaves is comprised mainly of sulfolipid and proteins; senescence of deciduous plants thus introduces significant amounts of sulfoquinovose into the soil (8). Sulfoacetate can also be the product of the bacterial assimilation of nitrogen from taurine (9,10). The latter precursor of sulfoacetate is a major organic solute in marine creatures (11,12) and in mammals (13), which excrete it in urine (14).…”

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confidence: 99%

Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16

Weinitschke

Hollemeyer

Kusian

et al. 2010

Journal of Biological Chemistry

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Bacterial degradation of sulfoacetate, a widespread natural product, proceeds via sulfoacetaldehyde and requires a considerable initial energy input. Whereas the fate of sulfoacetaldehyde in Cupriavidus necator (Ralstonia eutropha) H16 is known, the pathway from sulfoacetate to sulfoacetaldehyde is not. The genome sequence of the organism enabled us to hypothesize that the inducible pathway, which initiates sau (sulfoacetate utilization), involved a four-gene cluster (sauRSTU; H16_A2746 to H16_A2749). The sauR gene, divergently orientated to the other three genes, probably encodes the transcriptional regulator of the presumed sauSTU operon, which is subject to inducible transcription. SauU was tentatively identified as a transporter of the major facilitator superfamily, and SauT was deduced to be a sulfoacetate-CoA ligase. SauT was a labile protein, but it could be separated and shown to generate AMP and an unknown, labile CoA-derivative from sulfoacetate, CoA, and ATP. This unknown compound, analyzed by MALDI-TOF-MS, had a relative molecular mass of 889.7, which identified it as protonated sulfoacetyl-CoA (calculated 889.6). SauS was deduced to be sulfoacetaldehyde dehydrogenase (acylating). The enzyme was purified 175-fold to homogeneity and characterized. Peptide mass fingerprinting confirmed the sauS locus (H16_A2747). SauS converted sulfoacetyl-CoA and NADPH to sulfoacetaldehyde, CoA, and NADP ؉ , thus confirming the hypothesis.

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“…3a, b). The assimilation of taurine-nitrogen sometimes involves utilization of the compound concomitant with growth, as found in Acinetobacter calcoaceticus SW1, Alcaligenes faecalis MT1 and Rhodococcus opacus ISO-5 (Denger et al, 2004a;Weinitschke et al, 2005Weinitschke et al, , 2006, and sometimes with excretion and subsequent utilization of the ammonium ion as in Rhodopseudomonas palustris CGA009 (Denger et al, 2004b), as shown in Fig. 3(b).…”

Section: Discussionmentioning

confidence: 93%

“…The compound can also serve as a sole source of sulfur for growth (e.g. Kertesz, 2000), and a range of phenomena can be involved when organisms utilize the compound as a sole source of nitrogen; these include deamination without desulfonation, not always concomitant with substrate utilization (Denger et al, 2004b;Styp von Rekowski et al, 2005;Weinitschke et al, 2005), and utilization concomitant with taurine carbon (Denger et al, 2004a). Two general pathways for the dissimilation of taurine have been hypothesized , one of which has received significant experimental support in Silicibacter pomeroyi DSS-3, especially for the genes encoding an ATP-binding cassette transporter (TauABC), taurine : pyruvate aminotransferase (Tpa) and alanine dehydrogenase (Ald) (analogous to Fig.…”

Section: Introductionmentioning

confidence: 99%

Genome-enabled analysis of the utilization of taurine as sole source of carbon or of nitrogen by Rhodobacter sphaeroides 2.4.1

2006

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In the present study, R. sphaeroides 2.4.1 was found to grow exponentially with taurine as the sole source of carbon and energy for growth. When taurine was the sole source of nitrogen in succinate-salts medium, the taurine was rapidly degraded, and most of the organic nitrogen was excreted as the ammonium ion, which was then utilized for growth. Most of the enzymes involved in dissimilation, taurine dehydrogenase (TDH), sulfoacetaldehyde acetyltransferase (Xsc) and phosphate acetyltransferase (Pta), were found to be inducible, and evidence for transcription of the corresponding genes (tauXY, xsc and pta), as well as of tauKLM, encoding the postulated TRAP transporter for taurine, and of tauZ, encoding the sulfate exporter, was obtained by reverse-transcription PCR. An additional branch of the pathway, observed by Novak et al. (2004) (Microbiology 150, 1881-1891) in R. sphaeroides TAU3, involves taurine : pyruvate aminotransferase (Tpa) and a presumptive ABC transporter (NsbABC). No evidence for a significant role of this pathway, or of the corresponding alanine dehydrogenase (Ald), was obtained for R. sphaeroides 2.4.1. The anaplerotic pathway needed under these conditions in R. sphaeroides 2.4.1 seems to involve malyl-CoA lyase, which was synthesized inducibly, and not malate synthase (GlcB), whose presumed gene was not transcribed under these conditions.

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Sulfoacetate generated by Rhodopseudomonas palustris from taurine

Cited by 35 publications

References 28 publications

The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16

Genome-enabled analysis of the utilization of taurine as sole source of carbon or of nitrogen by Rhodobacter sphaeroides 2.4.1

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