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  • 1
    Online Resource
    Online Resource
    Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase
    Springer Science and Business Media LLC ; 2008
    In:  Archives of Microbiology Vol. 190, No. 2 ( 2008-8), p. 159-168
    Details
    In: Archives of Microbiology, Springer Science and Business Media LLC, Vol. 190, No. 2 ( 2008-8), p. 159-168
    Type of Medium: Online Resource
    ISSN: 0302-8933 , 1432-072X
    URL: Article
    DOI: 10.1007/s00203-008-0386-2
    RVK:
    WA 15000
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2008
    detail.hit.zdb_id: 1458451-7
    detail.hit.zdb_id: 477-7
    detail.hit.zdb_id: 124824-8
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  • 2
    Online Resource
    Online Resource
    Assimilation of sulfur from alkyl- and arylsulfonates by Clostridium spp.
    Springer Science and Business Media LLC ; 1997
    In:  Archives of Microbiology Vol. 167, No. 2-3 ( 1997-3-7), p. 177-181
    Details
    In: Archives of Microbiology, Springer Science and Business Media LLC, Vol. 167, No. 2-3 ( 1997-3-7), p. 177-181
    Type of Medium: Online Resource
    ISSN: 0302-8933 , 1432-072X
    URL: Article
    DOI: 10.1007/s002030050432
    RVK:
    WA 15000
    Language: Unknown
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1997
    detail.hit.zdb_id: 1458451-7
    detail.hit.zdb_id: 477-7
    detail.hit.zdb_id: 124824-8
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  • 3
    Online Resource
    Online Resource
    Ethanedisulfonate is degraded via sulfoacetaldehyde in Ralstonia sp. strain EDS1
    Springer Science and Business Media LLC ; 2001
    In:  Archives of Microbiology Vol. 176, No. 1-2 ( 2001-7-1), p. 89-95
    Details
    In: Archives of Microbiology, Springer Science and Business Media LLC, Vol. 176, No. 1-2 ( 2001-7-1), p. 89-95
    Type of Medium: Online Resource
    ISSN: 0302-8933 , 1432-072X
    URL: Article
    DOI: 10.1007/s002030100296
    RVK:
    WA 15000
    Language: Unknown
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2001
    detail.hit.zdb_id: 1458451-7
    detail.hit.zdb_id: 477-7
    detail.hit.zdb_id: 124824-8
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans
    Microbiology Society ; 2004
    In:  Microbiology Vol. 150, No. 4 ( 2004-04-01), p. 805-816
    Details
    In: Microbiology, Microbiology Society, Vol. 150, No. 4 ( 2004-04-01), p. 805-816
    Abstract: Growth of the α -proteobacterium Paracoccus denitrificans NKNIS with taurine or isethionate as sole source of carbon involves sulfoacetaldehyde acetyltransferase (Xsc), which is presumably encoded by an xsc gene in subgroup 3, none of whose gene products has been characterized. The genome of the α -proteobacterium Rhodobacter sphaeroides 2.4.1 was interpreted to contain a nine-gene cluster encoding the inducible dissimilation of taurine, and this deduced pathway included a regulator, a tripartite ATP-independent transporter, taurine dehydrogenase (TDH; presumably TauXY) as well as Xsc (subgroup 3), a hypothetical protein and phosphate acetyltransferase (Pta). A similar cluster was found in P. denitrificans NKNIS, in contrast to an analogous cluster encoding an ATP-binding cassette transporter in Paracoccus pantotrophus . Inducible TDH, Xsc and Pta were found in extracts of taurine-grown cells of strain NKNIS. TDH oxidized taurine to sulfoacetaldehyde and ammonium ion with cytochrome c as electron acceptor. Whereas Xsc and Pta were soluble enzymes, TDH was located in the particulate fraction, where inducible proteins with the expected masses of TauXY (14 and 50 kDa, respectively) were detected by SDS-PAGE. Xsc and Pta were separated by anion-exchange chromatography. Xsc was effectively pure; the molecular mass of the subunit (64 kDa) and the N-terminal amino acid sequence confirmed the identification of the xsc gene. Inducible isethionate dehydrogenase (IDH), Xsc and Pta were assayed in extracts of isethionate-grown cells of strain NKNIS. IDH was located in the particulate fraction, oxidized isethionate to sulfoacetaldehyde with cytochrome c as electron acceptor and correlated with the expression of a 62 kDa protein. Strain NKNIS excreted sulfite and sulfate during growth with a sulfonate and no sulfite dehydrogenase was detected. There is considerable biochemical, genetic and regulatory complexity in the degradation of these simple molecules.
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/mic.0.26795-0
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2004
    detail.hit.zdb_id: 2008736-6
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  • 5
    Online Resource
    Online Resource
    Molecular genetics and biochemistry of N-acetyltaurine degradation by Cupriavidus necator H16
    Microbiology Society ; 2011
    In:  Microbiology Vol. 157, No. 10 ( 2011-10-01), p. 2983-2991
    Details
    In: Microbiology, Microbiology Society, Vol. 157, No. 10 ( 2011-10-01), p. 2983-2991
    Abstract: Cupriavidus necator H16 (DSM 428), whose genome has been sequenced, was found to degrade N -acetyltaurine as a sole source of carbon and energy for growth. Utilization of the compound was quantitative. The degradative pathway involved an inducible N -acetyltaurine amidohydrolase (NaaS), which catalysed the cleavage of N -acetyltaurine to acetate and taurine. The degradation of the latter compound is via an inducible, degradative pathway that involves taurine dehydrogenase [EC 1.4.2.–], sulfoacetaldehyde acetyltransferase [EC 2.3.3.15] , phosphotransacetylase [EC 2.4.1.8] , a sulfite exporter [TC 9.A.29.2.1] and sulfite dehydrogenase [EC 1.8.2.1] . Induction of the expression of representative gene products, encoded by at least four gene clusters, was confirmed biochemically. The acetate released by NaaS was activated to acetyl-CoA by an inducible acetate–CoA ligase [EC 6.2.1.1]. NaaS was purified to homogeneity; it had a K m value of 9.4 mM for N -acetyltaurine, and it contained tightly bound Zn and Fe atoms. The denatured enzyme has a molecular mass of about 61 kDa (determined by SDS-PAGE) and the native enzyme was apparently monomeric. Peptide-mass fingerprinting identified the locus tag as H16_B0868 in a five-gene cluster, naaROPST (H16_B0865–H16_B0869). The cluster presumably encodes a LysR-type transcriptional regulator (NaaR), a membrane protein (NaaO), a solute : sodium symporter-family permease [TC 2.A.21] (NaaP), the metal-dependent amidohydrolase (NaaS) and a putative metallochaperone (COG0523) (NaaT). Reverse-transcription PCR indicated that naaOPST were inducibly transcribed.
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/mic.0.048462-0
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2011
    detail.hit.zdb_id: 2008736-6
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  • 6
    Online Resource
    Online Resource
    Bifurcated Degradative Pathway of 3-Sulfolactate in Roseovarius nubinhibens ISM via Sulfoacetaldehyde Acetyltransferase and ( S )-Cysteate Sulfolyase
    American Society for Microbiology ; 2009
    In:  Journal of Bacteriology Vol. 191, No. 18 ( 2009-09-15), p. 5648-5656
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 191, No. 18 ( 2009-09-15), p. 5648-5656
    Abstract: 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.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/JB.00569-09
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2009
    detail.hit.zdb_id: 1481988-0
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  • 7
    Online Resource
    Online Resource
    Sulfoquinovose is a select nutrient of prominent bacteria and a source of hydrogen sulfide in the human gut
    Springer Science and Business Media LLC ; 2021
    In:  The ISME Journal Vol. 15, No. 9 ( 2021-09), p. 2779-2791
    Details
    In: The ISME Journal, Springer Science and Business Media LLC, Vol. 15, No. 9 ( 2021-09), p. 2779-2791
    Abstract: Responses of the microbiota to diet are highly personalized but mechanistically not well understood because many metabolic capabilities and interactions of human gut microorganisms are unknown. Here we show that sulfoquinovose (SQ), a sulfonated monosaccharide omnipresent in green vegetables, is a selective yet relevant substrate for few but ubiquitous bacteria in the human gut. In human feces and in defined co-culture, Eubacterium rectale and Bilophila wadsworthia used recently identified pathways to cooperatively catabolize SQ with 2,3-dihydroxypropane-1-sulfonate as a transient intermediate to hydrogen sulfide (H 2 S), a key intestinal metabolite with disparate effects on host health. SQ-degradation capability is encoded in almost half of E. rectale genomes but otherwise sparsely distributed among microbial species in the human intestine. However, re-analysis of fecal metatranscriptome datasets of four human cohorts showed that SQ degradation (mostly from E. rectale and Faecalibacterium prausnitzii ) and H 2 S production (mostly from B. wadsworthia ) pathways were expressed abundantly across various health states, demonstrating that these microbial functions are core attributes of the human gut. The discovery of green-diet-derived SQ as an exclusive microbial nutrient and an additional source of H 2 S in the human gut highlights the role of individual dietary compounds and organosulfur metabolism on microbial activity and has implications for precision editing of the gut microbiota by dietary and prebiotic interventions.
    Type of Medium: Online Resource
    ISSN: 1751-7362 , 1751-7370
    URL: Article
    DOI: 10.1038/s41396-021-00968-0
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2021
    detail.hit.zdb_id: 2299378-2
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  • 8
    Online Resource
    Online Resource
    Sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12) from Desulfonispora thiosulfatigenes: purification, properties and primary sequence
    Portland Press Ltd. ; 2001
    In:  Biochemical Journal Vol. 357, No. 2 ( 2001-7-15), p. 581-
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 357, No. 2 ( 2001-7-15), p. 581-
    Type of Medium: Online Resource
    ISSN: 0264-6021
    URL: Article
    DOI: 10.1042/0264-6021:3570581
    RVK:
    WA 15000
    Language: Unknown
    Publisher: Portland Press Ltd.
    Publication Date: 2001
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12) from Desulfonispora thiosulfatigenes: purification, properties and primary sequence
    Portland Press Ltd. ; 2001
    In:  Biochemical Journal Vol. 357, No. 2 ( 2001-07-15), p. 581-586
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 357, No. 2 ( 2001-07-15), p. 581-586
    Abstract: The strictly anaerobic bacterium Desulfonispora thiosulfatigenes ferments taurine via sulphoacetaldehyde, which is hydrolysed to acetate and sulphite by sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12). The lyase was expressed at high levels and a two-step, 4.5-fold purification yielded an apparently homogeneous soluble protein, which was presumably a homodimer in its native form; the molecular mass of the subunit was about 61kDa (by SDS/PAGE). The mass was determined to be 63.8kDa by matrix-assisted laser-desorption ionization–time-of-flight (MALDI–TOF) MS. The purified enzyme converted 1mol of sulphoacetaldehyde to 1mol each of sulphite and acetate, but no requirement for thiamine pyrophosphate (TPP) was detected. The N-terminal and two internal amino acid sequences were determined, which allowed us to generate PCR primers. The gene was amplified and sequenced. The DNA sequence had no significant homologue in the databases searched, whereas the derived amino acid sequence indicated an oxo-acid lyase, revealed a TPP-binding site and gave a derived molecular mass of 63.8kDa.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj3570581
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2001
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Dissimilation of C3-sulfonates
    Springer Science and Business Media LLC ; 2006
    In:  Archives of Microbiology Vol. 185, No. 2 ( 2006-3), p. 83-90
    Details
    In: Archives of Microbiology, Springer Science and Business Media LLC, Vol. 185, No. 2 ( 2006-3), p. 83-90
    Type of Medium: Online Resource
    ISSN: 0302-8933 , 1432-072X
    URL: Article
    DOI: 10.1007/s00203-005-0069-1
    RVK:
    WA 15000
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2006
    detail.hit.zdb_id: 1458451-7
    detail.hit.zdb_id: 477-7
    detail.hit.zdb_id: 124824-8
    SSG: 12
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