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http://purl.uniprot.org/citations/11830598http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11830598http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11830598http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11830598http://www.w3.org/2000/01/rdf-schema#comment"The hyperthermophilic euryarchaeon Methanococcus jannaschii uses coenzyme M (2-mercaptoethanesulfonic acid) as the terminal methyl carrier in methanogenesis. We describe an enzyme from that organism, (2R)-phospho-3-sulfolactate synthase (ComA), that catalyzes the first step in coenzyme M biosynthesis. ComA catalyzed the stereospecific Michael addition of sulfite to phosphoenolpyruvate over a broad range of temperature and pH conditions. Substrate and product analogs moderately inhibited activity. This enzyme has no significant sequence similarity to previously characterized enzymes; however, its Mg(2+)-dependent enzyme reaction mechanism may be analogous to one proposed for enolase. A diverse group of microbes and plants have homologs of ComA that could have been recruited for sulfolactate or sulfolipid biosyntheses."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201011200"xsd:string
http://purl.uniprot.org/citations/11830598http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201011200"xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"Graham D.E."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"Graham D.E."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/pages"13421-13429"xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/pages"13421-13429"xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/title"Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/title"Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes."xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11830598http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11830598http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11830598
http://purl.uniprot.org/citations/11830598http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11830598
http://purl.uniprot.org/citations/11830598http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11830598