http://purl.uniprot.org/citations/11830598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11830598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11830598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/11830598 | http://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/11830598 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m201011200"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m201011200"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "Graham D.E."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "Graham D.E."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "White R.H."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "White R.H."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/pages | "13421-13429"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/pages | "13421-13429"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://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/11830598 | http://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/11830598 | http://purl.uniprot.org/core/volume | "277"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://purl.uniprot.org/core/volume | "277"xsd:string |
http://purl.uniprot.org/citations/11830598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11830598 |
http://purl.uniprot.org/citations/11830598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11830598 |
http://purl.uniprot.org/citations/11830598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11830598 |