| http://purl.uniprot.org/citations/20047909 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20047909 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20047909 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/20047909 | http://www.w3.org/2000/01/rdf-schema#comment | "Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the condensation of acetyl-CoA with glyoxylate. In the glyoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway the reaction is separated into two proteins: malyl-CoA lyase, a well-known enzyme catalyzing the Claisen condensation of acetyl-CoA with glyoxylate and yielding malyl-CoA, and an unidentified malyl-CoA thioesterase that hydrolyzes malyl-CoA into malate and CoA. In this study the roles of Mcl1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inactivation and biochemical studies. Mcl1 is a true (3S)-malyl-CoA lyase operating in the ethylmalonyl-CoA pathway. Notably, Mcl1 is a promiscuous enzyme and catalyzes not only the condensation of acetyl-CoA and glyoxylate but also the cleavage of beta-methylmalyl-CoA into glyoxylate and propionyl-CoA during acetyl-CoA assimilation. In contrast, Mcl2 was shown to be the sought (3S)-malyl-CoA thioesterase in the ethylmalonyl-CoA pathway, which specifically hydrolyzes (3S)-malyl-CoA but does not use beta-methylmalyl-CoA or catalyze a lyase or condensation reaction. The identification of Mcl2 as thioesterase extends the enzyme functions of malyl-CoA lyase homologs that have been known only as "Claisen condensation" enzymes so far. Mcl1 and Mcl2 are both related to malate synthase, an enzyme which catalyzes both a Claisen condensation and thioester hydrolysis reaction."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.01267-09"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.01267-09"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Alber B.E."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Alber B.E."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Fuchs G."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Fuchs G."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Erb T.J."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Erb T.J."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Frerichs-Revermann L."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/author | "Frerichs-Revermann L."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/pages | "1249-1258"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/pages | "1249-1258"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/title | "The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/title | "The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase."xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/volume | "192"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://purl.uniprot.org/core/volume | "192"xsd:string |
| http://purl.uniprot.org/citations/20047909 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20047909 |