| http://purl.uniprot.org/citations/21069965 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21069965 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21069965 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/21069965 | http://www.w3.org/2000/01/rdf-schema#comment | "There are very few fungal polyketide synthases that have been characterized by mass spectrometry. In this paper we describe the in vitro reconstitution and FT-ICR-MS verification of the full activity of an intact 277 kDa fungal polyketide synthase LovF of the lovastatin biosynthetic pathway. We report here both the verification of the reconstitution of fully functional holo-LovF by using (13)C-labeled malonyl-CoA to form α-methylbutyrate functionality and also detection of five predicted intermediates covalently bound to the 4'-phosphopantetheine at the acyl carrier protein (ACP) active site utilizing the phosphopantetheine ejection assay and high-resolution mass spectrometry. Under in vitro conditions, the diketide acetoacetyl intermediate did not accumulate on the ACP active site of holo-LovF following incubation with malonyl-CoA substrate. We found that incubation of holo-LovF with acetoacetyl-CoA served as an effective means of loading the diketide intermediate onto the ACP active site of LovF. Our results demonstrate that subsequent α-methylation of the acetoacetyl intermediate stabilizes the intermediate onto the ACP active site and facilitates the formation and mass spectrometric detection of additional intermediates en route to the formation of α-methylbutyrate."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi1014776"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi1014776"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Dorrestein P.C."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Dorrestein P.C."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Tang Y."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Tang Y."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Xie X."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Xie X."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Zhao X."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Zhao X."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Meehan M.J."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/author | "Meehan M.J."xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/pages | "287-299"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/pages | "287-299"xsd:string |
| http://purl.uniprot.org/citations/21069965 | http://purl.uniprot.org/core/title | "FT-ICR-MS characterization of intermediates in the biosynthesis of the alpha-methylbutyrate side chain of lovastatin by the 277 kDa polyketide synthase LovF."xsd:string |