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http://purl.uniprot.org/citations/17113998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17113998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17113998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/17113998http://www.w3.org/2000/01/rdf-schema#comment"The natural product lovastatin and its semisynthetic, more effective derivative, simvastatin, are important drugs for the treatment of hypercholesterolemia. Here, we report the biochemical characterization of a dedicated acyltransferase, LovD, encoded in the lovastatin biosynthetic pathway. We demonstrate that LovD has broad substrate specificity towards the acyl carrier, the acyl substrate, and the decalin acyl acceptor. LovD can efficiently catalyze the acyl transfer from coenzyme A thioesters or N-acetylcysteamine (SNAC) thioesters to monacolin J. When alpha-dimethylbutyryl-SNAC was used as the acyl donor, LovD was able to convert monacolin J and 6-hydroxyl-6-desmethylmonacolin J into simvastatin and huvastatin, respectively. Using the Escherichia coli LovD overexpression strain as a whole-cell biocatalyst, preparative amounts of simvastatin were synthesized in a single fermentation step. Our results demonstrate LovD is an attractive enzyme for engineered biosynthesis of pharmaceutically important cholesterol-lowering drugs."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2006.09.008"xsd:string
http://purl.uniprot.org/citations/17113998http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2006.09.008"xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Tang Y."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Tang Y."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Xie X."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Xie X."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Watanabe K."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Watanabe K."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Wang C.C."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Wang C.C."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Wojcicki W.A."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/author"Wojcicki W.A."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/pages"1161-1169"xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/pages"1161-1169"xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/title"Biosynthesis of lovastatin analogs with a broadly specific acyltransferase."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/title"Biosynthesis of lovastatin analogs with a broadly specific acyltransferase."xsd:string
http://purl.uniprot.org/citations/17113998http://purl.uniprot.org/core/volume"13"xsd:string