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http://purl.uniprot.org/citations/23090579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23090579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23090579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/23090579http://www.w3.org/2000/01/rdf-schema#comment"The prenyltransferase FtmPT1 from Aspergillus fumigatus is involved in the biosynthesis of fumitremorgin-type alkaloids and catalysed the regular C2-prenylation of brevianamide F (cyclo-L-Trp-L-Pro). It has been shown that FtmPT1 also accepted a number of other tryptophan-containing cyclic dipeptides and prenylated them, in the presence of dimethylallyl diphosphate, at C-2 of the indole nucleus. Detailed analysis of the incubation mixtures of FtmPT1 with these cyclic dipeptides revealed the presence of additional product peaks in the HPLC chromatograms. Seven regularly C3-prenylated hexahydropyrrolo[2,3-b]indoles were isolated and identified by HR-ESI-MS and NMR analyses including HMBC, HMQC and NOESY experiments. Further experiments proved that the C2- and C3-prenylated products are both independent enzyme products. To the best of our knowledge, this is the first report on the enzymatic formation of regularly C3-prenylated indolines. A reaction mechanism for both C2- and C3-prenylated derivatives was proposed."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.org/dc/terms/identifier"doi:10.1039/c2ob26149a"xsd:string
http://purl.uniprot.org/citations/23090579http://purl.org/dc/terms/identifier"doi:10.1039/c2ob26149a"xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Xie X."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Xie X."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Li S.M."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Li S.M."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Ludwig L."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Ludwig L."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Wollinsky B."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/author"Wollinsky B."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/name"Org. Biomol. Chem."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/name"Org. Biomol. Chem."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/pages"9262-9270"xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/pages"9262-9270"xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/title"Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/title"Breaking the regioselectivity of indole prenyltransferases: identification of regular C3-prenylated hexahydropyrrolo[2,3-b]indoles as side products of the regular C2-prenyltransferase FtmPT1."xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/23090579http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/23090579http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23090579