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http://purl.uniprot.org/citations/24954722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24954722http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24954722http://www.w3.org/2000/01/rdf-schema#comment"The exploitation of catalytic promiscuity and the application of de novo design have recently opened the access to novel, non-natural enzymatic activities. Here we describe a structural bioinformatic method for predicting catalytic activities of enzymes based on three-dimensional constellations of functional groups in active sites ('catalophores'). As a proof-of-concept we identify two enzymes with predicted promiscuous ene-reductase activity (reduction of activated C-C double bonds) and compare them with known ene-reductases, that is, members of the Old Yellow Enzyme family. Despite completely different amino acid sequences, overall structures and protein folds, high-resolution crystal structures reveal equivalent binding modes of typical Old Yellow Enzyme substrates and ligands. Biochemical and biocatalytic data show that the two enzymes indeed possess ene-reductase activity and reveal an inverted stereopreference compared with Old Yellow Enzymes for some substrates. This method could thus be a tool for the identification of viable starting points for the development and engineering of novel biocatalysts."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.org/dc/terms/identifier"doi:10.1038/NCOMMS5150"xsd:string
http://purl.uniprot.org/citations/24954722http://purl.org/dc/terms/identifier"doi:10.1038/ncomms5150"xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Gruber K."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Gruber K."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Lyskowski A."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Lyskowski A."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Pavkov-Keller T."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Pavkov-Keller T."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Schwab H."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Schwab H."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Steiner K."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Steiner K."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Macheroux P."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Macheroux P."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Steinkellner G."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Steinkellner G."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Winkler C."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Winkler C."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Oberer M."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Oberer M."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Faber K."xsd:string
http://purl.uniprot.org/citations/24954722http://purl.uniprot.org/core/author"Faber K."xsd:string