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• W2065349718 abstract "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." @default.
• W2065349718 created "2016-06-24" @default.
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• W2065349718 date "2014-06-23" @default.
• W2065349718 modified "2023-10-14" @default.
• W2065349718 title "Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations" @default.
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• W2065349718 doi "https://doi.org/10.1038/ncomms5150" @default.
• W2065349718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4083419" @default.
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