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• W3025378082 abstract "A structural model of the enoyl reductase (ER) catalytic domain of the fungal highly-reducing polyketide synthase squalestatin tetraketide synthase (SQTKS) was developed. Simulated docking of substrates and inhibitors allowed the definition of active site residues involved in catalysis and substrate selectivity. These were investigated in silico with the aim of extending the substrate scope. Residues were identified which limit the substrate selectivity of the SQTKS ER, and these were mutated and the engineered ER domain assayed in vitro. Significant changes to the programming of the mutant SQTKS ER domains were observed allowing the processing of longer and more methylated substrates." @default.
• W3025378082 created "2020-05-21" @default.
• W3025378082 creator A5034746401 @default.
• W3025378082 creator A5064022391 @default.
• W3025378082 date "2020-01-01" @default.
• W3025378082 modified "2023-10-03" @default.
• W3025378082 title "Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase" @default.
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• W3025378082 doi "https://doi.org/10.1039/d0ra04026f" @default.
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