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• W2788751465 abstract "An enoylreductase (ER) domain of a polyketide synthase module recruiting a methylmalonate extender unit sets the C2 methyl branch to either the S or R configuration during processing of a polyketide intermediate carried by an acyl carrier protein (ACP) domain. In the present study, pantetheine- and ACP-bound trans-2-methylcrotonyl substrate surrogates were used to scrutinize the stereospecificity of the ER domains. The pantetheine-bound thioester was reduced to mixtures of both 2R and 2S products, whereas the expected 2S epimer was almost exclusively generated when the cognate ACP-bound substrate surrogate was utilized. The analogous incubation of an ER with the substrate surrogate carried by a noncognate ACP significantly increased the generation of the unexpected 2R epimer, highlighting the dependence of stereospecificity on proper protein–protein interactions between ER and ACP domains. The ER mutant assays revealed the involvement of the conserved tyrosine and lysine in stereocontrol. Taken together, these results expand the current understanding of the ER stereochemistry and help in the engineering of modular PKSs." @default.
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• W2788751465 date "2018-02-13" @default.
• W2788751465 modified "2023-10-13" @default.
• W2788751465 title "Stereospecificity of Enoylreductase Domains from Modular Polyketide Synthases" @default.
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• W2788751465 doi "https://doi.org/10.1021/acschembio.7b00982" @default.
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