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- W4294958740 abstract "Abstract Acyl‐CoAs are key precursors of primary and secondary metabolism. Their efficient biosynthesis is often impeded by the limited substrate specificity and low in vivo activity of acyl‐CoA synthetases (ACSs) due to regulatory acylation of the catalytically important lysine residue in motif A10 (Lys‐A10). In this study, we identified an unusual ACS (UkaQ) from the UK‐2A biosynthetic pathway that naturally lacks the Lys‐A10 residue and exhibits extraordinarily broad substrate specificity. Protein engineering significantly improved its stability and catalytic activity, enabling it to synthesize a large variety of acyl‐CoAs with highly robust activity. By combining it with permissive carboxylases, we produced a large array of polyketide extender units and obtained six novel halobenzyl‐containing antimycin analogues through an engineered biosynthetic pathway. This study significantly expands the catalytic mode of ACSs and provides a potent tool for the biosynthesis of acyl‐CoA‐derived natural products." @default.
- W4294958740 created "2022-09-08" @default.
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- W4294958740 date "2022-09-29" @default.
- W4294958740 modified "2023-09-26" @default.
- W4294958740 title "An Atypical Acyl‐CoA Synthetase Enables Efficient Biosynthesis of Extender Units for Engineering a Polyketide Carbon Scaffold" @default.
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- W4294958740 doi "https://doi.org/10.1002/anie.202208734" @default.
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