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- W4289277735 endingPage "2053" @default.
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- W4289277735 abstract "Nonribosomal peptide synthetases (NRPSs) are a family of multidomain enzymes dedicated to the production of peptide natural products. Central to NRPS function are condensation (C) domains, which catalyze peptide bond formation and a number of specialized transformations including dehydroamino acid and β-lactam synthesis. Structures of C domains in catalytically informative states are limited due to a lack of clear strategies for stabilizing C domain interactions with their substrates and client domains. Inspired by a β-lactam forming C domain, we report herein the synthesis and application of 1, which forms irreversible cross-links with engineered thiol nucleophiles in a C domain active site. Deployment of 1 demonstrates the synthetic tractability of trapping late-stage nascent peptides in C domains and provides a readily adaptable tactic for stabilizing C domain interactions in multidomain NRPS fragments." @default.
- W4289277735 created "2022-08-01" @default.
- W4289277735 creator A5003830850 @default.
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- W4289277735 date "2022-08-01" @default.
- W4289277735 modified "2023-09-27" @default.
- W4289277735 title "Accurate Substrate-Like Probes for Trapping Late-Stage Intermediates in Nonribosomal Peptide Synthetase Condensation Domains" @default.
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- W4289277735 doi "https://doi.org/10.1021/acschembio.2c00474" @default.
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