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• W2800247165 abstract "Modular nonribosomal peptide synthetases (NRPSs) are large, multidomain engines of bioactive natural product biosynthesis that function as molecular “assembly lines” in which monomer units are selectively bound, modified, and linked in a specific order and number dictated by their mega-enzyme templates. Recently, a condensation domain in an NRPS was discovered to carry out the synthesis of an integrated β-lactam ring from a substrate seryl residue during antibiotic biosynthesis. We report here a series of experiments supporting a mechanism that involves C–N bond formation by stepwise elimination/addition reactions followed by canonical NRPS-catalyzed amide bond synthesis to achieve β-lactam formation. Partitioning of reactive intermediates formed during the multistep catalytic cycle provided insight into the ability of the NRPS to overcome the reversibility of corresponding reactions in solution and enforce directionality during synthesis." @default.
• W2800247165 created "2018-05-17" @default.
• W2800247165 creator A5001598260 @default.
• W2800247165 creator A5067252545 @default.
• W2800247165 date "2018-04-27" @default.
• W2800247165 modified "2023-09-23" @default.
• W2800247165 title "Mechanism of Integrated β-Lactam Formation by a Nonribosomal Peptide Synthetase during Antibiotic Synthesis" @default.
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• W2800247165 doi "https://doi.org/10.1021/acs.biochem.8b00411" @default.
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