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• W2095923527 startingPage "11951" @default.
• W2095923527 abstract "Nonribosomal peptides (NRPs) are produced by NRP synthetase (NRPS) enzymes that function as molecular assembly lines. The modular architecture of NRPSs suggests that a domain responsible for activating a building block could be replaced with a domain from a foreign NRPS to create a chimeric assembly line that produces a new variant of a natural NRP. However, such chimeric NRPS modules are often heavily impaired, impeding efforts to create novel NRP variants by swapping domains from different modules or organisms. Here we show that impaired chimeric NRPSs can be functionally restored by directed evolution. Using rounds of mutagenesis coupled with in vivo screens for NRP production, we rapidly isolated variants of two different chimeric NRPSs with approximately 10-fold improvements in enzyme activity and product yield, including one that produces new derivatives of the potent NRP/polyketide antibiotic andrimid. Because functional restoration in these examples required only modest library sizes (10(3) to 10(4) clones) and three or fewer rounds of screening, our approach may be widely applicable even for NRPSs from genetically challenging hosts." @default.
• W2095923527 created "2016-06-24" @default.
• W2095923527 creator A5030038763 @default.
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• W2095923527 creator A5050241478 @default.
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• W2095923527 date "2007-07-17" @default.
• W2095923527 modified "2023-10-17" @default.
• W2095923527 title "Directed evolution can rapidly improve the activity of chimeric assembly-line enzymes" @default.
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• W2095923527 doi "https://doi.org/10.1073/pnas.0705348104" @default.
• W2095923527 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1924594" @default.
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• W2095923527 hasPublicationYear "2007" @default.
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