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- W2079251921 abstract "Modular natural products are biosynthesized by series of enzymes that activate, assemble, and process a nascent chain of building blocks. Adenylation domains are gatekeepers in nonribosomal peptide biosynthesis, providing the entry point for assembly of typical peptide-based natural products. We report the directed evolution of an adenylation domain based on a strategy of using a weak, promiscuous activity as a springboard for reprogramming the biosynthetic assembly line. Randomization of residues invoked in a specificity-conferring code and selection for a non-native substrate lead to mutant G2.1, favoring smaller amino acids with a specificity change of 10(5): a 170-fold improvement for L-alanine corresponds to a 10(3)-fold decrease for its original substrate (L-phenylalanine). These results establish directed evolution as a method to change gatekeeper domain specificity and suggest that adaptation of modules in combinatorial biosynthesis is achievable with few mutations during evolution." @default.
- W2079251921 created "2016-06-24" @default.
- W2079251921 creator A5046173039 @default.
- W2079251921 creator A5051612157 @default.
- W2079251921 date "2011-10-01" @default.
- W2079251921 modified "2023-10-18" @default.
- W2079251921 title "Directed Evolution of a Gatekeeper Domain in Nonribosomal Peptide Synthesis" @default.
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- W2079251921 doi "https://doi.org/10.1016/j.chembiol.2011.06.014" @default.
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