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• W3049710153 endingPage "2455" @default.
• W3049710153 startingPage "2444" @default.
• W3049710153 abstract "Nonribosomal peptide synthesis is capable of utilizing a wide range of amino acid residues due to the selectivity of adenylation (A)-domains. Changing the selectivity of A-domains could lead to new bioactive nonribosomal peptides, although remodeling efforts of A-domains are often unsuccessful. Here, we explored and successfully reengineered the specificity of the module 3 A-domain from glycopeptide antibiotic biosynthesis to change the incorporation of 3,5-dihydroxyphenylglycine into 4-hydroxyphenylglycine. These engineered A-domains remain selective in a functioning peptide assembly line even under substrate competition conditions and indicate a possible application of these for the future redesign of GPA biosynthesis." @default.
• W3049710153 created "2020-08-21" @default.
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• W3049710153 date "2020-08-14" @default.
• W3049710153 modified "2023-09-25" @default.
• W3049710153 title "Redesign of Substrate Selection in Glycopeptide Antibiotic Biosynthesis Enables Effective Formation of Alternate Peptide Backbones" @default.
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• W3049710153 doi "https://doi.org/10.1021/acschembio.0c00435" @default.
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• W3049710153 hasPublicationYear "2020" @default.
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