Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 23, Issue 4, Pages 603-612Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2013.06.012
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Funding
- National Science Foundation [CHE-1151299]
- NIH [1R01GM104258-01]
- NC State University Faculty Research and Development Awards
- NC State University
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM104258] Funding Source: NIH RePORTER
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Naturally occurring polyketides and nonribosomal peptides with broad and potent biological activities continue to inspire the discovery of new and improved analogs. The biosynthetic apparatus responsible for the construction of these natural products has been the target of intensive protein engineering efforts. Traditionally, engineering has focused on substituting individual enzymatic domains or entire modules with those of different building block specificity, or by deleting various enzymatic functions, in an attempt to generate analogs. This review highlights strategies based on site-directed mutagenesis of substrate binding pockets, semi-rational mutagenesis, and whole-gene random mutagenesis to engineer the substrate specificity, activity, and protein interactions of polyketide and nonribosomal peptide biosynthetic machinery.
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