期刊
ACS CHEMICAL BIOLOGY
卷 8, 期 3, 页码 473-487出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb3005325
关键词
-
资金
- National Institutes of Health [1R01 GM097142]
- University of Illinois Department of Chemistry Harold R. Snyder Fellowship
Ribosomally synthesized posttranslationally modified peptides (RiPPs) are a rapidly growing class of natural products with diverse structures and activities. In recent years, a great deal of progress has been made in elucidating the biosynthesis of various RiPP family members. As with the study of nonribosomal peptide and polyketide biosynthetic enzymes, these investigations have led to the discovery of entirely new biological chemistry. With each unique enzyme investigated, a more complex picture of Nature's synthetic potential is revealed. This Review focuses on recent reports (since 2008) that have changed the way that we think about ribosomal natural product biosynthesis and the enzymology of complex bond-forming reactions.
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