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American Chemical Society, ACS Chemical Biology, 3(8), p. 473-487, 2013

DOI: 10.1021/cb3005325

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Revealing Nature’s Synthetic Potential Through the Study of Ribosomal Natural Product Biosynthesis

Journal article published in 2013 by Kyle L. Dunbar ORCID, Douglas A. Mitchell ORCID
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.