Abstract
Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes.
Copyright © 2014 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Anti-Bacterial Agents / biosynthesis
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Anti-Bacterial Agents / chemistry
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Bacteria / metabolism
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Bacteriocins / biosynthesis*
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Bacteriocins / chemistry*
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Hydro-Lyases / chemistry
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Oxidoreductases / chemistry
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Peptide Hydrolases / chemistry*
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Peptides / chemistry*
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Protein Conformation
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Protein Processing, Post-Translational*
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Ribosomes / metabolism
Substances
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Anti-Bacterial Agents
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Bacteriocins
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Peptides
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epilancin 15X
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Oxidoreductases
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Peptide Hydrolases
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Hydro-Lyases