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Structure and mechanism of lanthipeptide biosynthetic enzymes.

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.

SUBMITTER: van der Donk WA

PROVIDER: S-EPMC4267917 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Structure and mechanism of lanthipeptide biosynthetic enzymes.

van der Donk Wilfred A WA Nair Satish K SK

Current opinion in structural biology 20141014

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 ...[more]

PMID: 25460269

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Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.

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Correction: Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.

Project description:[This corrects the article DOI: 10.1039/D0SC01651A.].

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