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Curr Opin Struct Biol. 2010 Apr;20(2):234-40. doi: 10.1016/j.sbi.2010.01.009. Epub 2010 Feb 10.

Nonribosomal peptide synthetases: structures and dynamics.

Author information

1
Philipps-University Marburg, Department of Chemistry/Biochemistry, Hans-Meerwein-Strasse, Marburg, Germany.

Abstract

Nonribosomal peptide synthetases (NRPSs) are large multimodular biocatalysts that utilize complex regiospecific and stereospecific reactions to assemble structurally and functionally diverse peptides that have important medicinal applications. During this ribosome-independent peptide synthesis, catalytic domains of NRPS select, activate or modify the covalently tethered reaction intermediates to control the iterative chain elongation process and product release. Recent advances in structural elucidation of domains, didomains, and an entire termination module revealed valuable insights into the mechanism of nonribosomal synthesis and are highlighted herein.

PMID:
20153164
DOI:
10.1016/j.sbi.2010.01.009
[Indexed for MEDLINE]

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