| Literature DB >> 20153164 |
Matthias Strieker1, Alan Tanović, Mohamed A Marahiel.
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.Mesh:
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Year: 2010 PMID: 20153164 DOI: 10.1016/j.sbi.2010.01.009
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809