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| Research article summary (published 30 Dec 2008): |
Chapter 14. Biosynthesis of nonribosomal peptide precursors.
Full Abstract
Nonribosomal peptides are natural products typically of bacterial and fungal origin. These highly complex molecules display a broad spectrum of biological activities, and have been exploited for the development of immunosuppressant, antibiotic, anticancer, and other therapeutic agents. The nonribosomal peptides are assembled by nonribosomal peptide synthetase (NRPS) enzymes comprising repeating modules that are responsible for the sequential selection, activation, and condensation of precursor amino acids. In addition to this, fatty acids, alpha-keto acids and alpha-hydroxy acids, as well as polyketide derived units, can also be utilized by NRPS assembly lines. Final tailoring-steps, including glycosylation and prenylation, serve to further decorate the nonribosomal peptides produced. The wide range of experimental methods that are employed in the elucidation of nonribosomal peptide precursor biosynthesis will be discussed, with particularly emphasis on genomics based approaches which have become wide spread over the last 5 years.
Author information
Author/s: Wilkinson, Barrie (B); Micklefield, Jason (J);
Affiliation: Biotica, Chesterford Research Park, Little Chesterford, Essex, United Kingdom.
Journal and publication information
Publication Type: Journal Article
Journal: Methods in enzymology (Methods Enzymol), published in United States. (Language: eng)
Reference: 2009-; vol 458 (issue ) : pp 353-78
Dates: Created 2009/04/20; Completed 2009/06/23;
PMID: 19374990, status: MEDLINE (last retrieval date: 6/23/2009, IMS Date: )
Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.
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