Literature DB >> 29455106

Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.

Trey A Ronnebaum1, Audrey L Lamb2.   

Abstract

Microbes synthesize small, iron-chelating molecules known as siderophores to acquire iron from the environment. One way siderophores are generated is by nonribosomal peptide synthetases (NRPSs). The bioactive peptides generated by NRPS enzymes have unique chemical features, which are incorporated by accessory and tailoring domains or proteins. The first part of this review summarizes recent progress in NRPS structural biology. The second part uses the biosynthesis of pyochelin, a siderophore from Pseudomonas aeruginosa, as a case study to examine enzymatic methods for generating the observed diversity in NRPS-derived natural products.
Copyright © 2018 Elsevier Ltd. All rights reserved.

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Year:  2018        PMID: 29455106      PMCID: PMC6093814          DOI: 10.1016/j.sbi.2018.01.015

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  68 in total

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4.  In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities.

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10.  Catalytic trajectory of a dimeric nonribosomal peptide synthetase subunit with an inserted epimerase domain.

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