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Issue 5, 2015
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Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

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Abstract

Covering up to 2014

Nonribosomal peptides (NRPs) account for a large portion of drugs and drug leads currently available in the pharmaceutical industry. They are one of two main families of natural products biosynthesized on megaenzyme assembly-lines composed of multiple modules that are, in general, each comprised of three core domains and on occasion of accompanying auxiliary domains. The core adenylation (A) domains are known to delineate the identity of the specific chemical components to be incorporated into the growing NRPs. Previously believed to be inactive, A domains interrupted by auxiliary enzymes have recently been proven to be active and capable of performing two distinct chemical reactions. This highlight summarizes current knowledge on A domains and presents the various interrupted A domains found in a number of nonribosomal peptide synthetase (NRPS) assembly-lines, their predicted or proven dual functions, and their potential for manipulation and engineering for chemoenzymatic synthesis of new pharmaceutical agents with increased potency.

Graphical abstract: Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

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Article information


Submitted
15 Sep 2014
First published
27 Jan 2015

Nat. Prod. Rep., 2015,32, 641-653
Article type
Highlight
Author version available

Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

K. J. Labby, S. G. Watsula and S. Garneau-Tsodikova, Nat. Prod. Rep., 2015, 32, 641
DOI: 10.1039/C4NP00120F

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