Issue 5, 2015

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

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

Article information

Article type
Highlight
Submitted
15 set 2014
First published
27 jan 2015

Nat. Prod. Rep., 2015,32, 641-653

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements