Issue 1, 2012
From the journal:

Natural Product Reports

Beyond ethylmalonyl-CoA: The functional role of crotonyl-CoAcarboxylase/reductase homologs in expanding polyketide diversity

Micheal C. Wilsona  and  Bradley S. Moore*ab  

* Corresponding authors

a Scripps Institution of Oceanography, University of California at San Diego, La Jolla, California, USA

b Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, California, USA
E-mail: bsmoore@ucsd.edu

Abstract

Covering: up through August 2011

This review covers the emerging biosynthetic role of crotonyl-CoA carboxylase/reductase (CCR) homologs in extending the structural and functional diversity of polyketide natural products. CCRs catalyze the reductive carboxylation of α,β-unsaturated acyl-CoA substrates to produce a variety of substituted malonyl-CoA derivatives employed as polyketide synthase extender units. Here we discuss the history of CCRs in both primary and secondary metabolism, the mechanism by which they function, examples of new polyketide diversity from pathway specific CCRs, and the role of CCRs in facilitating the bioengineering novel polyketides.

Graphical abstract: Beyond ethylmalonyl-CoA: The functional role of crotonyl-CoA carboxylase/reductase homologs in expanding polyketide diversity

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Article information

DOI
https://doi.org/10.1039/C1NP00082A
Article type
Review Article
Submitted
18 Oct 2011
First published
29 Nov 2011

Nat. Prod. Rep., 2012,29, 72-86

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Beyond ethylmalonyl-CoA: The functional role of crotonyl-CoA carboxylase/reductase homologs in expanding polyketide diversity

M. C. Wilson and B. S. Moore, Nat. Prod. Rep., 2012, 29, 72 DOI: 10.1039/C1NP00082A

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