Issue 15, 2022
From the journal:

Chemical Science

Enzymology of standalone elongating ketosynthases

Aochiu Chen, ORCID logo a   Ziran Jiang ORCID logo a  and  Michael D. Burkart ORCID logo *a  

* Corresponding authors

a Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA
E-mail: mburkart@ucsd.edu

Abstract

The β-ketoacyl-acyl carrier protein synthase, or ketosynthase (KS), catalyses carbon–carbon bond formation in fatty acid and polyketide biosynthesis via a decarboxylative Claisen-like condensation. In prokaryotes, standalone elongating KSs interact with the acyl carrier protein (ACP) which shuttles substrates to each partner enzyme in the elongation cycle for catalysis. Despite ongoing research for more than 50 years since KS was first identified in E. coli, the complex mechanism of KSs continues to be unravelled, including recent understanding of gating motifs, KS–ACP interactions, substrate recognition and delivery, and roles in unsaturated fatty acid biosynthesis. In this review, we summarize the latest studies, primarily conducted through structural biology and molecular probe design, that shed light on the emerging enzymology of standalone elongating KSs.

Graphical abstract: Enzymology of standalone elongating ketosynthases

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Article information

DOI
https://doi.org/10.1039/D1SC07256K
Article type
Review Article
Submitted
30 Dec 2021
Accepted
09 Mar 2022
First published
09 Mar 2022
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2022,13, 4225-4238

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Enzymology of standalone elongating ketosynthases

A. Chen, Z. Jiang and M. D. Burkart, Chem. Sci., 2022, 13, 4225 DOI: 10.1039/D1SC07256K

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