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Issue 20, 2021
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Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node

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Abstract

Chorismate and isochorismate represent an important branching point connecting primary and secondary metabolism in bacteria, fungi, archaea and plants. Chorismate- and isochorismate-converting enzymes are potential targets for new bioactive compounds, as well as valuable biocatalysts for the in vivo and in vitro synthesis of fine chemicals. The diversity of the products of chorismate- and isochorismate-converting enzymes is reflected in the enzymatic three-dimensional structures and molecular mechanisms. Due to the high reactivity of chorismate and its derivatives, these enzymes have evolved to be accurately tailored to their respective reaction; at the same time, many of them exhibit a fascinating flexibility regarding side reactions and acceptance of alternative substrates. Here, we give an overview of the different (sub)families of chorismate- and isochorismate-converting enzymes, their molecular mechanisms, and three-dimensional structures. In addition, we highlight important results of mutagenetic approaches that generate a broader understanding of the influence of distinct active site residues for product formation and the conversion of one subfamily into another. Based on this, we discuss to what extent the recent advances in the field might influence the general mechanistic understanding of chorismate- and isochorismate-converting enzymes. Recent discoveries of new chorismate-derived products and pathways, as well as biocatalytic conversions of non-physiological substrates, highlight how this vast field is expected to continue developing in the future.

Graphical abstract: Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node

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Article information


Submitted
12 Dec 2020
Accepted
12 Feb 2021
First published
19 Feb 2021

This article is Open Access

Chem. Commun., 2021,57, 2441-2463
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Chorismate- and isochorismate converting enzymes: versatile catalysts acting on an important metabolic node

F. Hubrich, M. Müller and J. N. Andexer, Chem. Commun., 2021, 57, 2441
DOI: 10.1039/D0CC08078K

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