Issue 3, 2018

Enhanced structural diversity in terpenoid biosynthesis: enzymes, substrates and cofactors

Abstract

The enormous diversity of terpenes found in nature is generated by enzymes known as terpene synthases, or cyclases. Some are also known for their ability to convert a single substrate into multiple products. This review comprises monoterpene and sesquiterpene synthases that are multiproduct in nature along with the regulation factors that can alter the product specificity of multiproduct terpene synthases without genetic mutations. Variations in specific assay conditions with focus on shifts in product specificity based on change in metal cofactors, assay pH and substrate geometry are described. Alterations in these simple cellular conditions provide the organism with enhanced chemodiversity without investing into new enzymatic architecture. This versatility to modulate product diversity grants organisms, especially immobile ones like plants with access to an enhanced defensive repertoire by simply altering cofactors, pH level and substrate geometry.

Graphical abstract: Enhanced structural diversity in terpenoid biosynthesis: enzymes, substrates and cofactors

Article information

Article type
Review Article
Submitted
16 8月 2017
Accepted
18 12月 2017
First published
18 12月 2017
This article is Open Access
Creative Commons BY license

Org. Biomol. Chem., 2018,16, 348-362

Enhanced structural diversity in terpenoid biosynthesis: enzymes, substrates and cofactors

A. Vattekkatte, S. Garms, W. Brandt and W. Boland, Org. Biomol. Chem., 2018, 16, 348 DOI: 10.1039/C7OB02040F

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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