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Updated: Jul 16, 2026

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
Published on: October 4, 2019
Terpene synthases are highly substrate tolerant - among them BcBOT2 is a "jack of all trades"
Jan Luca Budde1, Mehdi D Davari2, Ahmed Hassanin2,3
1Institute of Organic Chemistry, Leibniz University Hannover, Schneiderberg 1B, D-30167 Hannover, Germany. andreas.kirschning@oci.uni-hannover.de.
Abstract:
Covering: up to 2026A traditional view regarding enzymes assigns them a markedly low substrate promiscuity. This is based, among other factors, on concepts concerning the evolution of metabolism, which, according to the "patchwork model", assumes that the first enzymes converted a variety of substrates more or less effectively into quite different products and that enzymes then differentiated through evolution and became more substrate selective. Starting from linear oligoprenyl diphosphate precursors, terpene synthases produce oligocyclic terpenes via complex carbocation cascades. It was found that these sometimes exhibit unusual substrate acceptance. Using the example of the fungal sesquiterpene synthase BcBOT2, it is shown that the "terpenome" can be expanded in an unprecedented way, whereby completely new terpene backbones can be generated that nature is usually unable to access, as of today.
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