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Validation of an insertion-engineered isoprene synthase as a strategy to functionalize terpene synthases

RSC Adv. 2021-09; 
C Raul Gonzalez-Esquer, Bryan Ferlez, Sarathi M Weraduwage, Henning Kirst, Alexandra T Lantz, Aiko Turmo, Thomas D Sharkey, Cheryl A Kerfeld
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Bacterial Expression … was codon optimized for E. coli and the chloroplastic targeting peptide was removed from the gene (resulting in gene ISPS). All genes were ordered from Genscript Biotech (Piscataway … Get A Quote

摘要

Terpene synthases are biotechnologically-relevant enzymes with a variety of applications. However, they are typically poor catalysts and have been difficult to engineer. Structurally, most terpene synthases share two conserved domains (α- and β-domains). Some also contain a third domain containing a second active site (γ-domain). Based on the three-domain architecture, we hypothesized that αβ terpene synthases could be engineered by insertion of a heterologous domain at the site of the γ-domain (an approach we term "Insertion-engineering terpene synthase"; Ie-TS). We demonstrate that by mimicking the domain architecture of αβγ terpene synthases, we can redesign isoprene synthase (ISPS), an αβ terpene... More

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