Issue 13, 2019

Mechanistic characterization of three sesquiterpene synthases from the termite-associated fungus Termitomyces

Abstract

Three terpene synthases from the termite associated fungus Termitomyces were functionally characterized as (+)-intermedeol synthase, (−)-γ-cadinene synthase and (+)-germacrene D-4-ol synthase, with the germacrene D-4-ol synthase as the first reported enzyme that produces the (+)-enantiomer. The enzymatic mechanisms were thoroughly investigated by incubation with isotopically labeled precursors to follow the stereochemical courses of single reaction steps in catalysis. The role of putative active site residues was tested by site directed mutagenesis of a highly conserved tryptophan in all three enzymes and additional residues in (−)-γ-cadinene synthase that were identified by homology model analysis.

Graphical abstract: Mechanistic characterization of three sesquiterpene synthases from the termite-associated fungus Termitomyces

Supplementary files

Article information

Article type
Paper
Submitted
05 noy 2018
Accepted
22 yan 2019
First published
22 yan 2019

Org. Biomol. Chem., 2019,17, 3348-3355

Mechanistic characterization of three sesquiterpene synthases from the termite-associated fungus Termitomyces

I. Burkhardt, N. B. Kreuzenbeck, C. Beemelmanns and J. S. Dickschat, Org. Biomol. Chem., 2019, 17, 3348 DOI: 10.1039/C8OB02744G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements