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

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 enzy...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2019, Vol.17 (13), p.3348-3355
Main Authors: Burkhardt, Immo, Kreuzenbeck, Nina B, Beemelmanns, Christine, Dickschat, Jeroen S
Format: Article
Language:English
Subjects:
Cadinene
Catalysis
Cloning
Enantiomers
Enzymes
Fungi
Germacrene
Homology
Mutagenesis
NMR
Nuclear magnetic resonance
Residues
Site-directed mutagenesis
Tryptophan
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Summary: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.
ISSN:1477-0520
1477-0539
DOI:10.1039/c8ob02744g