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Using Terpene Synthase Plasticity in Catalysis: On the Enzymatic Conversion of Synthetic Farnesyl Diphosphate Analogues
Author(s) -
Hou Anwei,
Dickschat Jeroen S.
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202103049
Subject(s) - sesquiterpene , farnesyl diphosphate synthase , terpene , germacrene , atp synthase , enzyme , farnesol , chemistry , terpenoid , stereochemistry , prenyltransferase , farnesyl pyrophosphate , farnesyl diphosphate farnesyltransferase , biotransformation , biochemistry , biosynthesis , prenylation , farnesyltransferase
Abstract Four synthetic farnesyl diphosphate analogues were enzymatically converted with three bacterial sesquiterpene synthases, including β‐himachalene synthase (HcS) and ( Z )‐γ‐bisabolene synthase (BbS) from Cryptosporangium arvum , and germacrene A synthase (SmTS6) from Streptomyces mobaraensis . These enzyme reactions not only yielded several previously unknown compounds, showing that this approach opened the door to a new chemical space, but substrates with blocked or altered reactivities also gave interesting insights into the cyclisation mechanisms and the potential to catalyse reactions with different initial cyclisation modes.