Abstract
Terpene synthases often catalyze complex carbocation cascade reactions. It has been previously shown that single-residue switches involving replacement of a key aliphatic residue with serine or threonine can "short-circuit" such reactions that are presumed to act indirectly via dipole stabilization of intermediate carbocations. Here a similar switch was found in the structurally characterized ent-kaurene synthase from Bradyrhizobium japonicum. Application of a recently developed computational approach to terpene synthases, TerDockin, surprisingly indicates direct action of the introduced serine hydroxyl as a catalytic base. Notably, this model suggests an alternative interpretation of previous results and potential routes toward reengineering terpene synthase activity more generally.
Original language | English (US) |
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Pages (from-to) | 8867-8871 |
Number of pages | 5 |
Journal | ACS Catalysis |
Volume | 9 |
Issue number | 10 |
DOIs | |
State | Published - Jan 1 2019 |
Keywords
- acid-base catalysis
- biosynthesis
- enzymology
- natural products
- terpene synthases
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)