Switching on a Nontraditional Enzymatic Base - Deprotonation by Serine in the ent-Kaurene Synthase from Bradyrhizobium japonicum

Meirong Jia, Yue Zhang, Justin B. Siegel, Dean J. Tantillo, Reuben J. Peters

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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 languageEnglish (US)
Pages (from-to)8867-8871
Number of pages5
JournalACS Catalysis
Volume9
Issue number10
DOIs
StatePublished - Jan 1 2019

Keywords

  • acid-base catalysis
  • biosynthesis
  • enzymology
  • natural products
  • terpene synthases

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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