Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of
Journal or Book Title
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.
American Chemical Society
Jia, Meirong; Zhang, Yue; Siegel, Justin B.; Tantillo, Dean J.; and Peters, Reuben J., "Switching on a Nontraditional Enzymatic Base—Deprotonation by Serine in the ent-Kaurene Synthase from Bradyrhizobium japonicum" (2019). Biochemistry, Biophysics and Molecular Biology Publications. 256.