Chimeric Terpene Synthases Possessing both Terpene Cyclization and Prenyltransfer Activities

Takaaki Mitsuhashi; Ikuro Abe

doi:10.1002/cbic.201800120

Chimeric Terpene Synthases Possessing both Terpene Cyclization and Prenyltransfer Activities

Chembiochem. 2018 Apr 20. doi: 10.1002/cbic.201800120. Online ahead of print.

Authors

Takaaki Mitsuhashi¹, Ikuro Abe¹

Affiliation

¹ Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.

PMID: 29675947
DOI: 10.1002/cbic.201800120

Abstract

Prenyltransferase (PT) and terpene synthase (TPS) are key enzymes in the formation of the basic carbon skeletons of terpenoids. The PTs determine the prenyl carbon chain length, whereas TPSs generate the structural complexity of the molecular scaffolds, forming various ring structures. Normally, PTs and TPSs are separate, independent enzymes. However, in 2007, a chimeric enzyme, in which the PT was fused with the TPS, was found in a fungus. Recent studies have revealed that such chimeric TPSs are widely distributed in fungi and function in the biosyntheses of various terpene natural products, including sesterterpenes, which are a relatively rare group of terpenoids. This review summarizes the accumulated knowledge of these recently discovered, unique, chimeric TPSs.

Keywords: biosynthesis; cyclization; enzymes; structure-activity relationships; terpenoids.

Publication types

Review