Mitsuhashi Takaaki, Abe Ikuro
Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Chembiochem. 2018 Apr 20. doi: 10.1002/cbic.201800120.
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.
异戊烯基转移酶（PT）和萜类合酶（TPS）是萜类化合物基本碳骨架形成过程中的关键酶。PTs决定异戊烯基碳链长度，而TPSs则产生分子支架的结构复杂性，形成各种环状结构。通常情况下，PTs和TPSs是独立的酶。然而，2007年在一种真菌中发现了一种嵌合酶，其中PT与TPS融合。最近的研究表明，这种嵌合TPSs在真菌中广泛分布，并在包括倍半萜烯（一类相对罕见的萜类化合物）在内的各种萜类天然产物的生物合成中发挥作用。本综述总结了这些最近发现的独特嵌合TPSs的积累知识。
