Mechanistic investigations on multiproduct β-himachalene synthase from Cryptosporangium arvum.

ABSTRACT: A bacterial terpene synthase from Cryptosporangium arvum was characterised as a multiproduct β-himachalene synthase. In vitro studies showed not only a high promiscuity with respect to its numerous sesquiterpene products, including the structurally demanding terpenes longicyclene, longifolene and α-longipinene, but also to its substrates, as additional activity was observed with geranyl- and geranylgeranyl diphosphate. In-depth mechanistic investigations using isotopically labelled precursors regarding the stereochemical course of both 1,11-cyclisation and 1,3-hydride shift furnished a detailed catalytic model suggesting the molecular basis of the observed low product selectivity. The enzyme's synthetic potential was also exploited in the preparation of sesquiterpene isotopomers, wh

SUBMITTER: Rinkel J 

PROVIDER: S-EPMC6541374 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature