Identification of amino acid networks governing catalysis in the closed complex of class I terpene synthases.

ABSTRACT: Class I terpene synthases generate the structural core of bioactive terpenoids. Deciphering structure-function relationships in the reactive closed complex and targeted engineering is hampered by highly dynamic carbocation rearrangements during catalysis. Available crystal structures, however, represent the open, catalytically inactive form or harbor nonproductive substrate analogs. Here, we present a catalytically relevant, closed conformation of taxadiene synthase (TXS), the model class I terpene synthase, which simulates the initial catalytic time point. In silico modeling of subsequent catalytic steps allowed unprecedented insights into the dynamic reaction cascades and promiscuity mechanisms of class I terpene synthases. This generally applicable methodology enables the active-site lo

SUBMITTER: Schrepfer P 

PROVIDER: S-EPMC4776449 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature