Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase.

ABSTRACT: The structure of ent-copalyl diphosphate synthase reveals three α-helical domains (α, β and γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in ent-copalyl diphosphate synthase but exclusively in the α domain of taxadiene synthase. Modular domain architecture in plant diterpene cyclases enables the evolution of alternative active sites and chemical strategies for catalyzing isoprenoid cyclization reactions.

SUBMITTER: Koksal M 

PROVIDER: S-EPMC3118866 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature