title: 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.
authors: Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
authors: Mustafa
authors: M
authors: Köksal
authors: Huayou
authors: H
authors: Hu
authors: Robert M
authors: RM
authors: Coates
authors: Reuben J
authors: RJ
authors: Peters
authors: David W
authors: DW
authors: Christianson
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