skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Abstract

The structure of ent-copalyl diphosphate synthase reveals three {alpha}-helical domains ({alpha}, {beta} and {gamma}), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the {beta}{gamma} domains in ent-copalyl diphosphate synthase but exclusively in the {alpha} 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:
; ; ; ;  [1];  [2];  [2]
  1. (UIUC)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1023674
Resource Type:
Journal Article
Journal Name:
Nat. Chem. Biol.
Additional Journal Information:
Journal Volume: 7; Journal Issue: 07, 2011
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CYCLASES; CYCLIZATION; ENZYMES; INTERFACES; ISOMERASES; TERPENES

Citation Formats

Köksal, Mustafa, Hu, Huayou, Coates, Robert M., Peters, Reuben J., Christianson, David W., Iowa State), and Penn). Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. United States: N. p., 2011. Web. doi:10.1038/nchembio.578.
Köksal, Mustafa, Hu, Huayou, Coates, Robert M., Peters, Reuben J., Christianson, David W., Iowa State), & Penn). Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. United States. doi:10.1038/nchembio.578.
Köksal, Mustafa, Hu, Huayou, Coates, Robert M., Peters, Reuben J., Christianson, David W., Iowa State), and Penn). Tue . "Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase". United States. doi:10.1038/nchembio.578.
@article{osti_1023674,
title = {Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase},
author = {Köksal, Mustafa and Hu, Huayou and Coates, Robert M. and Peters, Reuben J. and Christianson, David W. and Iowa State) and Penn)},
abstractNote = {The structure of ent-copalyl diphosphate synthase reveals three {alpha}-helical domains ({alpha}, {beta} and {gamma}), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the {beta}{gamma} domains in ent-copalyl diphosphate synthase but exclusively in the {alpha} 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.},
doi = {10.1038/nchembio.578},
journal = {Nat. Chem. Biol.},
number = 07, 2011,
volume = 7,
place = {United States},
year = {2011},
month = {9}
}