Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase

The structure of ent-copalyl diphosphate synthase (CPS) reveals three α-helical domains (α, β, γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in CPS but exclusively in the α domain of taxadiene synthase....

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Autores principales: Köksal, Mustafa, Hu, Huayou, Coates, Robert M., Peters, Reuben J., Christianson, David W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3118866/
https://www.ncbi.nlm.nih.gov/pubmed/21602811
http://dx.doi.org/10.1038/nchembio.578
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author Köksal, Mustafa
Hu, Huayou
Coates, Robert M.
Peters, Reuben J.
Christianson, David W.
author_facet Köksal, Mustafa
Hu, Huayou
Coates, Robert M.
Peters, Reuben J.
Christianson, David W.
author_sort Köksal, Mustafa
collection PubMed
description The structure of ent-copalyl diphosphate synthase (CPS) reveals three α-helical domains (α, β, γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in CPS 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.
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spelling pubmed-31188662012-01-01 Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase Köksal, Mustafa Hu, Huayou Coates, Robert M. Peters, Reuben J. Christianson, David W. Nat Chem Biol Article The structure of ent-copalyl diphosphate synthase (CPS) reveals three α-helical domains (α, β, γ), as also observed in the related diterpene cyclase taxadiene synthase. However, active sites are located at the interface of the βγ domains in CPS 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. 2011-05-22 /pmc/articles/PMC3118866/ /pubmed/21602811 http://dx.doi.org/10.1038/nchembio.578 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Köksal, Mustafa
Hu, Huayou
Coates, Robert M.
Peters, Reuben J.
Christianson, David W.
Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title_full Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title_fullStr Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title_full_unstemmed Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title_short Structure and Mechanism of the Diterpene Cyclase ent-Copalyl Diphosphate Synthase
title_sort structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3118866/
https://www.ncbi.nlm.nih.gov/pubmed/21602811
http://dx.doi.org/10.1038/nchembio.578
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