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Structural biology and chemistry of the terpenoid cyclases.

David W. Christianson
- 01 Jun 2006 - 
- Vol. 106, Iss: 8, pp 3412-3442
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This article is published in Chemical Reviews.The article was published on 2006-06-01. It has received 665 citations till now.

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Glycosyltransferases: structures, functions, and mechanisms.

TL;DR: The expected two-step double-displacement mechanism is rendered less likely by the lack of conserved architecture in the region where a catalytic nucleophile would be expected, and a mechanism involving a short-lived oxocarbenium ion intermediate now seems the most likely, with the leaving phosphate serving as the base.
Journal ArticleDOI

The family of terpene synthases in plants: A mid-size family of genes for specialized metabolism that is highly diversified throughout the kingdom

TL;DR: The terpene synthases (TPSs) as mentioned in this paper are a family of enzymes responsible for the synthesis of various terpenes from two isomeric 5-carbon precursor molecules, leading to 5-carbinear isoprene, 10-carbon monoterpenes, 15-carbon sesquiterpenes and 20-carbenes.
Journal ArticleDOI

Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants.

TL;DR: This review covers the monoterpene and sesquiterpene synthases presenting an up-to-date list of enzymes reported and evidence for their ability to form multiple products.
References
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Journal ArticleDOI

Cation-π Interactions in Chemistry and Biology: A New View of Benzene, Phe, Tyr, and Trp

TL;DR: A great deal of direct and circumstantial evidence indicates that cation-π interactions are important in a variety of proteins that bind cationic ligands or substrates.
Journal ArticleDOI

Plant terpenoid synthases: Molecular biology and phylogenetic analysis

TL;DR: This review focuses on the monoterpene, sesquiterpenes, and diterpene synthases of plant origin that use the corresponding C10, C15, and C20 prenyl diphosphates as substrates to generate the enormous diversity of carbon skeletons characteristic of the terpenoid family of natural products.
Journal ArticleDOI

Structural Basis for Cyclic Terpene Biosynthesis by Tobacco 5-Epi-Aristolochene Synthase

TL;DR: These structures reveal an unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the stereochemical selectivity displayed by other cyclases in the biosynthesis of pharmacologically important cyclic terpenes.
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