R
Robert M. Coates
Researcher at University of Illinois at Urbana–Champaign
Publications - 182
Citations - 6557
Robert M. Coates is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Diterpene & Cyclase. The author has an hindex of 42, co-authored 179 publications receiving 6193 citations. Previous affiliations of Robert M. Coates include University of Kentucky.
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Journal ArticleDOI
Redirection of cytosolic or plastidic isoprenoid precursors elevates terpene production in plants.
TL;DR: The strategy increased synthesis of the sesquiterpenes patchoulol and amorpha-4,11-diene more than 1,000-fold, as well as the monoterpene limonene 10–30 fold, and seems equally suited to generating higher levels of other terpenes for research, industrial production or therapeutic applications.
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Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase.
Douglas A. Whittington,Mitchell L. Wise,Marek Urbansky,Robert M. Coates,Rodney Croteau,David W. Christianson +5 more
TL;DR: Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide “snapshots” of the terpene cyclization cascade.
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Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis
Mustafa Köksal,Yinghua Jin,Yinghua Jin,Robert M. Coates,Rodney Croteau,David W. Christianson +5 more
TL;DR: The X-ray crystal structure of a truncation variant lacking the transit sequence and an additional 27 residues at the N terminus is reported, hereafter designated TXS, which reveals a definitive connection between the two distinct cyclase classes in the evolution of terpenoid biosynthesis.
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Structure of limonene synthase, a simple model for terpenoid cyclase catalysis
David Hyatt,BuHyun Youn,Yuxin Zhao,Bindu Santhamma,Robert M. Coates,Rodney Croteau,ChulHee Kang +6 more
TL;DR: The crystal structure of (4S)-limonene synthase from Mentha spic ata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-Å; resolution in two forms liganded to the substrate and intermediate analogs.
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Identification of syn-pimara-7,15-diene synthase reveals functional clustering of terpene synthases involved in rice phytoalexin/allelochemical biosynthesis.
TL;DR: The observed correlation between physical proximity and common metabolic function indicates that other such class I and class II terpene synthase gene clusters may similarly catalyze consecutive reactions in shared biosynthetic pathways.