Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 466, Issue 2, Pages 260-266Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.06.016
Keywords
terpenoid synthase; farnesyl diphosphate; sesquiterpene; protein crystallography
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Funding
- NIGMS NIH HHS [R01 GM030301, R01 GM056838, R01 GM013956, R37 GM030301, GM13956, R01 GM056838-10, GM30301, GM56838] Funding Source: Medline
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Trichodiene synthase is a terpenoid cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to form the bicyclic sesquiterpene hydrocarbon trichodiene (89%), at least five sesquiterpene side products (11%), and inorganic pyrophosphate (PPi). Incubation of trichodiene synthase with 2-fluorofarnesyl diphosphate or 4-methylfarnesyl diphosphate similarly yields sesquiterpene mixtures despite the electronic effects or steric bulk introduced by substrate derivatization. The versatility of the enzyme is also demonstrated in the 2.85 A resolution X-ray crystal structure of the complex with Mg-3(2+)-PPi and the benzyl triethylammonium cation, which is a bulkier mimic of the bisabolyl carbocation intermediate in catalysis. Taken together, these findings show that the active site of trichodiene synthase is sufficiently flexible to accommodate bulkier and electronically-diverse substrates and intermediates, which could indicate additional potential for the biosynthetic utility of this terpenoid cyclase. (c) 2007 Elsevier Inc. All rights reserved.
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