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Exploring biosynthetic diversity with trichodiene synthase.

Archives of biochemistry and biophysics (2007-08-07)
L Sangeetha Vedula, Yuxin Zhao, Robert M Coates, Tanetoshi Koyama, David E Cane, David W Christianson
ZUSAMMENFASSUNG

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 (PP(i)). 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 2.85A resolution X-ray crystal structure of the complex with Mg(2+) (3)-PP(i) 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.

MATERIALIEN
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Marke
Produktbeschreibung

Sigma-Aldrich
Benzyltrimethylammoniumchlorid, 97%
Sigma-Aldrich
Benzyltrimethylammoniumhydroxid -Lösung, 40 wt. % in H2O
Sigma-Aldrich
Benzyltrimethylammoniumhydroxid -Lösung, 40 wt. % in methanol
Sigma-Aldrich
Benzyltrimethylammoniumbromid, 97%
Sigma-Aldrich
Benzyltrimethylammoniumchlorid -Lösung, technical, ~60% in H2O