Record number :
1628787
Title of article :
Exploring biosynthetic diversity with trichodiene synthase
Author/Authors :
Vedula، نويسنده , , L. Sangeetha and Zhao، نويسنده , , Yuxin and Coates، نويسنده , , Robert M. and Koyama، نويسنده , , Tanetoshi and Cane، نويسنده , , David E. and Christianson، نويسنده , , David W.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
7
From page :
260
To page :
266
Abstract :
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 إ 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.
Keywords :
Terpenoid synthase , Farnesyl diphosphate , Protein Crystallography , sesquiterpene
Journal title :
Archives of Biochemistry and Biophysics
Link To Document :