2q9z: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Single protein]]

[[Category: Trichodiene synthase]]

[[Category: Cane, D.E.]]

[[Category: Cane, D E.]]

[[Category: Christianson, D.W.]]

[[Category: Christianson, D W.]]

[[Category: Coates, R.M.]]

[[Category: Coates, R M.]]

[[Category: Koyama, T.]]

[[Category: Vedula, L.S.]]

[[Category: Vedula, L S.]]

[[Category: Zhao, Y.]]

[[Category: EDO]]

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[[Category: terpenoid synthase fold]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Trichodiene synthase]]
-[[Category: Cane, D.E.]]
+[[Category: Cane, D E.]]
-[[Category: Christianson, D.W.]]
+[[Category: Christianson, D W.]]
-[[Category: Coates, R.M.]]
+[[Category: Coates, R M.]]
 [[Category: Koyama, T.]]
-[[Category: Vedula, L.S.]]
+[[Category: Vedula, L S.]]
 [[Category: Zhao, Y.]]
 [[Category: EDO]]
@@ Line 28: / Line 28: @@
 [[Category: terpenoid synthase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:37:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:37:31 2008''