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| - Isopentenyl Diphosphate Isomerase. Mechanism-BasedInhibition by Diene Analogues of Isopentenyl Diphosphateand Dimethylallyl Diphosphate
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| - Isopentenyl diphosphate isomerase (IDI) catalyzes the interconversion of isopentenyl diphosphate(IPP) and dimethylallyl diphosphate (DMAPP). This is an essential step in the mevalonate entry into theisoprenoid biosynthetic pathway. The isomerization catalyzed by type I IDI involves protonation of thecarbon−carbon double bond in IPP or DMAPP to form a tertiary carbocation, followed by deprotonation.Diene analogues for DMAPP (E-2-OPP and Z-2-OPP) and IPP (4-OPP) were synthesized and found to bepotent active-site-directed irreversible inhibitors of the enzyme. X-ray analysis of the E·I complex betweenEscherichia coli IDI and 4-OPP reveals the presence of two isomers that differ in the stereochemistry ofthe newly formed C3−C4 double bond in the hydrocarbon chain of the inhibitor. In both adducts C5 of theinhibitor is joined to the sulfur of C67. In these structures the methyl group formed upon protonation of thediene moiety in 4-OPP is located near E116, implicating that residue in the protonation step.
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