Isopentenyl diphosphate isomerase (IDI) catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), the basic building blocks of isoprenoid compounds.  Two structurally unrelated forms of IDI are known.  IDI-1, discovered in the late 1950s, uses a divalent metal to facilitate a protonation-deprotonation reaction; whereas, IDI-2, discovered in 2001, requires reduced flavin mononucleotide (FMN).  Both protonation-deprotonation and hydrogen atom addition-abstration mechanisms have been suggested for IDI-2.  The use of substrate analogs of IPP and DMAPP to distinguish between the two mechanisms for IDI-2 will be discussed.

Isopentenyl diphosphate isomerase: Mechanistic studies of the type-2 enzyme

240th National Meeting (2010)

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