Premium
Stereochemical Studies of the Type II Isopentenyl Diphosphate–Dimethylallyl Diphosphate Isomerase Implicate the FMN Coenzyme in Substrate Protonation
Author(s) -
Calveras Jordi,
Thibodeaux Christopher J.,
Mansoorabadi Steven O.,
Liu Hungwen
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100694
Subject(s) - isomerase , chemistry , protonation , cofactor , substrate (aquarium) , stereochemistry , catalysis , biochemistry , enzyme , organic chemistry , biology , ion , ecology
The type II isopentenyl diphosphate: Dimethylallyl diphosphate isomerase (IDI‐2) is a flavoenzyme catalyzing the interconversion of IPP and DMAPP (see scheme). Chiral methyl analysis and proton inventory studies were used to probe the stereochemical course of this reaction. The results suggest that FMN acts as both the acid and base in IDI‐2 catalysis.