Title : The type II isopentenyl Diphosphate:Dimethylallyl diphosphate isomerase (IDI-2): A model for acid/base chemistry in flavoenzyme catalysis.

Pub. Date : 2017 Oct 15

PMID : 28577910






4 Functional Relationships(s)
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1 Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens
2 Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens
3 While not entirely without precedent, IDI-2 is by far the most extensively studied flavoenzyme that employs flavin-mediated acid/base catalysis. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens
4 Thus, IDI-2 serves as an important mechanistic model for understanding this often overlooked, but potentially widespread reactivity of flavin coenzymes. 4,6-dinitro-o-cresol isopentenyl-diphosphate delta isomerase 2 Homo sapiens