| Literature DB >> 16880565 |
Peter M Brown1, Tom T Caradoc-Davies, James M Dickson, Garth J S Cooper, Kerry M Loomes, Edward N Baker.
Abstract
Myo-inositol oxygenase (MIOX) catalyzes the novel oxidative cleavage of myo-inositol (MI) and its epimer D-chiro inositol (DCI) to D-glucuronate. MIOX utilizes an Fe(II)/Fe(III) binuclear iron centre for the dioxygen-dependent cleavage of the C1-C6 bond in MI. Despite its key role in inositol metabolism, the structural basis of its unique four-electron oxidation mechanism and its substrate specificity remain unknown. In order to answer these questions and to facilitate the use of this key enzyme for the development of new therapeutic strategies for diabetes, the mouse enzyme has been cloned, expressed in Escherichia coli, purified and crystallized from 4.4 M sodium formate. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.87, b = 77.26, c = 84.84 angstroms, and diffract to 2.8 angstroms resolution.Entities:
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Year: 2006 PMID: 16880565 PMCID: PMC2242914 DOI: 10.1107/S1744309106028144
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091