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The multi-domain enzyme isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix was studied by denaturant-induced unfolding. At pH 7.5, changes in circular dichroism ellipticity and intrinsic fluorescence showed a complex unfolding transition, whereas at pH 3.0, an apparently two-state and highly reversible unfolding occurred. Analytical ultracentrifugation revealed the dissociation from...
Isocitrate dehydrogenase from Aeropyrum pernix (ApIDH) is a homodimeric enzyme that belongs to the β-decarboxylating dehydrogenase family and is the most thermostable IDH identified. It catalyzes the NADP + and metal-dependent oxidative decarboxylation of isocitrate to α-ketoglutarate. We have solved the crystal structures of a native ApIDH at 2.2Å, a pseudo-native ApIDH at 2.1Å, and of ApIDH...
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