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EC Number Renatured (Commentary) Reference
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363denatured in 8 M urea and dissociated into its two inactive subunits (MW 50000 Da). Denaturation leads to an approximately 80% decrease in protein fluorescence and a 20-nm red shift in the emission maximum. Upon dilution, the urea-treated enzyme regains catalytic activity (approximately 70%). The reactivated enzyme is indistinguishable from the native enzyme based on a number of physicochemical and enzymological criteria. The kinetics of renaturation and reactivation are monitored. Reactivation is stimulated to different degrees by either the initial or delayed addition of NAD+, NADP+, or glucose 6-phosphate. During the initial, rapid phase of renaturation, approximately 3 of the enzyme's 12 histidine residues become unreactive toward diethyl pyrocarbonate; concomitant with the subsequent reactivation, approximately 7 more histidines become inaccessible to diethyl pyrocarbonate 721570
Show all pathways known for 1.1.1.363Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.363in 4 M guanidine-HCl, the dimeric enzyme glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides dissociates to subunits and is extensively unfolded. Rapid dilution of this high guanidine hydrochloride concentration allowes the enzyme to partially renature. The fraction of the enzyme which does not renature aggregates and precipitates out of solution, a process which can not be substantially prevented by stabilizing additives. A renaturation mechanism is described, which involves a bi-unimolecular (subunit association-folding) reaction sequence. This mechanism involves an inactive, dimeric, glucose-6-phosphate dehydrogenase-folding intermediate 721695
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