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Literature summary for 1.1.1.363 extracted from

  • Plomer, J.J.; Gafni, A.
    Denaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides by guanidine hydrochloride; identification of inactive, partially unfolded, dimeric intermediates (1992), Biochim. Biophys. Acta, 1122, 234-242.
    View publication on PubMed

Organic Solvent Stability

Organic Solvent Comment Organism
guanidine-HCl between 0.9 and 1.2 M denaturant the enzyme undergoes a conformational change, exposing tryptophan residues to solvent, with some loss of secondary structure and a complete loss of enzymatic activity but without dimer dissociation to subunits. This inactive, partially unfolded, dimeric intermediate was susceptible to slow aggregation. A second equilibrium transition, reflecting extensive unfolding and dimer dissociation, occurrs at denaturant concentrations above 1.4 M. In the denaturant concentration range of 1.7-1.9 M the fluorescence change occurrs in two distinct steps. The first step involves a large, very rapid drop in fluorescence whose rate is strongly dependent on the denaturant concentration. This is followed by a small, relatively slow rise in the emission intensity, the rate of which is independent of denaturant concentration. Enzymatic activity is lost with a denaturant-concentration-dependent rate, which is approx. 3times slower than the rate of the first step in fluorescence change. A denaturation mechanism incorporating several unfolding intermediates and which accounts for all the above results is presented and discussed. While the fully unfolded enzyme regains up to 55% of its original activity upon dilution of denaturant to a concentration that would be expected to support native enzyme, denaturation intermediates are able to reactivate only minimally and in fact are found to aggregate and precipitate out of solution Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
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