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Literature summary extracted from

  • Pauly, H.E.; Pfleiderer, G.
    Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenase (1977), Biochemistry, 16, 4599-4604.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.1.47 unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl Priestia megaterium
1.1.1.47 unstable at low ionic strength, in 67 mM phosphate buffer enzyme activity decreases to 80% within 5 hours at pH 6.5 and 0.01 mg/ml protein, reduction to 57% at 40 mM phosphate, high concentration of NAD inhibit dissociation Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Priestia megaterium
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.1.47 renaturation of enzyme denatured by urea, restores more than 90% of the original activity 60 min after dilution and after complete dialysis. Optimal temperature for refolding is 25°C Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.47 additional information
-
-
 Priestia megaterium
1.1.1.47 4
-
 30 min, about 50% loss of activity Priestia megaterium
1.1.1.47 5 6.5 30 min, stable Priestia megaterium
1.1.1.47 7.3
-
 30 min, about 50% loss of activity Priestia megaterium
1.1.1.47 7.5
-
 30 min, about 95% loss of activity Priestia megaterium
1.1.1.47 9
-
-
 Priestia megaterium