Literature summary for 1.1.1.47 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.

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General Stability

General Stability	Organism
unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl	Priestia megaterium
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

Organism	UniProt	Comment	Textmining
Priestia megaterium	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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

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

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Release 2023.1 (January 2023)