Literature summary for 1.1.1.47 extracted from

Maurer, E.; Pfleiderer, G.
Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. I. Conformational and functional changes (1985), Biochim. Biophys. Acta, 827, 381-388.

No PubMed abstract available

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General Stability

General Stability	Organism
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	-	-	-

Subunits

Subunits	Comment	Organism
More	the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers	Priestia megaterium
More	at very low ionic strength, the tetrameric state becomes unstable, even at pH 6.5	Priestia megaterium
More	complete dissociation at pH 9 is possible only at NaCl and KH2PO4 concentrations below 20 mM	Priestia megaterium

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
9	-	the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9 the enzyme is completely and reversibly dissociated into four inactive protomers	Priestia megaterium

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Release 2023.1 (January 2023)