Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

General Stability

EC Number General Stability Organism
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
-
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.47 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
1.1.1.47 More at very low ionic strength, the tetrameric state becomes unstable, even at pH 6.5 Priestia megaterium
1.1.1.47 More complete dissociation at pH 9 is possible only at NaCl and KH2PO4 concentrations below 20 mM Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.47 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