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 | UniProt | Comment | Textmining |
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Priestia megaterium | - |
- |
- |
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 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 |