EC Number   |
General Stability |
Reference |
|---|
   3.5.1.88 | additon of metal ions required during purification |
393803 |
| 3.5.1.88 | denaturation with guanidinium hydrochloride, protein 1 unfolds at more than 3 M, protein 2 unfolds at 1.7 M |
393815 |
| 3.5.1.88 | elimination of the divalent cation from the enzyme destabilizes the enzyme |
756111 |
| 3.5.1.88 | enhanced in vitro stability by binding of Zn2+ |
393798, 393799 |
| 3.5.1.88 | enhanced stabilitiy in concentrated form |
393807 |
| 3.5.1.88 | enhanced stability by binding of Co2+ |
393800 |
| 3.5.1.88 | extremely labile |
393805, 393806 |
| 3.5.1.88 | limited proteolysis of AtPDF1B with trypsin results in the relatively slow formation of a lower molecular mass form (AtPDF1Bt) reduced by approximately 3 kDa. Although small reductions in molecular mass are observed after prolonged incubation, the proteolyzed AtPDF1B generated was largely resistant to further digestion. Recombinant AtPDF1B has a requirement for 0.5 M NaCl for solubility at concentrations of 0.5 mg/ml. After proteolysis with trypsin, AtPDF1B loses this characteristic and is soluble without NaCl at concentrations of 30 mg/ml |
685008 |
| 3.5.1.88 | Ni2+ activates and stabilizes at 5 mM |
756147 |
| 3.5.1.88 | Ni2+ and Co2+ increase stability compared to the Fe2+ enzyme |
666013 |
