EC Number   |
General Stability |
Reference |
|---|
    1.1.1.85 | at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa |
762765 |
| 1.1.1.85 | at pH 7.6, the enzyme from Shewanella oneidensis is slightly more stable against hydrostatic pressure than the enzyme from Shewanella benthica, contrary to the physiological pressures of their normal environments. Pressure unfolding of these enzymes (IPMDHs) follows a two-state unfolding model between a native dimer and two unfolded monomers, and the dimer structure is pressure-tolerant up to 200 MPa. The pressure-dependent activity does not originate from structural perturbations such as unfolding or dimer dissociation |
762765 |
| 1.1.1.85 | complete loss of activity in presence of 4 M urea |
639131 |
| 1.1.1.85 | dilute solutions, 1 mg/ml or less, precipitate upon thawing |
639148 |
| 1.1.1.85 | higher thermal stability of the dimer as compared to monomer. B24-B24' is the major contributor to maintaining subunit-subunit interaction at 64°C |
763370 |
| 1.1.1.85 | in contrast to 3-isopropylmalate dehydrogenase from other sources, K+ and Na+ are not essential for stability of the Sulfolobus enzyme |
639162 |
| 1.1.1.85 | K+ does not stabilize the enzyme |
639162 |
| 1.1.1.85 | slow inactivation occurs in presence of relatively high concentrations of EDTA, 0.01 M |
639148 |
