General Stability | Organism |
---|---|
50% inactivation after 10 min in 1 M guanidinium HCl | Azotobacter vinelandii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
52000 | - |
x * 52000, model of quarternary structure, SDS-PAGE, immunoblot | Azotobacter vinelandii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter vinelandii | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
inactivation by 4 M guanidinium HCl, 4-6% reactivation after transfer in 100 mM Tris buffer, pH 7.5 containing 100 mM FAD | Azotobacter vinelandii |
Subunits | Comment | Organism |
---|---|---|
octamer | x * 52000, model of quarternary structure, SDS-PAGE, immunoblot | Azotobacter vinelandii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
approx. 50% activity lost after about 2 min, almost complete loss of activity after 20 min, biphasic inactivation: 70% activity lost with a first-order inactivation constant, 30% is lost much more rapidly, rate of thermal inactivation depends on concentration of NAD+, NADP+, NADH, NADPH, free FAD, Mg2+ and phosphate, independent of pH between pH 5 and pH 9, significant acceleration outside this range, addition of 1 mM FAD lowers inactivation rate about 20fold | Azotobacter vinelandii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | reduction of FAD leads to its dissociation at enzyme concentrations of 10-100 nM and 30°C-40°C, the apoenzyme can be reactivated to 10-15% by addition of FAD | Azotobacter vinelandii |