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Literature summary for 3.1.3.1 extracted from
- Reversible inactivation of alkaline phosphatase from Atlantic cod (Gadus morhua) in urea (2006), Biochim. Biophys. Acta, 1764, 190-198.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Urea | reversible inactivation. At low concentrations of urea, the first detected alteration in properties is an increase in the activity of the enzyme. This is followed by inactivation and the release of half of the zinc content when the amount of urea reaches levels of 2 M. Intrinsic tryptophan fluorescence and circular dichroism ellipticity change in the range 2.5 to 8 M urea, signalling dimer dissociation, followed by one major monomer unfolding transition at 6-8 M urea as indicated by ANS fluorescence and KI fluorescence quenching | Gadus morhua |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Magnesium | enzyme contains magnesium | Gadus morhua | |
| Zinc | enzyme contains zinc | Gadus morhua | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gadus morhua | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| incubation in 4 M urea followed by a 15fold dilution of the urea at pH 7.5 results in a 100% recovery of initial activity after 20 or 90 min | Gadus morhua |
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