General Stability | Organism |
---|---|
unfolding and denaturation in 6 M guanidinium hydrochloride, the protein almost completely unfolds in 4.0 M guanidinium hydrochloride, overview | Aspergillus fischeri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
guanidinium hydrochloride | the enzyme loses 54% and 70% of the original activity in 0.5 M and 1.0 M guanidinium hydrochloride, respectively. Irreversible denaturation at higher concentration of 6 M of guanidinium hydrochloride, kinetics, overview. The protein almost completely unfolds in 4.0 M guanidinium hydrochloride | Aspergillus fischeri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fischeri | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methylumbelliferyl alpha-D-mannopyranoside + H2O | - |
Aspergillus fischeri | 4-methylumbelliferol + alpha-D-mannopyranose | - |
? | |
4-nitrophenyl alpha-D-mannopyranoside + H2O | - |
Aspergillus fischeri | 4-nitrophenol + alpha-D-mannopyranose | - |
? |
Synonyms | Comment | Organism |
---|---|---|
class II alpha-mannosidase | - |
Aspergillus fischeri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Aspergillus fischeri |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 90 | activity is reduced by 8% at 50°C while positive ellipticity at 190-195 nm is almost same in the temperature range of 35-50°C. The activity is not affected in this range. At 60°C, 18% and at 70°C and above, 25% loss in the alpha-helical content of the protein occurs with significant decrease in the positive ellipticity, the protein does not completely unfold at 90°C | Aspergillus fischeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 6.5 | - |
Aspergillus fischeri |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
pH dependent denaturation, kinetics, overview | Aspergillus fischeri |
5 | 7 | the enzyme is most stable, inactivation below pH 5.0 and above pH 8.0 is irreversible | Aspergillus fischeri |