Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Saccharolobus solfataricus |
expression in Escherichia coli | Saccharolobus solfataricus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
conduritol B epoxide | i.e. DL-1,2 anhydro-myo-inositol. The inhibitor is covalently bound to E387. Inhibitor-enzyme intermediate complex is formed more rapidly and hydrolyzed at a lower rate than it is for other glycosidases. One molecule of the inhibitor is covalently bound to each enzyme subunit | Saccharolobus solfataricus | |
DL-1,2 anhydro-myo-inositol | the enzyme is fully inactivated at 65°C in presence of the inhibitor, according to pseudo-first-order kinetics. The process takes place through the formation of a stabilized inhibitor-enzyme intermediate. One molecule of the inhibitor is covalently bound to each enzyme subunit. The inhibitor iss covalently bound to E387 | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl beta-D-glucopyranoside + H2O | - |
Saccharolobus solfataricus | 4-nitrophenol + beta-D-glucose | - |
? | |
4-nitrophenyl beta-D-glucoside + H2O | - |
Saccharolobus solfataricus | 4-nitrophenol + beta-D-glucose | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | - |
assay at | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Saccharolobus solfataricus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.25 | - |
DL-1,2 anhydro-myo-inositol | pH 6.5, 75°C | Saccharolobus solfataricus | |
0.25 | - |
conduritol B epoxide | pH 6.5, 65°C | Saccharolobus solfataricus |