Literature summary extracted from
Nakano, M.; Sacktor, B.
Isolation and characterization of four forms of trehalase from rabbit kidney cortex (1985), J. Biochem., 97, 1329-1335.
General Stability
EC Number |
General Stability |
Organism |
---|
3.2.1.28 |
enzyme form A1 becomes labile on addition of glycerol, activity in presence of 20% or 40% glycerol is about 30-40% lower than in absence of glycerol. Enzyme form B2 becomes more stable on addition of glycerol, activity in presence of 20% or 40% glycerol is about 30 higher than in absence of glycerol |
Oryctolagus cuniculus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.2.1.28 |
Hg2+ |
the glycoprotein enzyme forms are more susceptible than the nonglycoprotein forms |
Oryctolagus cuniculus |
|
3.2.1.28 |
methyl beta-glucoside |
- |
Oryctolagus cuniculus |
|
3.2.1.28 |
phlorizin |
- |
Oryctolagus cuniculus |
|
3.2.1.28 |
Tris |
- |
Oryctolagus cuniculus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.2.1.28 |
Na+ |
the glycoprotein enzyme forms show lower activation than the nonglycoprotein forms |
Oryctolagus cuniculus |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.2.1.28 |
175000 |
- |
gel filtration |
Oryctolagus cuniculus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.28 |
Oryctolagus cuniculus |
- |
2 nonglycoprotein enzyme forms: A1 and B1 and 2 glycoprotein enzyme form A2 and B2 |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.2.1.28 |
glycoprotein |
2 nonglycoprotein enzyme forms: A1 and B1, and 2 glycoprotein enzyme forms: A2 and B2 |
Oryctolagus cuniculus |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.2.1.28 |
4 enzyme form |
Oryctolagus cuniculus |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
3.2.1.28 |
kidney |
cortex |
Oryctolagus cuniculus |
- |
Storage Stability
EC Number |
Storage Stability |
Organism |
---|
3.2.1.28 |
-80°C, 9 days, 15% loss of activity of enzyme form A1, 5% loss of activity of enzyme form A2, 35% loss of activity of enzyme form B1, 65% loss of activity of enzyme form B2 |
Oryctolagus cuniculus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.2.1.28 |
trehalose + H2O |
- |
Oryctolagus cuniculus |
D-glucose |
- |
? |
|
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.2.1.28 |
5.8 |
6 |
phosphate buffer |
Oryctolagus cuniculus |