Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli. Chi255 is excessively degraded by the action of Escherichia coli proteases. When the chitin binding domain (CBD) is deleted from Chi255, an active form (Chi2555DELTA5) of expected size of about 60000 Da is extracted from the Escherichia coli periplasmic fraction, without the observation of any proteolytic degradation | Bacillus thuringiensis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | in vitro progressive C-terminal Chi255 deleted derivatives are constructed in order to study their stability and their activity in Escherichia coli. When the chitin binding domain (CBD) is deleted from Chi255, an active form (Chi2555DELTA5) of expected size of about 60000 Da is extracted from the Escherichia coli periplasmic fraction, without the observation of any proteolytic degradation. Compared to Chi255, Chi255DELTA5 exhibits a higher chitinase activity on colloidal chitin. Both of the enzymes exhibit activities at broad pH and temperature ranges with maximal enzyme activities at pH 5 and pH 6 and at temperatures 50°C and 40°C, respectively for Chi255 and Chi255D5 | Bacillus thuringiensis |
General Stability | Organism |
---|---|
Chi255 is excessively degraded by the action of Escherichia coli proteases | Bacillus thuringiensis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Bacillus thuringiensis | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
70665 | - |
x * 70665, calculated from nucleotide sequence | Bacillus thuringiensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thuringiensis | - |
subsp. Kurstaki | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
colloidal chitin + H2O | - |
Bacillus thuringiensis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 70665, calculated from nucleotide sequence | Bacillus thuringiensis |
Synonyms | Comment | Organism |
---|---|---|
chitinase Chi255 | - |
Bacillus thuringiensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
mutant enzyme Chi255DELTA5 | Bacillus thuringiensis |
50 | - |
wild-type enzyme Chi25 | Bacillus thuringiensis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 80 | 30°C: about 25% of maximal activity, 50°C: about 70% of maximal activit, 60°C: no activity, 80°C: about 25% of maximal activity, mutant enzyme Chi255DELTA5 | Bacillus thuringiensis |
30 | 80 | 30°C: about 25% of maximal activity, 60°C: no activity, 80°C: about 15% of maximal activity, wild-type enzyme Chi25 | Bacillus thuringiensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
wild-type enzyme Chi255, a second pH optimum at pH 9.0 (40% of the activity at pH 5) | Bacillus thuringiensis |
6 | - |
mutant enzyme Chi255DELTA5, a second pH optimum at pH 9.0 (27% of the activity at pH 5) | Bacillus thuringiensis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 7 | pH 4.0: about 35% of maximal activity, pH 7.0: about 80% of maximal activity, mutant enzyme Chi255DELTA5 | Bacillus thuringiensis |
4 | 7 | pH 4.0: about 55% of maximal activity, pH 7.0: about 55% of maximal activity, wild-type enzyme Chi255 | Bacillus thuringiensis |