Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Driss, F.; Baanannou, A.; Rouis, S.; Masmoudi, I.; Zouari, N.; Jaoua, S.
    Effect of the chitin binding domain deletion from Bacillus thuringiensis subsp. kurstaki chitinase Chi255 on its stability in Escherichia coli (2007), Mol. Biotechnol., 36, 232-237.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.14 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

EC Number Protein Variants Comment Organism
3.2.1.14 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

EC Number General Stability Organism
3.2.1.14 Chi255 is excessively degraded by the action of Escherichia coli proteases Bacillus thuringiensis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.14 extracellular
-
 Bacillus thuringiensis
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.14 70665
-
 x * 70665, calculated from nucleotide sequence Bacillus thuringiensis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.14 Bacillus thuringiensis
-
 subsp. Kurstaki
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.14 colloidal chitin + H2O
-
 Bacillus thuringiensis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.14 ? x * 70665, calculated from nucleotide sequence Bacillus thuringiensis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.14 chitinase Chi255
-
 Bacillus thuringiensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.14 40
-
 mutant enzyme Chi255DELTA5 Bacillus thuringiensis
3.2.1.14 50
-
 wild-type enzyme Chi25 Bacillus thuringiensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.14 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
3.2.1.14 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.14 5
-
 wild-type enzyme Chi255, a second pH optimum at pH 9.0 (40% of the activity at pH 5) Bacillus thuringiensis
3.2.1.14 6
-
 mutant enzyme Chi255DELTA5, a second pH optimum at pH 9.0 (27% of the activity at pH 5) Bacillus thuringiensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.14 4 7 pH 4.0: about 35% of maximal activity, pH 7.0: about 80% of maximal activity, mutant enzyme Chi255DELTA5 Bacillus thuringiensis
3.2.1.14 4 7 pH 4.0: about 55% of maximal activity, pH 7.0: about 55% of maximal activity, wild-type enzyme Chi255 Bacillus thuringiensis