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Literature summary for 3.2.1.14 extracted from

  • Cai, W.; Sha, L.; Zhou, J.; Huang, Z.; Guan, X.
    Functional analysis of active site residues of Bacillus thuringiensis WB7 chitinase by site-directed mutagenesis (2009), World J. Microbiol. Biotechnol., 25, 2147-2155.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus thuringiensis

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of the three-dimensional structure of catalytic domain Bacillus thuringiensis

Protein Variants

Protein Variants Comment Organism
D205E 48% decrease in activity, narrow active pH range Bacillus thuringiensis
D205N inactive Bacillus thuringiensis
D207E inactive Bacillus thuringiensis
D207N inactive Bacillus thuringiensis
E209D inactive Bacillus thuringiensis
E209Q 29% decrease in activity, broad active pH range Bacillus thuringiensis
F201L inactive Bacillus thuringiensis
F201Y 72% decrease in activity, narrow active pH range Bacillus thuringiensis
G203A 70% decrease in activity, narrow active pH range Bacillus thuringiensis
G203D inactive Bacillus thuringiensis
W208C inactive Bacillus thuringiensis
W208R 31% decrease in activity Bacillus thuringiensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
74000
-
x * 74000, calculated Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-
Bacillus thuringiensis WB7
-
-
-

Subunits

Subunits Comment Organism
? x * 74000, calculated Bacillus thuringiensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
mutant G203A Bacillus thuringiensis
60
-
wild-type as well as mutants F201Y, D205E, W208R and E209Q Bacillus thuringiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
wild-type as well as mutants F201Y, G203A, D205E, W208R and E209Q Bacillus thuringiensis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus thuringiensis calculated
-
5.9