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Literature summary extracted from
- Truncation of the cellulose binding domain improved thermal stability of endo-beta-1,4-glucanase from Bacillus subtilis JA18 (2009), Biores. Technol., 100, 345-349.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.4 | expressed in Escherichia coli | Bacillus subtilis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.4 | additional information | C-terminus truncation mutant Egl330, truncation of the cellulose binding domain, a great improvement in thermal stability is observed in Egl330 | Bacillus subtilis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.4 | carboxymethylcellulose | binding of the cellulose-binding domain to avicel is inhibited by carboxymethylcellulose, but not by barley beta-glucan and glucose at concentration of 0.1% and 0.5% | Bacillus subtilis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.4 | additional information | - |
carboxymethylcellulose | Km of Egl330 and Egl499 are 1.73 x 10 mg/ml and 1.14 x 10 mg/ml, respectively. Vmax of Egl330 is 1.78fold higher than that of Egl499, increases from 284 U/mg to 786 U/mg. The catalytic efficiency (kcat/Km) of Egl330 is slightly higher than that of Egl499 | Bacillus subtilis |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 31000 | - |
C-terminus truncation mutant Egl330, calculated | Bacillus subtilis |
| 3.2.1.4 | 36000 | - |
C-terminus truncation mutant Egl330, calculated | Bacillus subtilis |
| 3.2.1.4 | 50000 | - |
Egl499 wild-type, SDS-PAGE | Bacillus subtilis |
| 3.2.1.4 | 55000 | - |
Egl499 wild-type, SDS-PAGE | Bacillus subtilis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.4 | Bacillus subtilis | - |
JA18 | - |
| 3.2.1.4 | Bacillus subtilis JA18 | - |
JA18 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.4 | affinity chromatography on Ni-NTA column | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.4 | barley beta-glucan + H2O | soluble substrate | Bacillus subtilis | ? | - |
? |  |
| 3.2.1.4 | barley beta-glucan + H2O | soluble substrate | Bacillus subtilis JA18 | ? | - |
? | |
| 3.2.1.4 | carboxymethylcellulose + H2O | soluble substrate | Bacillus subtilis | ? | - |
? | |
| 3.2.1.4 | carboxymethylcellulose + H2O | soluble substrate | Bacillus subtilis JA18 | ? | - |
? | |
| 3.2.1.4 | cellulose + H2O | - |
Bacillus subtilis | ? | - |
? | |
| 3.2.1.4 | cellulose + H2O | - |
Bacillus subtilis JA18 | ? | - |
? | |
| 3.2.1.4 | additional information | wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan | Bacillus subtilis | ? | - |
? | |
| 3.2.1.4 | additional information | wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan | Bacillus subtilis JA18 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.4 | Egl499 | - |
Bacillus subtilis |
| 3.2.1.4 | endo-beta-1,4-glucanase | - |
Bacillus subtilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 60 | - |
assay at | Bacillus subtilis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 50 | 75 | optimal enzymatic reaction temperature tested | Bacillus subtilis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 65 | 80 | - |
Bacillus subtilis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.4 | additional information | - |
additional information | kinetic analysis shows both the turnover rate (kcat) and the catalytic efficiency (kcat/Km) of Egl330 increased for the substrate carboxymethylcellulose compared to Egl499 | Bacillus subtilis | |
| 3.2.1.4 | 246 | - |
carboxymethylcellulose | wild-type | Bacillus subtilis | |
| 3.2.1.4 | 437 | - |
carboxymethylcellulose | the turnover rate (kcat) of Egl330 increased by 78% compared to wild-type | Bacillus subtilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 5.8 | - |
assay at | Bacillus subtilis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.4 | 4.5 | 7 | - |
Bacillus subtilis |
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