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Literature summary for 3.2.1.73 extracted from
- Cloning, expression of beta-1,3-1,4 glucanase from Bacillus subtilis SU40 and the effect of calcium ion on the stability of recombinant enzyme: in vitro and in silico analysis (2013), Bioinformation, 9, 958-962.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene SU40-glu, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Hg2+ | complete inhibition | Bacillus subtilis |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | metal ions such as Mn2+, Na+, K+, Mg2+ and Zn2+ show little or no effect on the enzyme activity | Bacillus subtilis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 24000 | - |
x * 24000, recombinant enzyme, SDS-PAGE | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | G0YW23 | gene SU40-glu | - |
| Bacillus subtilis SU40 | G0YW23 | gene SU40-glu | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| barley beta-glucan + H2O | - |
Bacillus subtilis | ? | - |
? | |
| barley beta-glucan + H2O | - |
Bacillus subtilis SU40 | ? | - |
? | |
| lichenan + H2O | - |
Bacillus subtilis | ? | - |
? | |
| lichenan + H2O | - |
Bacillus subtilis SU40 | ? | - |
? | |
| xylan + H2O | - |
Bacillus subtilis | ? | - |
? | |
| xylan + H2O | - |
Bacillus subtilis SU40 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 24000, recombinant enzyme, SDS-PAGE | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-1,3-1,4 glucanase | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Bacillus subtilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
purified recombinant enzyme, retains 54% activity at 80°C after incubation for 60 min | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Bacillus subtilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview | Bacillus subtilis |
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