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Literature summary for 3.2.1.39 extracted from
- A first glycoside hydrolase family 50 endo-beta-1,3-D-glucanase from Pseudomonas aeruginosa (2018), Enzyme Microb. Technol., 108, 34-41 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Pseudomonas aeruginosa |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | not influenced by metal ions | Pseudomonas aeruginosa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 83400 | - |
gel filtration | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | A0A223GEG1 | - |
- |
| Pseudomonas aeruginosa CAU 342A | A0A223GEG1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| curdlan + H2O | 100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide | Pseudomonas aeruginosa | ? | - |
? |  |
| curdlan + H2O | 100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide | Pseudomonas aeruginosa CAU 342A | ? | - |
? | |
| laminarin + H2O | 72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5 | Pseudomonas aeruginosa | ? | - |
? | |
| laminarin + H2O | 72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5 | Pseudomonas aeruginosa CAU 342A | ? | - |
? | |
| additional information | the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose | Pseudomonas aeruginosa | ? | - |
? | |
| additional information | the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose | Pseudomonas aeruginosa CAU 342A | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 79300, calculated from amino acid sequence | Pseudomonas aeruginosa |
| monomer | 1 * 86900, SDS-PAGE | Pseudomonas aeruginosa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bglu50A | - |
Pseudomonas aeruginosa |
| endo-beta-1,3-D-glucanase | - |
Pseudomonas aeruginosa |
| endo-type beta-1,3-glucanase | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Pseudomonas aeruginosa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 50 | the enzyme is almost completely inactivated at 50°C after 30 min. The half-lives of the enzyme at 40, 45, and 50°C are determined to be 872, 83 and 7 min, respectively | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Pseudomonas aeruginosa |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8 | the enzyme retains more than 80% of its maximal activity after incubation at 30°C within pH 4.0-8.0 for 30 min | Pseudomonas aeruginosa |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pseudomonas aeruginosa | calculated from amino acid sequence | - |
5.7 |
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Release 2023.1 (January 2023)
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