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Literature summary for 3.2.1.132 extracted from
- The hydrogen-bond network around Glu160 contributes to the structural stability of chitosanase CsnA from Renibacterium sp. QD1 (2018), Int. J. Biol. Macromol., 109, 880-887 .
Application
| Application | Comment | Organism |
|---|---|---|
| industry | the enzyme has a great potential for industrial applications due to its high yield and broad pH stability | Renibacterium sp. QD1 |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Renibacterium sp. QD1 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E160A | mutant enzyme with decreased thermal stability and reduced specific activity | Renibacterium sp. QD1 |
| E160Q | mutant enzyme with decreased thermal stability and reduced specific activity | Renibacterium sp. QD1 |
| K163A | mutant enzyme with decreased thermal stability and reduced specific activity | Renibacterium sp. QD1 |
| T114A | mutant enzyme with decreased thermal stability and slightly reduced specific activity | Renibacterium sp. QD1 |
General Stability
| General Stability | Organism |
|---|---|
| the hydrogen-bond network around Glu160 plays important roles in stabilization of the enzyme | Renibacterium sp. QD1 |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 26000 | - |
SDS-PAGE | Renibacterium sp. QD1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Renibacterium sp. QD1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Renibacterium sp. QD1 |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 250.87 | - |
pH 5.6, 55°C, mutant enzyme K163A | Renibacterium sp. QD1 |
| 261.73 | - |
pH 5.6, 55°C, mutant enzyme E160A | Renibacterium sp. QD1 |
| 283.93 | - |
pH 5.6, 55°C, mutant enzyme E160Q | Renibacterium sp. QD1 |
| 328.05 | - |
pH 5.6, 55°C, mutant enzyme T114A | Renibacterium sp. QD1 |
| 335.07 | - |
pH 5.6, 55°C, wild-type enzyme | Renibacterium sp. QD1 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chitosan + H2O | - |
Renibacterium sp. QD1 | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 26000, SDS-PAGE | Renibacterium sp. QD1 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chitosanase CsnA | - |
Renibacterium sp. QD1 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
assay at | Renibacterium sp. QD1 |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35.55 | - |
Tm-value of mutant enzyme E160A | Renibacterium sp. QD1 |
| 36.02 | - |
Tm-value of mutant enzyme E160Q | Renibacterium sp. QD1 |
| 37.36 | - |
Tm-value of mutant enzyme T114A | Renibacterium sp. QD1 |
| 38.86 | - |
Tm-value of mutant enzyme K163A | Renibacterium sp. QD1 |
| 40.36 | - |
Tm-value of wild-type enzyme | Renibacterium sp. QD1 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.6 | - |
assay at | Renibacterium sp. QD1 |
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