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Literature summary for 3.2.1.78 extracted from
- Modular hyperthermostable bacterial endo-beta-1,4-mannanase: molecular shape, flexibility and temperature-dependent conformational changes (2014), PLoS ONE, 9, e92996.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged full-length enzyme and catalytic domain | Thermotoga petrophila |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged full-length enzyme and catalytic domain, X-ray diffraction structure determination and analysis by dynamic light scattering and small-angle X-ray scattering. molecular modelling | Thermotoga petrophila |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga petrophila | A5IMX7 | isolated from the Kubiki oil reservoir in Niigata (Japan) | - |
| Thermotoga petrophila RKU-1 | A5IMX7 | isolated from the Kubiki oil reservoir in Niigata (Japan) | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged full-length enzyme and catalytic domain by nickel affinity chromatography | Thermotoga petrophila |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | the temperature range for growth is 47-88°C with an optimum at 80°C | Thermotoga petrophila | - |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview | Thermotoga petrophila |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Beta-mannanase | - |
Thermotoga petrophila |
| endo-beta-1,4-mannanase | - |
Thermotoga petrophila |
| TpMan | - |
Thermotoga petrophila |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 81 | 93 | - |
Thermotoga petrophila |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 100 | activity range, profile overview | Thermotoga petrophila |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
pH 6.0, the full-length enzyme is completely stable, while the isolated catalytic domain starts to precipitate | Thermotoga petrophila |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 6.5 | - |
Thermotoga petrophila |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6 | Thermotoga petrophila |
| physiological function | the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends | Thermotoga petrophila |
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Release 2023.1 (January 2023)
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