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Literature summary extracted from
- Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila (2010), Biochem. Biophys. Res. Commun., 399, 505-511.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.99 | expressed in Escherichia coli BL21 cells | Thermotoga petrophila |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 49000 | - |
1 * 49000, small angle X-ray scattering | Thermotoga petrophila |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.99 | Thermotoga petrophila | A5IKD4 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.99 | Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration | Thermotoga petrophila |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 152.1 | - |
purified protein, using L-arabinan as substrate, at pH 6.0 and 70°C | Thermotoga petrophila |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.99 | (1->5)-L-alphaarabinan + H2O | - |
Thermotoga petrophila | (1->5)-L-arabinooligosaccharides | - |
? |  |
| 3.2.1.99 | additional information | the enzyme acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan | Thermotoga petrophila | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.99 | monomer | 1 * 49000, small angle X-ray scattering | Thermotoga petrophila |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.99 | ABNA | - |
Thermotoga petrophila |
| 3.2.1.99 | endo-1,5-alpha-L-arabinanase | - |
Thermotoga petrophila |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 73 | - |
- |
Thermotoga petrophila |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 62 | 80 | the enzyme shows relative activity ranging from 77% to 78% at temperatures of 62°C and 80°C, respectively | Thermotoga petrophila |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 90 | 95 | the enzyme is fully heat-stable (up to 10 h) and retains activity at temperatures up to 90°C. The enzyme loses its activity only after 90 min when incubated at 95°C | Thermotoga petrophila |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 6 | - |
- |
Thermotoga petrophila |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.99 | 4 | 7 | the enzyme retains more than 75% activity over a pH range from 4.0 to 7.0 | Thermotoga petrophila |
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Release 2023.1 (January 2023)
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