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Literature summary extracted from
- Critical factors to high thermostability of an alpha-amylase from hyperthermophilic archaeon Thermococcus onnurineus NA1 (2007), J. Microbiol. Biotechnol., 17, 1242-1248.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | EDTA | 1 mM, 2 ng enzyme, 96% inhibition | Thermococcus onnurineus |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | expression in Escherichia coli | Thermococcus onnurineus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.1 | additional information | - |
starch | soluble starch: Km 4.57 mg/ml | Thermococcus onnurineus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 51948 | - |
x * 51948, calculated from sequence | Thermococcus onnurineus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Thermococcus onnurineus | Q2QC88 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | - |
Thermococcus onnurineus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | amylopectin + H2O | the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7) | Thermococcus onnurineus | ? | - |
? | |
| 3.2.1.1 | maltooligosaccharide + H2O | the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7) | Thermococcus onnurineus | ? | - |
? | |
| 3.2.1.1 | additional information | no hydrolysis of pullulan and cyclodextrin | Thermococcus onnurineus | ? | - |
? | |
| 3.2.1.1 | starch + H2O | the enzyme shows a liquefying activity, hydrolyzing maltooligosaccharides, amylopectin, and starch to produce mainly maltose (G2) to maltoheptaose (G7) | Thermococcus onnurineus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | ? | x * 51948, calculated from sequence | Thermococcus onnurineus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | TO_amyl | - |
Thermococcus onnurineus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 80 | - |
- |
Thermococcus onnurineus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 40 | 80 | less than 20% of maximal activity observed at 40-50°C, 80°C: optimum | Thermococcus onnurineus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 80 | - |
pH 6, half-life: 30 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 7581 min | Thermococcus onnurineus |
| 3.2.1.1 | 90 | - |
at pH 6, half-life: 10 min. Addition of 0.5 mM Ca2+ changes t1/2 at 90°C to 153 min. The thermostability is not enhanced by the addition of Zn2+ or other divalent metals, irrespective of the concentration | Thermococcus onnurineus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 5.5 | 6 | - |
Thermococcus onnurineus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.2.1.1 | Thermococcus onnurineus | - |
- |
4.6 |
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