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Literature summary for 3.2.1.1 extracted from
- Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics (2005), J. Biol. Chem., 280, 37360-37365.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamics and kinetics | Bacillus subtilis | |
| additional information | - |
additional information | thermodynamics and kinetics | Sus scrofa | |
| additional information | - |
additional information | thermodynamics and kinetics | Bacillus licheniformis | |
| additional information | - |
additional information | thermodynamics and kinetics | Bacillus amyloliquefaciens | |
| additional information | - |
additional information | thermodynamics and kinetics | Aspergillus oryzae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | increases the thermostability of the enzyme, five Ca2+ ions per enzyme molecule | Bacillus licheniformis |  |
| Ca2+ | increases the thermostability of the enzyme, four Ca2+ ions per enzyme molecule | Bacillus amyloliquefaciens | |
| Ca2+ | increases the thermostability of the enzyme, one Ca2+ ion per enzyme molecule | Sus scrofa | |
| Ca2+ | increases the thermostability of the enzyme, three Ca2+ ions per enzyme molecule | Bacillus subtilis | |
| Ca2+ | increases the thermostability of the enzyme, two Ca2+ ions per enzyme molecule | Aspergillus oryzae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
| Bacillus amyloliquefaciens | - |
- |
- |
| Bacillus licheniformis | - |
- |
- |
| Bacillus subtilis | - |
- |
- |
| Sus scrofa | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Bacillus subtilis | - |
| commercial preparation | - |
Bacillus licheniformis | - |
| commercial preparation | - |
Bacillus amyloliquefaciens | - |
| commercial preparation | - |
Aspergillus oryzae | - |
| commercial preparation | pancreatic alpha-amylase | Sus scrofa | - |
| pancreas | - |
Sus scrofa | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme | Bacillus subtilis |
| additional information | - |
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme | Sus scrofa |
| additional information | - |
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme | Bacillus licheniformis |
| additional information | - |
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme | Bacillus amyloliquefaciens |
| additional information | - |
analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme | Aspergillus oryzae |
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