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Literature summary for 3.2.1.1 extracted from
- Bacterial and mold amylases (1971), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 5, 235-271.
No PubMed abstract available
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Bacillus subtilis |
- |
Aspergillus oryzae |
General Stability
| General Stability | Organism |
|---|---|
| pH 7, 20°C, stable against 6 M urea in presence of dialyzable Ca2+. In absence of dialyzable Ca2+, urea at less than 4 M denatures | Aspergillus oryzae |
| stable against denaturation by SDS | Aspergillus oryzae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Bacillus subtilis |  |
| EDTA | - |
Geobacillus stearothermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
- |
Geobacillus stearothermophilus |
| 41000 | - |
approach to equilibium method | Bacillus subtilis |
| 47000 | - |
monomer, equilibrium sedimentation | Bacillus subtilis |
| 48000 | 52700 | equilibrium sedimentation | Geobacillus stearothermophilus |
| 48900 | - |
monomer, sedimentation and diffusion data | Bacillus subtilis |
| 49000 | - |
- |
Geobacillus stearothermophilus |
| 49000 | - |
gel filtration | Aspergillus oryzae |
| 50000 | 51000 | sedimentation and diffusion data | Aspergillus oryzae |
| 52600 | - |
equilibrium sedimentation | Aspergillus oryzae |
| 61000 | - |
acid-stable and acid-unstable enzyme, equilibrium sedimentation | Aspergillus niger |
| 96900 | - |
dimer, sedimentation and diffusion data | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
acid-stable and acid-unstable enzyme | - |
| Aspergillus oryzae | - |
- |
- |
| Bacillus subtilis | - |
- |
- |
| Geobacillus stearothermophilus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | carbohydrate moiety is heterogeneous | Aspergillus oryzae |
| glycoprotein | acid-stable and acid-unstable alpha-amylase contains 24 mol and 7 mol of mannose, and 4 mol and 1 mol of hexosamine per mol protein, respectively | Aspergillus niger |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Bacillus subtilis |
- |
Aspergillus oryzae |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| acid-denatured enzyme is able to regain the intact structure by neutralization, irreversible denaturation after exposure to an alkaline pH , denaturation under high pressure, reduced enzyme in 8 M urea or 6 M guanidine hydrochloride is completely denatured to a randomly coiled state, Ca2+ has a profound effect on the renaturation process | Aspergillus oryzae |
| denaturation under high pressure, enzyme denatured by 8 M urea can refold to regain its activity. Rate and extent of reactivation increases in the presence of various other proteins, bovine serum albumin is most effective | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | - |
Bacillus subtilis | additional information | - |
? | |
| starch + H2O | - |
Geobacillus stearothermophilus | additional information | - |
? | |
| starch + H2O | - |
Aspergillus niger | additional information | - |
? | |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 10.5 | stable | Aspergillus oryzae |
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