Any feedback?
Literature summary for 3.2.1.1 extracted from
- Role of the calcium-binding residues Asp231, Asp233, and Asp438 in alpha-amylase of Bacillus amyloliquefaciens as revealed by mutational analysis (2010), Curr. Microbiol., 60, 162-166.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D231N | the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH | Bacillus amyloliquefaciens |
| D233N | the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively | Bacillus amyloliquefaciens |
| D438G | the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH | Bacillus amyloliquefaciens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 25.1 | - |
starch | mutant enzyme D233N | Bacillus amyloliquefaciens |  |
| 157 | - |
starch | mutant enzyme D231N | Bacillus amyloliquefaciens | |
| 161.7 | - |
starch | mutant enzyme D438G | Bacillus amyloliquefaciens | |
| 167.6 | - |
starch | wild type enzyme | Bacillus amyloliquefaciens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | the Ca2+-binding residue Asp233 affects significantly the alpha-amylase specific activity | Bacillus amyloliquefaciens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 58000 | - |
SDS-PAGE | Bacillus amyloliquefaciens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | Bacillus amyloliquefaciens | - |
malto-oligosaccharides | - |
? | |
| starch + H2O | Bacillus amyloliquefaciens CICIM B2125 | - |
malto-oligosaccharides | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus amyloliquefaciens | P00692 | - |
- |
| Bacillus amyloliquefaciens CICIM B2125 | P00692 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | - |
Bacillus amyloliquefaciens | malto-oligosaccharides | - |
? | |
| starch + H2O | - |
Bacillus amyloliquefaciens CICIM B2125 | malto-oligosaccharides | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmyQ | - |
Bacillus amyloliquefaciens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 75 | in presence of 5 mM Ca2+, the optimum temperature of AmyQ is between 50 and 75°C | Bacillus amyloliquefaciens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
AmyQ remains stable at 60°C for 30 min | Bacillus amyloliquefaciens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 7 | - |
Bacillus amyloliquefaciens |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9.5 | - |
Bacillus amyloliquefaciens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
