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Literature summary for 3.2.1.133 extracted from
- Enhancing thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2 by DNA shuffling (2006), FEBS J., 273, 3335-3345.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli MC1061, His-tagged, wild-type and mutant protein | Bacillus thermoalkalophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N147D/F195L/N263S/D311G/A344V/F397S/N508D | mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated | Bacillus thermoalkalophilus |
| N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T | additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown | Bacillus thermoalkalophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | Bacillus thermoalkalophilus | - |
alpha-maltose + ? | - |
? |  |
| starch + H2O | Bacillus thermoalkalophilus ET2 | - |
alpha-maltose + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thermoalkalophilus | Q68KL3 | - |
- |
| Bacillus thermoalkalophilus ET2 | Q68KL3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type and mutant enzymes | Bacillus thermoalkalophilus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
kinetic properties determined in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling | Bacillus thermoalkalophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-cyclodextrin + H2O | main product alpha-maltose | Bacillus thermoalkalophilus | alpha-maltose + ? | - |
? | |
| beta-cyclodextrin + H2O | main product alpha-maltose | Bacillus thermoalkalophilus ET2 | alpha-maltose + ? | - |
? | |
| pullulan + H2O | main product panose | Bacillus thermoalkalophilus | panose + ? | - |
? | |
| pullulan + H2O | main product panose | Bacillus thermoalkalophilus ET2 | panose + ? | - |
? | |
| starch + H2O | - |
Bacillus thermoalkalophilus | alpha-maltose + ? | - |
? | |
| starch + H2O | - |
Bacillus thermoalkalophilus ET2 | alpha-maltose + ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BTMA | - |
Bacillus thermoalkalophilus |
| glucan 1,4-alpha-maltohydrolase | - |
Bacillus thermoalkalophilus |
| maltogenic amylase | - |
Bacillus thermoalkalophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
wild-type enzyme | Bacillus thermoalkalophilus |
| 80 | - |
mutants III-1 and III-2 | Bacillus thermoalkalophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
half-lives determined at 75°C, 78°C, 80°C, and 85°C, melting temperatures of mutants III-1 and III-2 determined by differential scanning calorimetry increased by 6.1°C and 11.4°C, respectively, hydrogen bonding, hydrophobic interaction, electrostatic interaction, proper packing, and deamidation predicted as mechanisms for enhanced thermostability in the mutant enzymes | Bacillus thermoalkalophilus |
| 78 | - |
half-life of mutant III-1 about 20 times greater than half-life of the wild-type at 78°C | Bacillus thermoalkalophilus |
| 80 | - |
half-life of mutant III-2 is 568 min, half-life of the wild-type is below 1 min at 80°C | Bacillus thermoalkalophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
thermostability tested at | Bacillus thermoalkalophilus |
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