EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.133 | expressed in Escherichia coli MC1061, His-tagged, wild-type and mutant protein | Bacillus thermoalkalophilus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.133 | 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 |
3.2.1.133 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.133 | starch + H2O | Bacillus thermoalkalophilus | - |
alpha-maltose + ? | - |
? | |
3.2.1.133 | starch + H2O | Bacillus thermoalkalophilus ET2 | - |
alpha-maltose + ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.133 | Bacillus thermoalkalophilus | Q68KL3 | - |
- |
3.2.1.133 | Bacillus thermoalkalophilus ET2 | Q68KL3 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.133 | wild-type and mutant enzymes | Bacillus thermoalkalophilus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.133 | beta-cyclodextrin + H2O | main product alpha-maltose | Bacillus thermoalkalophilus | alpha-maltose + ? | - |
? | |
3.2.1.133 | beta-cyclodextrin + H2O | main product alpha-maltose | Bacillus thermoalkalophilus ET2 | alpha-maltose + ? | - |
? | |
3.2.1.133 | pullulan + H2O | main product panose | Bacillus thermoalkalophilus | panose + ? | - |
? | |
3.2.1.133 | pullulan + H2O | main product panose | Bacillus thermoalkalophilus ET2 | panose + ? | - |
? | |
3.2.1.133 | starch + H2O | - |
Bacillus thermoalkalophilus | alpha-maltose + ? | - |
? | |
3.2.1.133 | starch + H2O | - |
Bacillus thermoalkalophilus ET2 | alpha-maltose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.133 | BTMA | - |
Bacillus thermoalkalophilus |
3.2.1.133 | glucan 1,4-alpha-maltohydrolase | - |
Bacillus thermoalkalophilus |
3.2.1.133 | maltogenic amylase | - |
Bacillus thermoalkalophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 70 | - |
wild-type enzyme | Bacillus thermoalkalophilus |
3.2.1.133 | 80 | - |
mutants III-1 and III-2 | Bacillus thermoalkalophilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 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 |
3.2.1.133 | 78 | - |
half-life of mutant III-1 about 20 times greater than half-life of the wild-type at 78°C | Bacillus thermoalkalophilus |
3.2.1.133 | 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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 8 | - |
thermostability tested at | Bacillus thermoalkalophilus |