EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.133 | EDTA | increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L | Thermus sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.133 | R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L | mutant enzyme shows highly improved thermostability and catalytic activity in presence of Ca2+ | Thermus sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.133 | Ca2+ | mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L shows highly improved thermostability and catalytic activity in presence of Ca2+. | Thermus sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.133 | Thermus sp. | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.133 | - |
Thermus sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.133 | beta-cyclodextrin + H2O | - |
Thermus sp. | maltose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.133 | maltogenic amylase | - |
Thermus sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 70 | - |
mutant R26Q/S169N/I333V/A398V/Q411L/P453L | Thermus sp. |
3.2.1.133 | 75 | - |
mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L | Thermus sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.133 | 82 | - |
Tm-value of mutant R26Q/S169N/I333V/A398V/Q411L/P453L is 81.5°C | Thermus sp. |
3.2.1.133 | 85 | - |
Tm-value of mutant enzyme R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L, Tm-value decreases to 79.9°C in presence of EDTA. Tm-value increases to 87.4°C in presence of CaCl2 | Thermus sp. |