EC Number   |
Protein Variants |
Reference |
|---|
   3.1.1.101 | A180I |
mutation results in more space on the binding center and higher activity than the wild-type enzyme |
750317 |
| 3.1.1.101 | C174S |
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is reduced to less than 5% compared to wild-type value |
-, 751663 |
| 3.1.1.101 | C210S |
production of 4-[(2-hydroxyethoxy)carbonyl]benzoate is is abolished |
-, 751663 |
| 3.1.1.101 | D174C/D253C |
increase in melting temperature in absence and in presence of Ca2+ |
-, 738254 |
| 3.1.1.101 | D177A |
inactive mutant enzyme |
-, 750317 |
| 3.1.1.101 | D204C/E253C |
increase in melting temperature |
-, 738254 |
| 3.1.1.101 | D204C/E253C/D174R |
increase in temperature optimum to 75-80°C, mutant causes a weight loss of PET films of 25.0% at 70 °C after a reaction time of 48 h, compared to 0.3% for wild-type |
-, 738254 |
| 3.1.1.101 | D204R |
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point |
-, 737915 |
| 3.1.1.101 | E253R |
mutation in residue involved in metal ion binding. Increase in melting point by 14 degrees compared to wild-type. Presence of 10 mM CaCl2 does not result in a considerable increase in melting point |
-, 737915 |
| 3.1.1.101 | G62A |
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme. Mutant G62A reveals a 5.5fold lower binding constant to the inhibitor mono-(2-hydroxyethyl) terephthalate than the wild type enzyme |
-, 737899 |
