EC Number   |
Protein Variants |
Reference |
|---|
    2.5.1.55 | A56P/N57DELTA |
mutation in the absolutely conserved KANRS motif. Complete loss of activity |
721641 |
| 2.5.1.55 | C11A |
mutant enzyme retains less than 1% of the wild-type activity and is incapable of metal binding. Activity is not stimulated by Mn2+, Co2+ and Zn2+. Cd2+ stimulates 2fold at a concentration above 1 mM |
658666 |
| 2.5.1.55 | C11N |
enzyme retains 10% of the wild-type activity in absence of metal ions. Addition of divalent metal ions does not affect the catalytic activity of the mutant enzyme and the catalytic efficiency, i.e. the ratio of turnover number to Km-value, is reduced only 12fold, the mutant enzyme has become metal-independent |
659404 |
| 2.5.1.55 | C11N |
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability |
685148 |
| 2.5.1.55 | C11N/S235P/Q237A |
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability |
685148 |
| 2.5.1.55 | C21N |
complete loss of activity |
721708 |
| 2.5.1.55 | D243A |
mutation of the absolutely conserved 243AspGlyPro245 motif, complete loss of activity |
721708 |
| 2.5.1.55 | D243Q |
mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency |
721708 |
| 2.5.1.55 | F114A |
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis |
737680 |
| 2.5.1.55 | F114R |
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis |
737680 |
