EC Number   |
Protein Variants |
Reference |
|---|
    3.6.1.5 | A75S |
the Km value for ADP of the isoform APY2 mutant is decreased compared to the wild type enzyme, while the Km value for ATP is substantially increased. The mutant shows higher specific acitivity for ADP than ATP |
734982 |
| 3.6.1.5 | C10S |
112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation |
656106 |
| 3.6.1.5 | C10S/C501S |
148% of wild-type ATPase activity, 133% of wild-type ADPase activity |
656106 |
| 3.6.1.5 | C10S/C501S/C509S |
79% of wild-type ATPase activity, 77% of wild-type ADPase activity |
656106 |
| 3.6.1.5 | C10S/C509S |
103% of wild-type ATPase activity, 99% of wild-type ADPase activity |
656106 |
| 3.6.1.5 | C501S |
130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid |
656106 |
| 3.6.1.5 | C501S/C509S |
138% of wild-type ATPase activity, 134% of wild-type ADPase activity |
656106 |
| 3.6.1.5 | C509S |
148% of wild-type ATPase activity, 155% of wild-type ADPase activity |
656106 |
| 3.6.1.5 | D209A |
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme |
720736 |
| 3.6.1.5 | E159A |
site-directed mutagenesis, inactive mutant |
698747 |
