EC Number |
Protein Variants |
Reference |
---|
3.4.22.53 | K226S |
Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme |
644019 |
3.4.22.53 | K230E |
Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme |
644019 |
3.4.22.53 | K230E |
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme |
644019 |
3.4.22.53 | K230S |
Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme |
644019 |
3.4.22.53 | K230S |
mutation has no significant effect on specific activity |
644019 |
3.4.22.53 | K234E |
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme |
644019 |
3.4.22.53 | K234S |
Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme |
644019 |
3.4.22.53 | K234S |
mutation decreases specific activity to 81% compared to wild-type enzyme |
644019 |
3.4.22.53 | K234W |
Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme |
644019 |
3.4.22.53 | K390R |
overexpression of K390R mutant fails to increase the calpain activity since sumoylation at K390 is important for calpain-2 activity |
707365 |