EC Number   |
Protein Variants |
Reference  |
|---|
   3.4.22.53 | more |
replacement of the five m-calpain residues 517-521, Glu-Ala-Asn-Ile-Glu by the corresponding six mu-calpain residues 528-533, Gln-Ala-Asn-Leu-Pro-Asp, replacement of three m-calpain residues 639-641, Pro-Cys-Gln, by the corresponding three mu-calpain residues 651-653, Asn-Lys-Lys, or replacement of two m-calpain residues 578-579, Lys-Ile by the corresponding mu-calpain residues 590-591, Arg-Ser. Mutations do not affect the expression and Kd values of the resultant calpains. In a series of hybrid mu/m large-subunit calpains, the Kd values decrease progressively towards that of mu-calpain as the portion of mu-type sequence increases from 0 to 90% |
643968 |
| 3.4.22.53 | C105S |
inactive mutant enzyme |
644016 |
| 3.4.22.53 | H262A |
inactive mutant enzyme |
644016 |
| 3.4.22.53 | N286A |
inactive mutant enzyme |
644016 |
| 3.4.22.53 | N286D |
mutant enzyme with low activity |
644016 |
| 3.4.22.53 | W288Y |
mutant enzyme with low activity |
644016 |
| 3.4.22.53 | E504S |
Ca2+ concentration required for half-maximal activity is 0.129 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 | E504S |
mutation decreases specific activity to 90% compared to wild-type enzyme |
644019 |
| 3.4.22.53 | K225S |
mutation decreases specific activity to 88% compared to wild-type enzyme |
644019 |
| 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 |
