3.4.22.53	C105S	inactive mutant enzyme	644016	
3.4.22.53	C105S	inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium	644028	
3.4.22.53	C105S	mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+	644029	
3.4.22.53	D346E	mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation	696327	
3.4.22.53	D362K	mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation	696327	
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	G423R	mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation	696327	
3.4.22.53	H262A	inactive mutant enzyme	644016	
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	
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	
3.4.22.53	additional information	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	additional information	used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2	696327	
3.4.22.53	N286A	inactive mutant enzyme	644016	
3.4.22.53	N286D	mutant enzyme with low activity	644016	
3.4.22.53	R417W	mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation	696327	
3.4.22.53	R628Q	mutant with decreased enzymatic activity	696327	
3.4.22.53	S369D	inactive mutant enzyme	644047	
3.4.22.53	S50D	mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme	644047	
3.4.22.53	S50E	mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme	644047	
3.4.22.53	S67E	mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme	644047	
3.4.22.53	T344M	mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation	696327	
3.4.22.53	T370E	inactive mutant enzyme	644047	
3.4.22.53	T70E	mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme	644047	
3.4.22.53	W288Y	mutant enzyme with low activity	644016