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