3.4.21.B48	D164	the mutant shows about 1.3% activity compared to the wild type enzyme	718028	
3.4.21.B48	D164A	inactive	718028	
3.4.21.B48	D164A	site-directed mutagenesis, no autoactivation of the proform, inactive mutant	-, 665094	
3.4.21.B48	D164N	site-directed mutagenesis, replacement of the catalytic residue of kumamolisin-As with that of subtilisin, disrupted interaction of Ser278 with residue 164, the mutant shows 1.3% of the wild-type turnover	-, 664913	
3.4.21.B48	D316A	site-directed mutagenesis, autoactivation similar to the wild-type enzyme, 3% of wild-type enzyme activity	-, 665094	
3.4.21.B48	D82A	site-directed mutagenesis, no autoactivation of the proform, inactive mutant	-, 665094	
3.4.21.B48	E32A	the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 5.7% of the native enzyme	-, 653914	
3.4.21.B48	E78A	site-directed mutagenesis, no autoactivation of the proform, inactive mutant	-, 665094	
3.4.21.B48	E78A/D164N	site-directed mutagenesis, completely inactive mutant which stays unprocessed	-, 664913	
3.4.21.B48	E78H	0.01% activity compared to wild-type enzyme, the canonical catalytic triad is disrupted	-, 652534	
3.4.21.B48	E78H/D164N	site-directed mutagenesis, replacement of the catalytic residues of kumamolisin-As with those of subtilisin, disruption of the catalytic triad, the mutant shows 0.0001% of the wild-type turnover	-, 664913	
3.4.21.B48	E78Q/D164N	site-directed mutagenesis, completely inactive mutant which stays unprocessed	-, 664913	
3.4.21.B48	additional information	mutational analysis of the Ser278 residue reveals that the mutant loses both auto-processing activity and proteolytic activity	-, 651795	
3.4.21.B48	S278A	an inactive pro-kumamolisin mutant, the catalytic domain of the mutant exhibits a virtually identical structure compared to the active enzyme	-, 731647	
3.4.21.B48	S278A	site-directed mutagenesis, no autoactivation of the proform, inactive mutant	-, 665094	
3.4.21.B48	S278A	the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitzo)Phe-Arg-Leu is reduced to 0.5% of the native enzyme	-, 653914	
3.4.21.B48	W129A	the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 3.8% of the native enzyme	-, 653914