3.4.23.23	A101T	the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme	754970	
3.4.23.23	A101T/G186D	the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme	754970	
3.4.23.23	E13A	the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme	754970	
3.4.23.23	E13D	the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme	754970	
3.4.23.23	E13P	the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme	754970	
3.4.23.23	E13Q	the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme	754970	
3.4.23.23	G186D	the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme	754970	
3.4.23.23	G186D/E13D	the mutant shows a significant milk-clotting activity. The mutant rennet can decrease hydrolysis of protein during ripening of cheese. The mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity	754970	
3.4.23.23	G186D/E13Q	the mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity	754970	
3.4.23.23	G186D/E13Q	the mutant shows a significant milk-clotting activity. The mutant rennet can decrease hydrolysis of protein during ripening of cheese. The mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity	754970	
3.4.23.23	L287G	the mutant shows an increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme	755331	
3.4.23.23	N331Q	the mutant enzyme is not glycosylated	-, 752456	
3.4.23.23	T218A/T218S/L287G	the mutations lead to a significant decrease in proteolytic activity compared to the wild type enzyme	755331	
3.4.23.23	T218S	the mutation causes a low thermostability and moderate increase in the clotting activity compared to the wild type enzyme. The mutant shows a 3.34fold increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme. The mutant can serve as a promising milk coagulant that contributes to an optimal flavor development in mature cheese	755331	
3.4.23.23	Y75N	crystallization data	667045