EC Number |
Protein Variants |
Reference |
---|
3.4.23.23 | Y75N |
crystallization data |
667045 |
3.4.23.23 | N331Q |
the mutant enzyme is not glycosylated |
-, 752456 |
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/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 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 | 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 | T218A/T218S/L287G |
the mutations lead to a significant decrease in proteolytic activity compared to the wild type enzyme |
755331 |
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 |