EC Number   |
Protein Variants |
Reference |
|---|
   3.4.23.1 | D215E |
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 65°C compared to 71°C for wild-type enzyme. The pH activity profiles of wild-type and mutant pepsin is similar. Mutant enzyme has a stronger affinity for the synthetic substrate KPAEFF(NO2)AL. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is 1.9fold lower than wild-type value |
679555 |
| 3.4.23.1 | D32E |
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 63°C compared to 71°C for wild-type enzyme. Pronounced decrease in activity below pH 2.5. Mutant enzyme has a stronger affinity for the synthetic substrate KPAEFF(NO2)AL. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is 8.7fold lower than wild-type value |
679555 |
| 3.4.23.1 | D32E/D215E |
unlike wild-type, the mutant fusion protein is incapable of autocatalytic activation upon acidification of the medium, as determined by Western blot analysis. Mature mutant pepsin is obtained by processing fusion protein samples through an immobilized pepsin column. Tm-value of mutant enzyme is 63°C compared to 71°C for wild-type enzyme. The pH activity profiles of wild-type and mutant pepsin is similar. KM-value for KPAEFF(NO2)AL is not significantly different relative to wild-type. Turnover number for mutant enzyme is significantly lower than that of the wild-type. kcat/Km is fold lower than wild-type value. kcat/Km is 13.3fold lower than wild-type value |
679555 |
| 3.4.23.1 | D37A |
inactive |
755425 |
| 3.4.23.1 | D37A |
the mutant is completely inactive towards the fluorogenic substrate Mca-KKPAEFFALK-Dnp at pH 4.0 |
717595 |
| 3.4.23.1 | DELTA240-246/+GD |
inactivation rate at pH 7.0 is 86% of that of the wild-type value. The Km-value for KPAEFF(NO2)AL is 2fold higher than that of the wild-type enzyme. The KM-value for LSF(NO2)-Nle-AL as substrate is 79% of the wild-type value |
653708 |
| 3.4.23.1 | E244N/V246T |
introduction of N-glycosylation site. Glycosylated mutant shows similar KM-value and substrate specificity as wild-type, but reduced catalytic efficiency |
668748 |
| 3.4.23.1 | E287M |
the ratio of turnover number to KM-value for KPILF(NO2)RL is 2.2fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 1.3fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 1.6fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 60% of that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 90% of that of the wild-type enzyme |
653827 |
| 3.4.23.1 | F111T/L112F |
the ratio of turnover number to KM-value for KPILF(NO2)RL is 3.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 1.9fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 2.3fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 1.7fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 2.9fold higher than that of the wild-type enzyme. Mutant enzyme cleaves SGGYDLSFLPQPPQE at one site Leu-Ser, compared to three sites cleaved by the wild-type enzyme, and at a rate 23fold higher than that of the wild-type enzyme |
653827 |
| 3.4.23.1 | F111T/L112F/E287M |
the ratio of turnover number to KM-value for KPILF(NO2)RL is 5.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIEF(NO2)RL is 2.8fold higher than that of the wild-type enzyme,the ratio of turnover number to KM-value for KPIQF(NO2)RL is 2.8fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPIKF(NO2)RL is 1.1fold higher than that of the wild-type enzyme, the ratio of turnover number to KM-value for KPPEF(NO2)RL is 3.7fold higher than that of the wild-type enzyme |
653827 |
