EC Number   |
Protein Variants |
Reference  |
|---|
   3.4.21.B48 | more |
mutational analysis of the Ser278 residue reveals that the mutant loses both auto-processing activity and proteolytic activity |
-, 651795 |
| 3.4.21.B48 | E78H |
0.01% activity compared to wild-type enzyme, the canonical catalytic triad is disrupted |
-, 652534 |
| 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 | 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 |
| 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 | E78A/D164N |
site-directed mutagenesis, completely inactive mutant which stays unprocessed |
-, 664913 |
| 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 | D164A |
site-directed mutagenesis, no autoactivation of the proform, inactive mutant |
-, 665094 |
