EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.B55 | D132A |
the purified mature form of the variant enzyme exhibits specific activity similar to that of wild-type enzyme. The heat inactivation profile of the mutant enzyme is similar to that of the wild-type enzyme at 95°C. It retains lower residual activities than that of the wild-type enzyme following incubation with EGTA at 95°C. These data indicate that the mutated residue is involved in calcium binding at the Ca3 site, which is required to stabilize pyrolysin |
752548 |
| 3.4.21.B55 | D132A/D136A |
the purified mature form of the variant enzyme exhibits specific activity similar to that of wild-type enzyme |
752548 |
| 3.4.21.B55 | D132A/N134A |
the purified mature form of the variant enzyme exhibits specific activity similar to that of wild-type enzyme. In the presence of EGTA, the protein quantity of very unstable variants enzyme does not decrease as much as that of the wild-type enzyme following heat treatment at 95°C |
752548 |
| 3.4.21.B55 | D132A/N134A/D136A |
the purified mature form of the variant enzyme exhibits specific activity similar to that of wild-type enzyme |
752548 |
| 3.4.21.B55 | D132N/D136N |
the heat inactivation profile of the mutant enzyme is similar to that of the wild-type enzyme at 95°C. It retains lower residual activities than that of the wild-type enzyme following incubation with EGTA at 95°C. These data indicate that the mutated residue is involved in calcium binding at the Ca3 site, which is required to stabilize pyrolysin |
752548 |
| 3.4.21.B55 | D136A |
the purified mature form of the variant enzyme exhibits specific activity similar to that of wild-type enzyme. The heat inactivation profile of the mutant enzyme is similar to that of the wild-type enzyme at 95°C. It retains lower residual activities than that of the wild-type enzyme following incubation with EGTA at 95°C. These data indicate that the mutated residue is involved in calcium binding at the Ca3 site, which is required to stabilize pyrolysin |
752548 |
| 3.4.21.B55 | D138A/Q139A/E140A/D141A |
the mutant enzyme displays heat resistance similar to that of the WT under nonchelating conditions but exhibits decreased residual activity compared to the wild-type enzyme following incubation with EGTA at 95°C. These results suggest that the residues downstream of motif 1 also contribute to calcium binding at the Ca3 site |
752548 |
| 3.4.21.B55 | D161A |
maturation defective variant |
752548 |
| 3.4.21.B55 | D161A/D163A |
the variant proform is capable of maturation, but the yield of mature enzyme is very low |
752548 |
| 3.4.21.B55 | D161A/D163A/D165A |
maturation defective variant |
752548 |
