EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.64 | M145F |
no effect on activity, increased stability of the serine protease subtilisin |
678927 |
| 3.4.21.64 | molecular biology |
proteinase K is widely used in molecular biology for its broad substrate specificity, wide pH stability, and high hydrolysis activity. Aminolysis by proteinase K is also attractive for chemoenzymatic peptide synthesis |
752347 |
| 3.4.21.64 | more |
immobilization of the enzyme proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK |
752470 |
| 3.4.21.64 | more |
proteinase K and Cu2+ ions are used to synthesize enzyme-inorganic hybrid nanoflowers (P-hNFs), method overview. The proteolytic activities and some important characteristics such as optimum pH and temperature of the P-hNFs are also evaluated by comparison with free proteinase K. Optimum pH values of free proteinase K and P-hNFs are determined as pH 10.0 and pH 11.0, respectively. Optimum temperatures recorded for both free proteinase K (at pH 10) and P-hNFs (at pH 11) are 40°C. The P-hNFs exhibit better activity than free proteinase K in the presence of all surfactants, i.e. CHAPS, DOC, SDS, Triton X-100 and Tergitol, except for Tween 80. Importantly, the P-hNFs is more stable and compatible with all tested solid laundry detergents. The P-hNFs can potentially be used as an additive in detergent formulations |
753849 |
| 3.4.21.64 | N95C |
lethal, increased stability of the serine protease subtilisin |
678927 |
| 3.4.21.64 | P265S |
no effect on activity, increased stability of the serine protease subtilisin |
678927 |
| 3.4.21.64 | P355S |
no effect on activity, increased stability of the serine protease subtilisin |
678927 |
| 3.4.21.64 | P97S |
lethal, increased stability of the serine protease subtilisin |
678927 |
| 3.4.21.64 | R237N |
no effect on activity |
678927 |
| 3.4.21.64 | S107D |
no effect on activity |
678927 |
