3.4.21.64	A199S	no effect on activity	678927	
3.4.21.64	A236V	lethal	678927	
3.4.21.64	E138A	lethal, increased stability of the serine protease subtilisin	678927	
3.4.21.64	G293A	strong positive effect on activity	678927	
3.4.21.64	I132V	positive effect on activity	678927	
3.4.21.64	I310K	no effect on activity, increased stability of the serine protease subtilisin	678927	
3.4.21.64	K208H	positive effect on activity	678927	
3.4.21.64	K332R	positive effect on activity	678927	
3.4.21.64	L180I	positive effect on activity	678927	
3.4.21.64	L299C	lethal, increased stability of the serine protease subtilisin	678927	
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	additional information	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	additional information	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	
3.4.21.64	S123A	positive effect on activity	678927	
3.4.21.64	S273T	positive effect on activity	678927	
3.4.21.64	S337N	positive effect on activity	678927	
3.4.21.64	V167I	no effect on activity	678927	
3.4.21.64	V267I	positive effect on activity	678927	
3.4.21.64	Y151A	strong positive effect on activity	678927	
3.4.21.64	Y194S	no effect on activity, random mutation obtained during synthesis of wild-type proteinase K	678927