3.4.21.64: peptidase K
This is an abbreviated version!
For detailed information about peptidase K, go to the full flat file.
Word Map on EC 3.4.21.64
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3.4.21.64
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3.4.21.4
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chymotrypsin
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subtilisins
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alpha-chymotrypsin
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carlsberg
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3.1.1.3
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synthesis
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degradation
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beta-trypsin
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diagnostics
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analysis
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pharmacology
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molecular biology
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medicine
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detergent
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3.4.17.1
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biotechnology
- 3.4.21.64
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3.4.21.4
- chymotrypsin
- subtilisins
- alpha-chymotrypsin
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carlsberg
-
3.1.1.3
- synthesis
- degradation
- beta-trypsin
- diagnostics
- analysis
- pharmacology
- molecular biology
- medicine
- detergent
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3.4.17.1
- biotechnology
Reaction
Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides =
Synonyms
EC 3.4.21.14, EC 3.4.21.4, EC 3.4.4.16, endopeptidase K, mesophilic proteinase K, PROK, Proteinase K, Proteinase, Tritirachium album serine, Tritirachium album proteinase K, Tritirachium alkaline proteinase
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3.4.21.64 peptidase KAdvanced search results
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Engineering on EC 3.4.21.64 - peptidase K
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
I310K
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no effect on activity, increased stability of the serine protease subtilisin
M145F
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no effect on activity, increased stability of the serine protease subtilisin
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
P265S
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no effect on activity, increased stability of the serine protease subtilisin
P355S
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no effect on activity, increased stability of the serine protease subtilisin
Y194S
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no effect on activity, random mutation obtained during synthesis of wild-type proteinase K
additional information
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
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
