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
-
3.4.21.64
-
3.4.21.4
-
chymotrypsin
-
subtilisins
-
alpha-chymotrypsin
-
carlsberg
-
3.1.1.3
-
synthesis
-
degradation
-
beta-trypsin
-
diagnostics
-
analysis
-
pharmacology
-
molecular biology
-
medicine
-
detergent
-
3.4.17.1
-
biotechnology
- 3.4.21.64
-
3.4.21.4
- chymotrypsin
- subtilisins
- alpha-chymotrypsin
-
carlsberg
-
3.1.1.3
- synthesis
- degradation
- beta-trypsin
- diagnostics
- analysis
- pharmacology
- molecular biology
- medicine
- detergent
-
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
ECTree
Advanced search results
Temperature Stability
Temperature Stability on EC 3.4.21.64 - peptidase K
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
16.2 - 80
the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical. Hydrolytic activity of Pr-derivatized proteinase K shows that the hydrolytic activity is 46fold higher at 70°C using synthetic nitroanilide substrate and 9 and 76fold higher at 70°C and 80°C using fluorescein isothiocyanate-labeled casein, respectively, in comparison with the native proteinase K. Furthermore, based on the yield of chemoenzymatic peptide syntheses, the aminolysis activity of Pr-derivatized proteinase K is 3.5 and 9.5fold higher than that of the native proteinase K at 50°C and 60°C, respectively
37
-
30 min, about 90% residual activity even in presence of 1% sodium dodecylsulfate
50
66
-
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66°C
70
additional information
-
30 min, 19% residual activity in presence of 1% sodium dodecylsulfate
-
Ca2+ contributes to the overal stability of the surface regions and improves the thermal stability
additional information
-
depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability