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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.64 peptidase K

Temperature Stability

Temperature Stability on EC 3.4.21.64 - peptidase K

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
46
-
15 min, 50% loss of activity of Ca2+-free enzyme
60
-
retains 83% activity after 2 h
65
-
15 min, 50% loss of activity of Ca2+-saturated enzyme
66
-
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66°C
additional information