EC Number   |
Natural Substrates |
|---|
   3.4.21.64 | Bap protein + H2O |
degradation |
| 3.4.21.64 | human sensitive prion protein Sc + H2O |
degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions |
| 3.4.21.64 | Keratin + H2O |
- |
| 3.4.21.64 | more |
segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site |
| 3.4.21.64 | more |
anti-biofilm activity of proteinase K in combination with antibiotics, streptomycin, gentamycin and ampicillin used against bap-positive Sthaphylococcus aureus V329 biofilms. Recovery of Bap, a large, multi-domain, cell surface-anchored Ca2+-dependent protein, which has a crucial role in the early stages of Staphylococcus aureus biofilm development, within 3 h after proteinase K treatment, overview. Binding of Ca2þ to Bap does not confer any immunity against proteolytic degradation |
| 3.4.21.64 | more |
intact Staphylococcus aureus cells, heat-killed Pseudomonas aeruginosa cells, free genomic DNA of Salmonella enterica, and a mixture of these targets are treated by a DNase I/proteinase K mixture, overview |
| 3.4.21.64 | more |
resistant and sensitive prion protein fractions, obtained by limited proteolysis and mass spectrometry, show that both have similar enzyme-cleavage maps and therefore seems to share the same basic architecture. In vivo proteinase K-resistance of prions may not be the rule but the exception |
