Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | presence of calcium ions, up to 10 mM, has no effect on enzymatic activity | Tritirachium album Limber |
Application | Comment | Organism |
---|---|---|
medicine | PK activity in the presence of brain correlates precisely with the concentration of Cu2+ ions that prevent PK digestion of cellular prion protein and other brain proteins. Apparent resistance of cellular prion protein to proteolysis by PK appears to be directly attributable to the inhibition of PK activity by copper-(II) ions | Tritirachium album Limber |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | at equilibrium two to three copper ions bind stoichiometrically to PK and destroy its activity. Initial reversible and weak binding phase and a slower, irreversible abolition of activity with a half-time of 6 min at saturating copper ion concentrations. PK digestion of cellular prion proteins and other proteins in brain homogenate is inhibited in a concentration-dependent manner at concentrations of more than 1 mM. Presence of calcium ions, up to 10 mM, has no effect on copper inhibition | Tritirachium album Limber | |
additional information | not inhibited by Zn2+ or Mn2+ | Tritirachium album Limber |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Tritirachium album Limber | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | PK is very effective in destroying cellular prion proteins and endogenous proteases present in brain homogenate | Tritirachium album Limber | ? | - |
? | |
p-nitrophenyl acetate + H2O | - |
Tritirachium album Limber | p-nitrophenol + acetate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Proteinase K | - |
Tritirachium album Limber |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.7 | 7.4 | - |
Tritirachium album Limber |