General Stability | Organism |
---|---|
proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation | Parengyodontium album |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Parengyodontium album | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Keratin + H2O | Parengyodontium album | - |
? | - |
? |
Organic Solvent | Comment | Organism |
---|---|---|
isopropanol | at 40% (v/v) isopropanol nearly half and at 50% (v/v) isopropanol all the tertiary structure is lost, beyond 30% (v/v) isopropanol there is some perturbation in the secondary structure of the protein | Parengyodontium album |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Parengyodontium album | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein + H2O | - |
Parengyodontium album | ? | - |
? | |
Keratin + H2O | - |
Parengyodontium album | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
endopeptidase K | - |
Parengyodontium album |
Proteinase K | - |
Parengyodontium album |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
66 | - |
thermal unfolding is cooperative at pH 7.0 with transition midpoint of 66°C | Parengyodontium album |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 7 | proteinase K maintains structural integrity in the range of pH 3.0-7.0 | Parengyodontium album |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
2.5 | - |
the enzyme acquires partially unfolded conformation at pH 2.5 with lower activity | Parengyodontium album |