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Literature summary for 3.4.21.64 extracted from

  • Tomar, R.; Dubey, V.K.; Jagannadham, M.V.
    Effect of alkyl alcohols on partially unfolded state of proteinase K: Differential stability of alpha-helix and beta-sheet rich regions of the enzyme (2009), Biochimie, 91, 951-960.
    View publication on PubMed

General Stability

General Stability Organism
proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation Parengyodontium album

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Parengyodontium album
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Keratin + H2O Parengyodontium album
-
?
-
?

Organic Solvent Stability

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

Organism UniProt Comment Textmining
Parengyodontium album
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Parengyodontium album ?
-
?
Keratin + H2O
-
Parengyodontium album ?
-
?

Synonyms

Synonyms Comment Organism
endopeptidase K
-
Parengyodontium album
Proteinase K
-
Parengyodontium album

Temperature Stability [°C]

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 Range

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 pH Stability Maximum Comment Organism
2.5
-
the enzyme acquires partially unfolded conformation at pH 2.5 with lower activity Parengyodontium album