3.4.21.64: peptidase K

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For detailed information about peptidase K, go to the full flat file.

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

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Results	in table
4	Activating Compound
9	AA Sequence
15	Application
1	CAS Registry Number
4	Cloned(Commentary)
21	Crystallization (Commentary)
16	Disease/ Diagnostics
11	General Information
6	General Stability
41	Inhibitors
28	KM Value [mM]
3	Localization
23	Metals/Ions
5	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
70	Organism
233	PDB ID
13	pH Optimum
4	pH Range
3	pH Stability
1	pI Value
1	Posttranslational Modification
27	Protein Variants
6	Purification (Commentary)
1	Reaction
1	Reaction Type
70	Reference
28	Source Tissue
4	Specific Activity [micromol/min/mg]
1	Storage Stability
75	Substrates and Products (Substrate)
5	Subunits
48	Synonyms
11	Temperature Optimum [°C]
2	Temperature Range [°C]
12	Temperature Stability [°C]
6	Turnover Number [1/s]

General Stability

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General Stability on EC 3.4.21.64 - peptidase K

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

Depletion of Ca2+ increases the rate of autolysis after about 48 h, it reduces the thermal stability and enhances the deactivation by 8 M urea

Parengyodontium album

-

29510

interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation

Parengyodontium album

P06873

753872

proteinase K is losing the proteolytic activity as the enzyme is attaining beta conformation

Parengyodontium album

-

707588

Relatively resistant to SDS, 0.2% in 50 mM Tris/HCl, pH 7.4

Parengyodontium album

-

29508

Relatively stable towards heat and denaturing agents

Parengyodontium album

-

29501

Urea, 4 M, stable

Parengyodontium album

-

29508