3.4.21.64: peptidase K

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

Word Map on EC 3.4.21.64

3.4.21.64

3.4.21.4

chymotrypsin

subtilisins

alpha-chymotrypsin

carlsberg

3.1.1.3

synthesis

degradation

beta-trypsin

diagnostics

analysis

pharmacology

molecular biology

medicine

detergent

3.4.17.1

biotechnology

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]

Activating Compound

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Activating Compound on EC 3.4.21.64 - peptidase K

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acetonitrile

Tritirachium album Limber

653845

spermine

Parengyodontium album

P06873

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. Spermine interacts with proteinase K spontaneously at single binding site

753872

additional information

2 entries