3.4.21.64: peptidase K
This is an abbreviated version!
For detailed information about peptidase K, go to the full flat file.
Word Map on EC 3.4.21.64
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3.4.21.64
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3.4.21.4
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chymotrypsin
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subtilisins
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alpha-chymotrypsin
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carlsberg
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3.1.1.3
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synthesis
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degradation
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beta-trypsin
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diagnostics
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analysis
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pharmacology
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molecular biology
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medicine
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detergent
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3.4.17.1
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biotechnology
- 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
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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
3.4.21.64 peptidase KAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.64 - peptidase K
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AAPA + H2O
?
-
molecular dynamics simulations of the proteinase K alone and in complex with the peptide substrate AAPA are performed to investigate the effect of substrate binding on the dynamics/molecular motions of proteinase K
-
-
?
beta-galactosidase + H2O
?
proteinase K activity determination with beta-galactosidase as sensitive macromolecular substrate, comparison of the native protein-attacking ability of free and immobilized proK, method evaluation, overview. beta-Galactosidase is inactivated by proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK
-
-
?
carboxybenzoyl-(Ala)2-Lys methyl ester + H2O
carboxybenzoyl-(Ala)2-Lys + methanol
-
-
-
-
?
carboxybenzoyl-D-Ala-L-Lys methyl ester + H2O
carboxybenzoyl-D-Ala-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-Gly-Lys methyl ester + H2O
carboxybenzoyl-Gly-Lys + methanol
-
-
-
-
?
carboxybenzoyl-L-Ala-L-Lys methyl ester + H2O
carboxybenzoyl-L-Ala-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-L-Lys methyl ester + H2O
carboxybenzoyl-L-Lys + methanol
-
-
-
-
?
carboxybenzoyl-Leu-Lys methyl ester + H2O
carboxybenzoyl-Leu-Lys + methanol
-
-
-
-
?
creatine kinase + H2O
?
Tritirachium album Limber
-
inactivation of rabbit muscle creatine kinase by processing
-
?
Glucose dehydrogenase + H2O
Hydrolyzed glucose dehydrogenase
-
upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments (K-protein, MW 26000 and K-peptide, MW 3000), the cleavage occurs in the C-terminal region of the polypeptide chain.-Leu-Ala-+-Ser-Ser-Glu is proposed as the cleavage site, the term -+- depicts the point of cleavage
upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments (K-protein, MW 26000 and K-peptide, MW 3000), the cleavage occurs in the C-terminal region of the polypeptide chain. Leu-Ala-+-Ser-Ser-Glu is proposed as the cleavage site, the term -+- depicts the point of cleavage
?
human growth hormone + H2O
?
-
proteolytic activity and specificity of PK is maintained after its immobilization to magnetic particles
-
-
?
N-succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + p-nitroaniline
Tritirachium album Limber
-
-
-
?
N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Leu + p-nitroaniline
-
-
-
-
?
N-succinyl-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe + 4-nitroaniline
-
-
-
?
normal cellular prion protein + H2O
pathogenic cellular prion protein + ?
in mouse brain
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
main cleavage sites: Gln4-His5, Ser9-His10, Leu11-Val12, Leu15-Tyr16, Leu17-Val18, Phe24-Phe25, Tyr26-Thr27
main cleavage sites: Gln4-His5, Ser9-His10, Leu11-Val12, Leu15-Tyr16, Leu17-Val18, Phe24-Phe25, Tyr26-Thr27
?
poly(L-lactide) + H2O
?
-
enzyme moves on the surface of substrate film to hydrolyze the film around it
-
-
?
pro-recombinant transglutaminase + H2O
?
-
successful cleavage at the pro-sequence
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
Synthetic peptide substrates + H2O
?
-
primarily specific against aromatic or hydrophobic amino acid residues at the carboxyl side of the splitting point, activity is markedly promoted by elongating the peptide chain to the N-terminal from the splitting point
-
-
?
Urea-denatured hemoglobin + H2O
Hydrolyzed urea-denatured hemoglobin
-
-
-
-
?
human sensitive prion protein Sc + H2O
?
degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions
-
-
?
prion protein + H2O
?
-
for mouse RML prions, the majority of proteinase K-sensitive disease-related prion protein isoforms do not appear to contribute significantly to infectivity. In human variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only 15% of this material resists digestion by proteinase K
-
-
?
prion protein + H2O
?
specific cleavage, that does not occur at cross-linker-modified residues
-
-
?
additional information
?
-
-
the smallest peptide hydrolyzable should be a tetrapeptide, so that the enzyme could be used as an appropriate tool for sequence analysis of medium size peptides
-
-
?
additional information
?
-
-
the combined action of detergent and proteinase K is effective in degrading `masked' proteins in a poly(adenosine diphosphoribose) preparation which cannot be attacked by the proteinase alone
-
-
?
additional information
?
-
-
specificity for peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids
-
-
?
additional information
?
-
-
segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site
-
-
?
additional information
?
-
-
digestion of mouse cell lysates overexpressing prion proteins
-
-
?
additional information
?
-
-
anti-biofilm activity of proteinase K in combination with antibiotics, streptomycin, gentamycin and ampicillin used against bap-positive Sthaphylococcus aureus V329 biofilms. Recovery of Bap, a large, multi-domain, cell surface-anchored Ca2+-dependent protein, which has a crucial role in the early stages of Staphylococcus aureus biofilm development, within 3 h after proteinase K treatment, overview. Binding of Ca2þ to Bap does not confer any immunity against proteolytic degradation
-
-
?
additional information
?
-
intact Staphylococcus aureus cells, heat-killed Pseudomonas aeruginosa cells, free genomic DNA of Salmonella enterica, and a mixture of these targets are treated by a DNase I/proteinase K mixture, overview
-
-
?
additional information
?
-
resistant and sensitive prion protein fractions, obtained by limited proteolysis and mass spectrometry, show that both have similar enzyme-cleavage maps and therefore seems to share the same basic architecture. In vivo proteinase K-resistance of prions may not be the rule but the exception
-
-
?
additional information
?
-
chemoenzymatic synthesis of oligo(L-phenylalanine) mediated by proteinase K from Tritirachium album, the synthesized linear oligo-phenylalanine showed a unique self-assembly in aqueous solutions, overview
-
-
?
additional information
?
-
substrate synthesis: a synthetic gene corresponding to the Syrian hamster prion protein sequence 90-232 with a 23-residue N-terminal fusion tag containing His6 and a thrombin cleavage site (MGSSHHHHHHSSGLVPRGSHMLE) is specifically synthesized and expressedas substrate for the enzyme
-
-
?
additional information
?
-
beta-galactosidase activity is measured spectrophotometrically with 2-nitrophenyl-beta-galactopyranoside. Hen egg lysozyme, horseradish peroxidase, or Aspergillus sp. glucose oxidase are not inactivated by proteinase K
-
-
?
additional information
?
-
the enzyme has a broad substrate specificity. Evaluation of aminolytic activity by polymerization of glutamic acid diethyl ester oligo(glutamic acid ethyl ester)
-
-
?
additional information
?
-
the enzyme has a broad-spectrum degradation capability to degrade proteins
-
-
?
additional information
?
-
Tritirachium album Limber
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exhibits a preference for carboxy groups adjacent to aliphatic and aromatic acids and especially those adjacent to alanine residues
-
?
additional information
?
-
Tritirachium album Limber
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PK is very effective in destroying cellular prion proteins and endogenous proteases present in brain homogenate
-
-
?
