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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

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

Application

Application on EC 3.4.21.64 - peptidase K

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
degradation
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use of enzyme to degrade poly(L-lactide) film. Adsorption of enzyme to film is irreversible, enzyme moves on the surface of substrate to hydrolyze the film around it
detergent
synthesized enzyme-inorganic hybrid nanoflowers (P-hNFs) can potentially be used as an additive in detergent formulations
diagnostics
prion disease diagnosis relies on the relative resistance of sensitive prion protein Sc, PtPSc, to the non-specific protease proteinase K in brain samples to discriminate between resistant and senstive prions, PrPC and PrPSc, in combination with immunological detection of the main enzyme-resistant part of PrPSc (PrP27-30)
medicine
molecular biology
proteinase K from Tritirachium album, which is one of the most widely used proteases in molecular biological studies. The synthesized linear oligo-phenylalanine shows a unique self-assembly in aqueous solutions
pharmacology
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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. Detection of proteinase K-sensitive isoforms of disease-related prion protein using thermolysin should be useful for improving diagnostic sensitivity in human prion diseases
synthesis
chemoenzymatic synthesis of oligo(L-phenylalanine) by the enzyme as a green and clean chemical reaction compared to organic synthesis