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
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3.4.21.4
- chymotrypsin
- subtilisins
- alpha-chymotrypsin
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carlsberg
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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
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Application
Application on EC 3.4.21.64 - peptidase K
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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 CreutzfeldtJakob 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
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protein engineering approach for increasing activity and heat stability of proteinase K. Protein design algorithms that only require the testing of a small number of variants represent a significant step towards a generic, resource-optimized protein engineering process
analysis
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis
analysis
improvement of RNA extraction from papillary cancer-derived K1 cells and thyroid fine-needle aspiration biopsy (FNAB) specimens suspended in liquid-based cytology (LBC) solutions during fine-needle aspiration biopsy diagnostics of thyroid diseases. Commercial proteinase K treatment is essential for efficient RNA extraction from the fixed cells. Proteinase K treatment facilitates RNA recovery from rigid cells after dehydration. RNA molecules are largely released from the fixed cells even after 1-h treatment. U6 small nuclear RNA was detected in these RNA samples by reverse transcription-PCR. Method overview
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proteinase K is successfully applied for the activation of purified pro-recombinant transglutaminase either as free or immobilized enzyme and the free enzyme is also applicable directly in the crude cell extract of Escherichia coli. Proteinase K enables a simple two-step activation/purification procedure resulting in protease-free and almost pure transglutaminase preparations
biotechnology
DNase I and proteinase K eliminate DNA from injured or dead bacteria but not from living bacteria in microbial reference systems and natural drinking water biofilms for subsequent molecular biology analyses, method evaluation, overview
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segment GGG of functionally important N-terminal octapeptide region of human prion protein, involved in spongifirm encephalopathy, strongly binds as a substrate at the substrate recognition site
medicine
Tritirachium album Limber
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PK activity in the presence of brain correlates precisely with the concentration of Cu2+ ions that prevent PK digestion of cellular prion protein and other brain proteins. Apparent resistance of cellular prion protein to proteolysis by PK appears to be directly attributable to the inhibition of PK activity by copper-(II) ions
medicine
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PK magnetic reactor is a useful tool for prion protein digestion
medicine
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proteinase K can be used in combination with antibiotics to enhance the dispersal/control of biofilms