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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Natural Substrates Products on EC 3.4.21.64 - peptidase K
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REACTION DIAGRAM
human sensitive prion protein Sc + H2O
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degradation, pathogenic isoform, sensitive prion protein complexes show higher molecular weight than resistant prions
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segment GGG of human prion protein strongly binds as a substrate at the substrate recognition site
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additional information
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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
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additional information
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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
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additional information
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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
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