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
ECTree
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Crystallization
Crystallization on EC 3.4.21.64 - peptidase K
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computer modeling studies indicates the presence of a small binding pocket in the vicinity of the proteinase K active site, which may be filled by the aromatic phenylalanine moiety
crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor
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Langmuir-Blodgett nanotemplate method and hanging drop vapor diffusion method, using 400 mM Na/K-tartrate in 25 mM HEPES pH 7.0
mercury-inhibited protein in presence of synthetic peptides GGGWGQPH and HGGGW, derived from N-terminal domain of human prion protein. Segment GGG is strongly bound as a substrate at the substrate recognition site
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purified enzyme, oil microbatch method, mixing of 0.001 ml of 40 mg/ml protein solution in 50 mM MES-NaOH, pH 6.5, with 0.001 ml of precipitant solution composed of 250 mM NaNO3, 50 mM CaCl2, and 50 mM MES-NaOH, pH 6.5, to form Pr3+-derivatized crystals, the precipitant solution containing additionally 25 mM PrCl3 is used, X-ray diffraction structure determination and analysis at 1.45 A resolution
structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2 A resolution, N-acetyl-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2
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the crystallization of proteinase K using PEG 8000 is performed at various degrees of solvent deuteration and X-ray crystallographic analysis at 1.1 A resolution confirms that deuteration has no effect on crystal quality or crystal structure in this case
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three-dimensional structure of the complex of proteinase K with its naturally occuring protein inhibitor, PKI3
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to 1.32 A resolution. final model contains two Ca2+ ions, a molecule of digalacturonic acid and a partially occupied HEPES molecule. The digalacturonic acid molecule has one sugar moiety disposed exactly on a crystallographic twofold axis and is bound through hydrogen-bonding networks involving residue S150 and water molecules
X-ray crystal structure at 1.5 A resolution shows that it has 2 binding sites for Ca2+
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