lysyl endopeptidase

This is an abbreviated version, for detailed information about lysyl endopeptidase, go to the full flat file.


Preferential cleavage: Lys-/-, including -Lys-/-Pro- =


Achrombacter protease I, Achromobacter lysyl endopeptidase, Achromobacter protease I, Achromobacter proteinase I, achromopeptidase, API, caseinase, endo-Lys-C protease, endopeptidase Lys-C, endoproteinase, endoproteinase Lys-C, KGP, LEP, Lys-C, Lys-C endoproteinase, Lys-specific serine endopeptidase, lysine endoproteinase, lysine specific gingipain, lysine specific protease, lysine specific proteinase, lysine-specific protease, Lysobacter lysyl endoproteinase, lysyl bond specific proteinase, Lysyl endopeptidase, protease I, protease IV, proteinase, Achromobacter lyticus alkaline I, proteinase, lysine specific, proteinase, Pseudomonas lyticus alkaline , I, Ps-1, Pseudomonas aeruginosa lysine -specific protease


     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
       lysyl endopeptidase


Crystallization on EC - lysyl endopeptidase

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mutants H210S and W169F, to 2.0 and 2.3 A resolution, respectively
neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A
purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 0.001 ml of protein with reservoir solution containing 27% PEG 4000, 100 mM sodium acetate, pH 5.0, and 0.2 M ammonium sulfate, equilibration over 0.5 ml of reservoir solution, one week, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement/heavy atom derivatization