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EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.20malfunction mutants with extended S1' binding pocket show specificity towards arginine in subsites S2'-S4' compared to the wild-type protease resulting from the additional negative charge which attract and interact with positively charged residues better than the wild-type. The strict lysine specificity at P1' is preserved in the recombinant rAm-LysN. Relative specificity of site-directed mutants in the substrate binding sites of rAm-LysN compared to the wild-type enzyme with the reference peptide SAQKMVS, overview 754029
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.20more identification of catalytic residues (Y85, E120, H123, T130, D132, Y135, G136, and D156) and mechanism of work, overview. The S1' binding pocket of LysN is quite narrow and lined with negative charge to specifically accommodate lysine. Residues M65, D83, V88, A101, T105, Q131, Q137, and E159 are involved in substrate specificity. Homology model of Am-LysN based on the crystal structure of Gf-LysN, molecular dynamic simulations, proposed subsite interaction, structure-function analysis, overview 754029
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.20physiological function peptidyl-Lys metallopeptidase (LysN) from Armillaria mellea is an aspzincin metalloprotease, which cleaves in front of lysines 754029
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