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Results 1 - 10 of 84 > >>
EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more as yet unknown lysozyme inhibitors may exist in some Grame-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more bacterial membrane proton motive force regulates the lytic activity of the secreted endolysin Lys44 from Oenococcus oeni phage fOg44. Cytoplasmic membrane voltage dissipation is necessary but not sufficient for the full sensitization of cells to Lys44 Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more lysozyme and its derived peptides are able to bind biotin-labeled pUC19 plasmid DNA. The nonpeptide RAWVAWRNR, amino acids 107-115 of lysozyme, binds DNA with a KD value comparable to histones. Binding results in conformational changes Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more study on the inhibitory effect on the enzymatic activity of lysozyme of a number of peptides each containing about 10 amino acids and overlapping exhaustively the protein sequence. A small fraction of them are able to inhibit the biological activity of the protein with micromolar efficiency. The peptide displaying the same sequence of segment 91-100 of the protein, and essentially corresponding to the last three turns of helix C, is the most efficient. The inhibitory mechanism is nonconventional. Local elementary structures formed in the denatured state, drive the folding process and selected peptides compete with these structures in binding complementary regions of the protein, preventing the formation of the native state Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more the enzyme shows resistance to proteolysis Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.17more the purified recombinant enzyme is resistant to pepsin and trypsin to some extent at 40°C Go to the Ligand Summary Page
Results 1 - 10 of 84 > >>