3.2.1.17 (GlcNAc)2 - 10813 3.2.1.17 (GlcNAc)3 - 9297 3.2.1.17 2-mercaptoethanol - 63 3.2.1.17 4-hexylresorcinol activates at low concentrations, up to 10-15 molcules of hexylresorcinol per protein globule, but inhibits at higher concentrations, at above 100 molecules of hexylresorcinol per protein globule the activity is abolished 4112 3.2.1.17 5-[(4,6-dichloro-1,3,5-triazin-2-yl)amino]-4-hydroxy-3-[(E)-phenyldiazenyl]naphthalene-2,7-disulfonate i.e. brilliant red. Non-covalent interaction with formation of multiple complexes such as lysozyme(brilliant red)17 at pH 2.0, lysozyme(brilliant red)15 at pH 3.3, lysozyme(brilliant red)12 at pH 4.4. Two-step binding model, in which one or two brilliant red molecules enter the hydrophobic outer surface of lysozyme. Binding results in change of lysozyme conformation and in its inhibition 150602 3.2.1.17 Ag+ 0.01 mM, 7% inhibition 75 3.2.1.17 Ag2+ - 1041 3.2.1.17 AgNO3 - 360 3.2.1.17 alginate inactivation of the wild-type enzyme at high concentrations 2943 3.2.1.17 Bacillus subtilis DNA in presence of 0-50 mM NaCl 102502 3.2.1.17 c-type inhibitor Ivy complete inhibition 197328 3.2.1.17 Ca2+ 34% activation at 5 mM, 150% activation at 10 mM, 280% at 5 mM of recombinant enzyme. 58% Inhibition at 10 mM, 97% at 50 mM of native enzyme, 66% inhibition at 20 mM, 97% at 50 mM of recombinant enzyme; 87% inhibition at 5 mM, 93% at 10 mM 15 3.2.1.17 chitotetraose - 2831 3.2.1.17 Co(NO3)2 10 mM 12478 3.2.1.17 CoCl2 10 mM 414 3.2.1.17 CoCl2 1 mM 414 3.2.1.17 CuSO4 - 263 3.2.1.17 CuSO4 10 mM 263 3.2.1.17 dithiothreitol - 45 3.2.1.17 DNA DNA from herring sperm, in presence of 0-50 mM NaCl 293 3.2.1.17 DNA inactivation of the wild-type enzyme at high concentrations 293 3.2.1.17 EDTA above 0.1 mM 21 3.2.1.17 EDTA at 10 and 20 mM causes 15% and 43% reduction of the enzyme activity 21 3.2.1.17 EDTA - 21 3.2.1.17 F-actin inhibition of the wild-type enzyme 6676 3.2.1.17 Fe3+ - 70 3.2.1.17 FeCl3 1 mM 702 3.2.1.17 g-type inhibitor PliG complete inhibition 197327 3.2.1.17 glucosamine - 2656 3.2.1.17 glutathione - 44 3.2.1.17 glycol chitosan - 16292 3.2.1.17 Hewli - 31825 3.2.1.17 Hg2+ - 33 3.2.1.17 HgCl2 - 110 3.2.1.17 histamine - 605 3.2.1.17 Human serum albumin the catalytic rate constant decreases tenfold when the albumin concentration increases, while the Michaelis constant remains almost constant in the albumin concentration range employed. Theoretical modeling of the structure of the human serum albumin-lysozyme complex shows that the Glu35 and Asp52 residues located in the active site of lysozyme are oriented toward the human serum albumin surface. This conformation will inactivate lysozyme molecules bound to human serum albumin, molecular dynamic calculations, overview 8302 3.2.1.17 ICl - 44244 3.2.1.17 inhibitor of vertebrate lysozyme Escherichia coli inhibitor of vertebrate lysozyme. Electrostatic interactions makes a dominant contribution to inhibition. Weaker binding mode between Ivy and goose lysozyme compared to hen lysozyme 74912 3.2.1.17 inhibitor of vertebrate lysozyme i.e. Escherichia coli inhibitor of vertebrate lysozyme. Electrostatic interactions makes a dominant contribution to inhibition. Weaker binding mode between Ivy and goose lysozyme compared to hen lysozyme 74912 3.2.1.17 Ivy lysozyme inhibitor from Escherichia coli, strong inhibition 35455 3.2.1.17 KCl - 79 3.2.1.17 lipoprotein lipoprotein in bound form, in presence of 0-5 mM NaCl 99392 3.2.1.17 lysozyme inhibitory protein Ivy homodimeric antitoxin, inhibitor of vertebrate lysozyme, from Escherichia coli 197329 3.2.1.17 MgCl2 - 196 3.2.1.17 MliC i.e. membrane bound lysozyme inhibitor of C-type lysozyme, crystallization data in complex with chicken egg white lysozyme. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues 74913 3.2.1.17 MliC i.e. membrane bound lysozyme inhibitors of c-type lysozyme, isolated from Escherichia coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in Escherichia coli. Related to a group of proteins with a common conserved COG3895 domain 74913 3.2.1.17 Mn2+ - 11 3.2.1.17 Mn2+ 0.01 M, 17% inhibition 11 3.2.1.17 additional information as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa 2 3.2.1.17 additional information as yet unknown lysozyme inhibitors may exist in some Grame-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa 2 3.2.1.17 additional information 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 2 3.2.1.17 additional information 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 2 3.2.1.17 additional information Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory 2 3.2.1.17 additional information 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 2 3.2.1.17 additional information interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM 2 3.2.1.17 additional information the enzyme shows resistance to proteolysis 2 3.2.1.17 additional information no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG 2 3.2.1.17 additional information the purified recombinant enzyme is resistant to pepsin and trypsin to some extent at 40°C 2 3.2.1.17 additional information design and construction, based on the protein structures of lambda lysozyme and the SH3 domain of human Crk, of a synthetic protein switch that controls the activity of lysozyme by sterically hindering its active cleft through the binding of SH3 to its CB1 peptide-binding partner, i.e. fusion proteins Venus-CB1-lysozyme, Venus-CB1-lysozyme-CB1, Venus-CB1 and His-nSH3C. Modelling of fusion protein designs with lysozyme and CB1, in the absence of SH3, the lysozyme-CB1 fusion protein functions normally. In the presence of SH3, the lysozyme activity is inhibited and with the addition of excess CB1 peptides to compete for SH3 binding, the lysozyme activity is restored 2 3.2.1.17 mucin inactivation of the wild-type enzyme at high concentrations 6711 3.2.1.17 N,N',N''-triacetylchitotriose competitive. Preincubation at neutral pH impairs aggregation of lysozyme and fibrillogenesis at pH 12.2. Lysozyme-chitotriose complex at pH 12.2 displays reduced thioflavin T and 8-anilino-1-naphthalene sulfonic acid fluorescence, small oligomers but no amyloid fibrils, absence of large aggregates, marginally more helical content, and more than 70% of enzymatic activity after 24 h 3550 3.2.1.17 N-acetylglucosamine - 458 3.2.1.17 N-acetylmuramic acid - 15859 3.2.1.17 N-bromosuccinimide pH 4 208 3.2.1.17 Na+ 14% inhibition at 10 mM, 81% at 100 mM; activates the native enzyme 3.43fold at 50 mM, the recombinant enzyme 4.3fold at 100 mM, inhibition of native, not recombinant, enzyme at 200 mM 59 3.2.1.17 NaCl - 42 3.2.1.17 NaCl almost complete inhibition at 0.8 M 42 3.2.1.17 NiCl 1 mM 96937 3.2.1.17 NiSO4 10 mM 2860 3.2.1.17 Nuclear lysozyme inhibitor other subcellular lysozymes except nuclear are unaffected 99507 3.2.1.17 PliC i.e. periplasmic lysozyme inhibitor of c-type lysozyme, isolated by affinity chromatography from a periplasmic extract of Salmonella enteritidis and related to a group of proteins with a common conserved COG3895 domain 151328 3.2.1.17 PliI periplasmic lysozyme inhibitor of the I-type lysozyme from Aeromonas hydrophila has a high affinity for I-type lysozyme, but does not bind or inhibit vertebrate C- or G-type lysozymes 159672 3.2.1.17 poly-alpha,D-Na-glutamate in presence of 0-100 mM NaCl 103522 3.2.1.17 poly-gamma,D-Na-glutamate in presence of 0-100 mM NaCl 103523 3.2.1.17 poly-L-lysine - 2769 3.2.1.17 porcine gastric mucin inhibits activity of lysozyme in solution in a pH-dependent manner. The amount of inhibition is dependent on mucin concentration, incubation time and temperature, and the structural integrity of the mucin 23849 3.2.1.17 potassium hyaluronate in presence of 0-5 mM NaCl 103549 3.2.1.17 RNA yeast RNA in presence of 0-50 mM NaCl 527 3.2.1.17 SDS - 124 3.2.1.17 Sodium citrate above 0.1 M 2357 3.2.1.17 Zn(NO3)2 10 mM 51970 3.2.1.17 ZnCl2 - 271 3.2.1.17 ZnCl2 10 mM 271 3.2.1.17 ZnCl2 inhibits at 2-30 mM 271