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3.2.1.17: lysozyme

This is an abbreviated version!
For detailed information about lysozyme, go to the full flat file.

Word Map on EC 3.2.1.17

Reaction

N,N',N'',N'''-tetraacetylchitotetraose
+
H2O
=
N,N',N''-triacetylchitotriose
 +
N-acetyl-D-glucosamine

Synonyms

1,4-beta-N-acetylmuramidase, 1,4-beta-N-acetylmuramidase 1, 1,4-beta-N-acetylmuramidase A/C, 1,4-beta-N-acetylmuramidase M1, 1,4-beta-N-acetylmuramoylhydrolase, 1,4-N-acetylmuramidase, abLysI, AcmB, ASTL, Autolysin, BA-lysozyme, c-type lysozyme, CCLys-g, CFL, chicken-type lysozyme, cLys3, CP-1 lysin, CP-7 lysin, CP-9 lysin, CPL, DEL-I, DEL-II, DEL-III, destabilase-lysozyme, EGL, Egyptian goose egg-white lysozyme, Egyptian goose lysozyme, endolysin, EQL, equine lysozyme, fOg44 endolysin, g-lysozyme, g-type lysozyme, GEWL, globulin G, globulin G1, goose type lysozyme, Goose-type lysozyme, gp144, gp36C, GSTL, HEWL, HLysG2, hLYZ, HLZ, i-type lysozyme, iLys, iLys2, invertebrate lysozyme, invertebrate type lysozyme, L-7001, LAL, lambda lysozyme, Late protein gp15, Lys-rich lysozyme 2, lysC, LYSC-1, LysG, LysgaY, LysGL, lysi1, lysi2, Lysis protein, Lysosyme, lysozym, Lysozyme, lysozyme 1, lysozyme 1 precursor, lysozyme A, lysozyme B, lysozyme c, lysozyme c-1, lysozyme g, lysozyme g-like 2, lysozyme SP0987, lysozyme-g, LYZ, LYZ2, M1L, Mdl1, MdL2, mlD-Ds1, mlD-Ds2, mlD-Ds3, MLL-A, MLL-B, mucopeptide glucohydrolase, mucopeptide N-acetylmuramic acid hydrolase, mucopeptide N-acetylmuramoylhydrolase, muramidase, mutanolysin, MV1 lysin, N,O-diacetylmuramidase, N-acetylglucosaminidase autolysin, N-acetylmuramic hydrolase, N-acetylmuramide glycanhydrolase, n-SalC, n-SalG, OEL, OHLysG1, OHLysG2, OHLysG3, Outer wedge of baseplate protein, P13, PALysG, Peptidoglycan hydrolase, peptidoglycan n-acetylmuramic hydrolase, phage-type like lysozyme, phiKZ endolysin, Ply3626, PR1-lysozyme, Protein gp17, Protein gp19, Protein Gp25, Protein Gp5, Protein gp54, Protein gpK, SalG, SjLys, SmLysC, SSTL A, SSTL B, T4 lysozyme, T4L, TJL, transglycosylase, VpLYZ, WGL, wood duck lysozyme

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.17 lysozyme

Crystallization

Crystallization on EC 3.2.1.17 - lysozyme

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM NH4H2PO4, 100 mM Tris pH 8.8, 45% 2-methyl-2,4-pentanediol
using 200xa0mM MgCl2, 100xa0mM Tris (pHxa08.0) and 20% (w/v) PEG 6000
modeling of complex with GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
hanging drop vapor diffusion method
-
recombinant bovine stomach lysozyme 2, to 1.5 A resolution. Space group P212121. Stability may be due to negatively charged surfaces, a shortened loop and slat bridges
crystal structure of mutant N44Q/N47Q/N49Q/N68Q/N103Q is substantially identical to that of the wild type, and the substitutions of Asn to Gln are appropriate for the folding and structural analyses of this protein
-
comparison of native and A-states
-
phage T4 induced: study of structural basis of thermal stability
-
hanging drop vapor diffusion method
-
asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings
atomic and molecular displacements
-
crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme
-
crystallization conditions
-
crystallization data in complex with membrane bound lysozyme inhibitor of C-type lysozyme MliC. 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
crystallographic studies of denaturation and renaturation
-
determinatipon of crystallization phase diagrams at pH 2.5, pH 6.0, and pH 7.5. At pH values below 4.5, the border between the metastable region and the nucleation region shifts to the lower precipitant concentration in the phase diagramm and at pH values above 4.5, the border shifts to higher precipitant concentrations. The qualities of crystals at different pH values are more or less equivalent
hanging drop method
-
hanging drop method and nanotemplate crystallization method. Crystals grown by the nanostructured template method appear radiation-resistant
-
hanging drop method, crystals of native enzyme and enzyme in complex with various alcohols (ethanol, 1-butanol, 1-pentanol, 2-propanol or TFE). Although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound water. Increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein
hanging drop vapor diffusion method, using 2.8-3.0% (w/v) (about 0.35 M) sodium nitrate
-
hexagonal crystal crystallize from a saturated sodium nitrate solution at pH 8.4, crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. 1.46 A resolution
-
in complex with arginine and benzyl alcohol, at 45°C, hanging drop vapor diffusion method
kinetics and thermodynamics of lysozyme precipitation in ammonium sulfate solutions at pH 4 and 8 and room temperature. If sufficient time is allowed, microcrystals develop following an induction period after initial lysozyme precipitation, even up to ionic strengths of 8 M and at acidic pH, where lysozyme is refractory to crystallization in ammonium sulfate
measurement of lysozyme solubility in aqueous solutions as a function of NaCl, KCl, and NH4Cl concentrations at 25°C and pH 4.5. Simple model for the crystalline phase based on salt partitioning between solution and the hydrated protein crystal
membrane crystallization of lysozyme under forced solution flow
-
mutants K33A and K33N. The side chain of K33 in wild-type hydrogen bonds with N37 involved in the substrate-binding region. Orientation of N37 differs in mutants K33A and K33N
pure enzyme, hanging drop vapour diffusion method, 50 or 150 mg/ml enzyme in 0.1 M sodium acetate, pH 4.5, sodium phosphate, pH 6.5, or Tris-HCl, pH 8.5, mixing of 0.0015 ml of protein solution and 0.0015 ml of reservoir solution, equilibration against 0.5 ml of reservoir solutiom, 20°C, crystallization method evaluation using Gly, Ser, Asp, Glu, Arg, ornithine, Lys and glycine ethyl ester as precipitants at pH 4.5, 6.5 and 8.5, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
-
purified enzyme in complex with 1-butyl-3-methylimidazoliumtetrafluoroborate, 1-butyl-3-methylimidazolium chloride, 1-butyl-3-methylimidazolium bromide, and 1,3-dimethylimidazolium iodine, 8% protein in 5% NaCl and 0.1 M sodium acetate, pH 4.5, ligands are injected into the protein solution. Supersaturated solutions are obtained by mixing protein stock solutions with precipitant solutions, 4°C, X-ray diffraction structure determination and analysis
-
purified recombinant mutant R101D/R115H, 7 mg/ml protein in 10 mM potassium phosphate, pH 6.0, 100 mM NaCl, is mixed with crystallization solution containing 20 mM sodium acetate, pH 4.3, and 1.25 M NaCl, 18°C, 3-4 days, X-ray diffraction structure determination and analysis at 2.04 A resolution, molecular replacement and modeling
-
purified recombinant MdL2, sitting drop vapour diffusion method, 18°C, precipitant solution containing 28% isopropanol, 21% PEG 4000, and 0.115 M sodium citrate pH 4.2, addition of 0.2 M ammonium acetate, 30% 2-methyl-2,2-pentanediol, 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 1 crystals belong to the monoclinic space group P2(1), unit-cell parameters a = 36.52, b = 79.44, c = 45.20 A, beta = 102.97°
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 2 crystals belong to the orthorhombic space group P2(1)2(1)2, unit-cell parameters are a = 73.90, b = 96.40, c = 33.27 A
vapour-diffusion sitting-drop method, structure of lysozyme c in native form and complexed form with (N-acetylglucosamine)3
1.9 A resolution, space group P212121. Positions of P104 in the substrate subsite A and other amino acids in the subsites E and F differ from those of hen egg white, while the overall stuctures are very similar
the x-ray structure of the lytic transglycosylase gp144 is determined to 2.5 A resolution, in complex with chitotetraose, (N-acetylglucosamine)4, to 2.6 A resolution
Phikzvirus phiKZ
vapor diffusion hanging drop method, crystal structure of the enzyme complexed with a trimer of N-acetylglucosamine to 1.6 A resolution
-
purified enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 150 mM NaCl and 50 mM HEPES, pH 7.25, is mixed with 0.001 ml of reservoir solutions containing 43-45% ammonium sulfate, 0.01 M cobalt chloride, and 0.1 M MES, pH 6.25-6.5, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 1.75 A resolution
hangingdrop and sitting-drop vapour-diffusion methods
-
-
Tequatrovirus T4
-
in complex with Ni2+ ions, sitting drop vapor diffusion method, using 20% (w/v) PEG 6000, 100 mM MES pH 5.0
Tequatrovirus T4
the crystal structure of the switch mutant L20/R63A liganded to both methyl- and ethylguanidinium ions is determined at resolutions of 1.7 A and 1.8 A, respectively
Tequatrovirus T4