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Information on EC 3.2.1.17 - lysozyme and Organism(s) Gallus gallus and UniProt Accession P00698

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.17 lysozyme
IUBMB Comments
cf. also EC 3.2.1.14 chitinase.
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This record set is specific for:
Gallus gallus
UNIPROT: P00698
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The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysozyme, endolysin, autolysin, t4 lysozyme, transglycosylase, muramidase, peptidoglycan hydrolase, lysozyme a, mutanolysin, lysozyme c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-N-acetylmuramidase
-
-
-
-
1,4-beta-N-acetylmuramidase A/C
-
-
-
-
1,4-beta-N-acetylmuramidase M1
-
-
-
-
1,4-beta-N-acetylmuramoylhydrolase
-
-
-
-
1,4-N-acetylmuramidase
-
-
-
-
Autolysin
-
-
-
-
CP-1 lysin
-
-
-
-
CP-7 lysin
-
-
-
-
CP-9 lysin
-
-
-
-
CPL
-
-
-
-
endolysin
-
-
-
-
globulin G
-
-
-
-
globulin G1
-
-
-
-
Goose-type lysozyme
-
-
-
-
L-7001
-
-
-
-
Late protein gp15
-
-
-
-
Lysis protein
-
-
-
-
Lysosyme
-
-
-
-
lysozym
-
-
Lysozyme
lysozyme g
-
-
-
-
mucopeptide glucohydrolase
-
-
-
-
mucopeptide N-acetylmuramic acid hydrolase
-
-
mucopeptide N-acetylmuramoylhydrolase
-
-
-
-
muramidase
MV1 lysin
-
-
-
-
N,O-diacetylmuramidase
-
-
-
-
N-acetylmuramic hydrolase
-
-
N-acetylmuramide glycanhydrolase
-
-
Outer wedge of baseplate protein
-
-
-
-
P13
-
-
-
-
Peptidoglycan hydrolase
-
-
-
-
peptidoglycan n-acetylmuramic hydrolase
-
-
PR1-lysozyme
-
-
-
-
Protein gp17
-
-
-
-
Protein gp19
-
-
-
-
Protein Gp25
-
-
-
-
Protein Gp5
-
-
-
-
Protein gp54
-
-
-
-
Protein gpK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
lysozyme has a potent antimicrobial effect due to the hydrolysis of the beta-linkage between muramic acid and N-acetyl glucosamine present in the microbial walls
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-63-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cell wall of Micrococcus luteus + H2O
?
show the reaction diagram
-
-
-
?
chito-oligosaccharide + H2O
?
show the reaction diagram
oligosaccharides with a degree of polymerization between three and six units, product analysis by mass and NMR spectrometry
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
show the reaction diagram
DA48
-
-
?
ethylene glycol chitin + H2O
?
show the reaction diagram
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ?
show the reaction diagram
-
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
show the reaction diagram
eight amino acid residues interact with the N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose oligomer: Arg73, Gly102, Asn103, Leu56, Ala107, Val109, Ala110, and Lys33
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
show the reaction diagram
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
increases the formation of lysozyme dimers
Mn
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
Ni
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
-
MliC
-
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
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
-
(GlcNAc)2
-
-
(GlcNAc)3
-
-
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
Bacillus subtilis DNA
-
in presence of 0-50 mM NaCl
-
DNA
-
DNA from herring sperm, in presence of 0-50 mM NaCl
Hewli
-
-
-
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
-
Ivy
-
lysozyme inhibitor from Escherichia coli, strong inhibition
-
lipoprotein
-
lipoprotein in bound form, in presence of 0-5 mM NaCl
-
N-acetylglucosamine
-
-
poly-alpha,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
poly-gamma,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
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
-
potassium hyaluronate
-
in presence of 0-5 mM NaCl
RNA
-
yeast RNA in presence of 0-50 mM NaCl
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TRAP
i.e. target of RNAIII activating protein , membrane-associated protein from Staphylococcus aureus. TRAP can specifically bind lysozyme and lysostaphin through its C-terminus and enhance lysozymal activities in vitro
-
1,3-dimethylimidazolium iodine
-
50% activation at 5%
1-butyl-3-methylimidazolium bromide
-
below 20% activation at 5%
1-butyl-3-methylimidazolium chloride
-
below 10% activation at 5%
1-butyl-3-methylimidazolium tetrafluoroborate
-
below 20% activation at 5%
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
5-methylresorcinol
-
interacts with the surface of lysozyme directly, not via water hydrogen bonds. This leads to a decrease in the denaturation temperature and an increase in the amplitude of equilibrium fluctuations, allowing it to be a powerful activator
Protein disulfide isomerase
-
enhances activity of the activity of renatured lysozyme
-
additional information
-
ionic liquids influence protein crystal morphology, size, polymorph, crystal quality, and modify solution properties, possible mechanisms, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.001
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
pH 6.2-6.3, 25°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
-
-
5 - 7
-
assay at
5.2
-
assay at
6.2
-
assay at
6.3
-
assay at
7
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8
-
immobilized enzyme, activity range, profile overview
5 - 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
assay at
30
-
assay at
37 - 42
-
assay at
40
-
assay at
65
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
-
immobilized enzyme, activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
isoelectric focusing
11.2
-
calculated from amino acid sequence
11.4
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme activates the human sweet taste receptor T1R2/T1R3
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYSC_CHICK
147
1
16239
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
-
14120
-
MADI-TOF
14310
-
FT-ICR mass spectroscopy
14600
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE
dimer
-
formation of covalent bonds between lysozyme molecules by zero-length cross-linking. Approximately one-third of the total lysozyme becomes cross-linked. The enzymatic activity of cross-linked lysozyme dimer is the same as monomer. The activity of lysozyme dimer remains constant up to 10 min at 80°C. Lysozyme possess a compact structure in the dimer form
monomer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
engineered glycosylation sites at postition 19 and 49
additional information
-
modified with methoxypolyethylene glycol-p-nitrophenyl carbonate (mPEG-pNP, MW 5000)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings
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
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, 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
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
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
atomic and molecular displacements
-
crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme
-
crystallization conditions
-
crystallographic studies of denaturation and renaturation
-
hanging drop method
-
hanging drop method and nanotemplate crystallization method. Crystals grown by the nanostructured template method appear radiation-resistant
-
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
-
membrane crystallization of lysozyme under forced solution flow
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K33A
140% of wild-type lytic activity, 116% of wild-type activity on glycol chitin
K33N
130% of wild-type lytic activity, 111% of wild-type activity on glycol chitin
R114A
decrease in activity toward substrate glycol chitin to 80.5%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta is about 50% of wild-type. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123
R114H
decrease in activity toward substrate glycol chitin to 79%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123
R114L
no decrease in activity toward substrate glycol chitin. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
D52S
-
inactive
N103D
-
increased structural flexibility and surface functional properties
N106D
-
increased structural flexibility and surface functional properties
R21T/G49N
-
better emulsifying properties
W108GA
-
site-directed mutagenesis
W111GA
-
site-directed mutagenesis
W123G
-
site-directed mutagenesis
W28GA
-
site-directed mutagenesis
W62GA
-
site-directed mutagenesis
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.2
lysozyme sponaneously forms soluble oligomers, which are later stabilized by intermolecular disulfide bonds
696471
2
the enzyme hydrolyzes at pH 2.0
752187
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78 - 90
melting temperature at pH 3.0. The enzyme hydrolyzes at 90°C
25
-
pH 3.2, half-life for the free enzyme is 39 h, for the enzyme immobilized on tosyl-activated and carboxylated micro-size magnetic particles is 280 h and 134 h, respectively
60
-
purified commercial enzyme, pH 6.2, 60 min, inactivation
76
-
mid-transition temperature is 76.3°C for S6K-lysozyme and 76.0°C for S7-lysozyme
77
-
mid-transition temperature of wild-type enzyme
80
-
the activity of lysozyme dimer remains constant up to 10 min
85
-
purified enzyme, pH 6.2, inactivation after 60 min
additional information
-
lysozyme's interaction with two types of rod-shaped gold nanostructures reveals that the structure, lytic activity, and stability of the enzyme has not undergone any undesirable change. Once the protein is adsorbed onto the surface of gold nanorod/gold nanorice, it gains a more regular structure, retaining lytic activity and stability, kinetics, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during egg storage, lysozyme activity is strongly decreased from day 10 day
-
microwave thermal modification of lysozyme can increase the formation of oligomers in comparison to conventional physical heating, improving the enzyme's hydrophobicity by the use of this heat source for physicochemical modification
-
the 295 nm damage threshold of lysozyme lies between 0.0001 and 0.0003 mW. Gold nanoparticles coated
-
the addition of guanidine hydrochloride accelerates strongly the lysozyme fibril formation. The addition of urea does not lead to lysozyme unfolding but can change the protein tertiary structure to a certain extent
-
the effects of sugars trehalose, maltose, and sucrose on the protein conformation are relatively weak, in agreement with the preferential hydration of lysozyme. Sugars seem to increase significantly the relaxation times of the protein. These effects are correlated to the fractional solvent accessibilities of lysozyme residues and further support the slaving of protein dynamics
-
the enzyme complexed to heparin shows a significantly reduced physical stability when stored at 37°C for 12 weeks
-
with hyaluronic acid and oleic acid efficiently protect lysozyme from the photochemical effects of UVB light
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose column chromatography
Superdex 200 gel filtration
anion exchange column chromatography, using the frustules from two cultured diatoms, Nitzschia bilobata and Psammodictyon panduriforme
-
efficient and inexpensive lysozyme purification from chicken egg white can be achieved by using polyethylene glycol-salt aqueous two-phase system
-
hydrophobic affinity ligand L-tryptophan immobilized magnetic poly(glycidyl methacrylate) [m-poly(GMA)] beads in monosize form (0.0016 mM in diameter) are used for the affinity purification of lysozyme from chicken egg white. The chemisorption processes can be the rate-limiting step in the adsorption process. After 10 adsorption-elution cycles, m-poly(GMA)-L-tryptophan beads can be used without significant loss in lysozyme adsorption capacity
-
purification of recombinant mutants in unfolded non-native state, solubilization of the recombinant mutants from Escherichia coli strain BL21(DE3) inclusion bodies in 20 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, and 8 M urea, pH 7.5, centrifugation, and cation exchange chromatography with elution by 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, and 4 M urea, pH 7.5
-
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expression in Saccharomyces cerevisiae
a large polymannose (Man310GlcNAc2) chain-linked lysozyme is predominantly expressed in Saccharomyces cerevisiae accompanied by small amounts of a core-type oligomannose chain (Man14GlcNAc2)-linked lysozyme in the yeast medium where the extracellular pH is kept at 3.5 or above, while an oligomannose chain lysozyme is preferentially expressed in the yeast medium where the pH is less than 3
-
expression in human cell lines HeLa and MCF-7
-
expression of enzyme mutants in Escherichia coli strain BL21(DE3) in inclusion bodies
-
expression of recombinant protein in Saccharomyces cerevisiae
-
expression of wild-type and engineered enzyme in Saccharomyces cerevisiae
-
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dithiothreitol decreases content of alpha-helices with a corresponding increase in random coil, while 2,2,2-trifluoroethanol has a negligible effect on secondary structure
measurement of lysozyme solubility in aqueous solutions as a function of NaCl, KCl, and NH4Cl concentrations at 25°C and pH 4.5. The dependence of solubility on salt type and concentration strongly correlates with the corresponding dependence of the preferential interaction coefficient. The solubility dependence on salt concentration is substantially affected by the corresponding change of protein chemical potential in the crystalline phase. Simple model for the crystalline phase based on salt partitioning between solution and the hydrated protein crystal
no noticeable enhancement in enzyme activity and stability in the presence of supercritical CO2 pretreatment for lysozyme samples denatured in 8 M urea at 50°C and pH 6.2. Supercritical CO2 pretreated lysozyme samples in 0.067 M phosphate buffer containing dithiothreitol at 0.1 M, pH 6.2, 25°C or 0.01 M dithiothreitol, pH 6.2, 50 °C at 2500 psi and 50°C have better residual activity relative to samples that are not pretreated. In addition, when denaturing at 65°C and pH 9.0, the pretreatment in supercritical CO2 at 2500 psi and 50°C results in the best stability of lysozyme
oxidative refolding carried out in presence of protein disulfide isomerase results in an increased refolding rate and a recovered activity exceeding 100%. Refolding is achieved through the formation of protein disulfide isomerase-lysozyme intermediates and the excess activity is derived from the nascent lysozyme released from these complexes
study on guanidinium chloride-induced equilibrium unfolding of monomer and dimer at pH 2.0. Unfolding curves at 222 and 289 nm in lysozyme dimer lack coincidence, while lysozyme monomer shows a single cooperative transition. Kinetic parameters are calculated on basis of a two-state mechanism for monomer and a three-state mechanism for dimer. Zero length cross-linking can stabilize the intermediate
catalytic properties during renaturation
-
characterization of the refolded hen lysozyme variant (4CAHEL) lacking two outside disulfide bonds (C6-C127 and C30-C115). 4CAHEL is a folding intermediated formed in the early stage of the refolding process of the reduced lysozyme
-
crystallographic studies of denaturation and renaturation
-
measurement of refolding after pressure unfolding. Pressure acts against aggregation and therefore no irreversible aggregation takes place during the pressure treatment. After the release of the pressure, folding intermediate structures are found which are formed during the decompression of the lysozyme. The intermediates are only formed if the protein is unfolded, subdenaturing pressure can not populate this intermediates
-
neutral cyclodextrins are better refolding agents than the charged sugars. The presence of anionic substitutents like carboxy and phosphate groups promote aggregate formation and completely abolish the refolding ability of the sugars. Cyclodextrins with cationic functional groups do not show any significant effects on lysozyme refolding. The presence of both anionic and cationic substituents on the same cyclodextrin molecule partially restores its renaturation ability
-
production of a three-disulfid derivative
-
stabilizing effect of cross-linked enzyme
-
the refolding rate increases with an increase in concentration of protein disulfide isomerase. About 100% activity is recovered after 10 min initiation of the reaction at 0.062 mM protein disulfide isomerase, whereas several hours are needed for 100% activity recovery in absence of protein disulfide isomerase
-
thermodynamic analysis of unfolding in presence of GdnHCl
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
food industry
dry-heated hen egg white lysozyme simultaneously exhibits enhanced foaming properties and aggregation capacity. It may self-associate at the air/water interface, stabilizing air bubbles
medicine
Hen egg white lysozyme amyloid fibrils cause extensive aggregation of human erythrocytes and lipid vesicles without any significant lysis. The membrane activity of lysozyme fibrils suggests that the interaction of lysozyme fibrils with cellular membranes could be a contributing factor under conditions of human lysozyme amyloidosis
food industry
industry
-
immobilization of lysozyme to the surface of stainless steel as a new strategy to protect the surface against the growth of biofilms
medicine
synthesis
-
the extracellular pH-sensitive glycosylation system can be used to obtain bioactive and surface functional neoglycoproteins
additional information
-
adsorption studies are conducted to investigate the effects of shaking rate, temperature, and initial lysozyme concentration on the uptake rate of lysozyme by the NaY zeolite (immobilization support)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tomizawa, H.; Yamada, H.; Ueda, T.; Imoto, T.
Isolation and characterization of 101-succinimide lysozyme that possesses the cyclic imide at Asp101-Gly102
Biochemistry
33
8770-8774
1994
Gallus gallus
Manually annotated by BRENDA team
Matthias, P.D.; Renkawitz, R.; Grez, M.; Schutz, G.
Transient expression of the chicken lysozyme gene after transfer into human cells
EMBO J.
1
1207-1212
1982
Gallus gallus
Manually annotated by BRENDA team
Ries-Kautt, M.M.; Ducruix, A.F.
Relative effectiveness of various ions on the solubility and crystal growth of lysozyme
J. Biol. Chem.
264
745-748
1989
Gallus gallus
Manually annotated by BRENDA team
Doucet, J.; Benoit, J.P.
Molecular dynamics studied by analysis of the X-ray diffuse scattering from lysozyme crystals
Nature
325
643-646
1987
Gallus gallus
Manually annotated by BRENDA team
Cho, R.K.; Okitani, A.; Kato, H.
Chemical properties and polymerizing ability of the lysozyme monomer isolated after storage with glucose
Agric. Biol. Chem.
48
3081-3089
1984
Gallus gallus
-
Manually annotated by BRENDA team
Perkins, S.J.; Johnson, L.N.; Machin, P.A.; Phillips, D.C.
Crystal structure of egg-white lysozyme of hen in acetate-free medium of lysozyme complexes with N-acetylglucosamine and beta-methyl N-acetylglucosaminide
Biochem. J.
173
607-616
1978
Gallus gallus
Manually annotated by BRENDA team
Fernandez-Sousa, J.M.; Perez-Castells R.; Rodriguez, R.
A simple, one-step chromatographic procedure for the purification of lysozyme
Biochim. Biophys. Acta
523
430-434
1978
Gallus gallus
Manually annotated by BRENDA team
Yonath, A.; Sielecki, A.; Moult, J.; Podjarny, A.; Traub, W.
Crystallographic studies of protein denaturation and renaturation. 1. Effects of denaturants on volume and X-ray pattern of cross-linked triclinic lysozyme crystals
Biochemistry
16
1413-1417
1977
Gallus gallus
Manually annotated by BRENDA team
Yonath, A.; Podjarny, A.; Honig, B.; Sielecki, A.; Traub, W.
Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme
Biochemistry
16
1418-1430
1977
Gallus gallus
Manually annotated by BRENDA team
Junowicz, E.; Charm, S.E.
Purification of lysozyme by affinity chromatography
FEBS Lett.
57
219-221
1975
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Wang, S.L.; Murao, S.; Arai, M.
Inhibition of lysozyme activity by acidic polymers
Agric. Biol. Chem.
55
1401-1402
1991
Brassica sp., Gallus gallus, Homo sapiens, Meleagris gallopavo, Streptomyces globisporus
-
Manually annotated by BRENDA team
Van den Berg, B.; Chung, E.W.; Robinson, C.V.; Dobson, C.M.
Characterization of the dominant oxidative folding intermediate of hen lysozyme
J. Mol. Biol.
290
781-796
1999
Gallus gallus
Manually annotated by BRENDA team
Bernard, M.; Canioni, P.; Cozzone, P.; Berthou, J.; Jolles, P.
Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
Int. J. Protein Res.
36
46-55
1990
Gallus gallus
Manually annotated by BRENDA team
Shu, Y.; Maki, S.; Nakamura, S.; Kato, A.
Double-glycosylated lysozyme at positions 19 and 49 constructed by genetic modification and its surface functional properties
J. Agric. Food Chem.
46
2433-2438
1998
Gallus gallus
Manually annotated by BRENDA team
Mande, S.C.; Sobhia, M.E.
Structural characterization of protein-denaturant interactions: Crystal structures of hen egg-white lysozyme in complex with DMSO and guanidinium chloride
Protein Eng.
13
133-141
2000
Gallus gallus
Manually annotated by BRENDA team
Ueda, T.; Yamada, H.; Sakamoto, N.; Abe, Y.; Kawano, K.; Terada, Y.; Imoto, T.
Preparations and properties of a lysozyme derivative in which two domains are cross-linked intramolecularly between Trp62 and Asp101
J. Biochem.
110
719-725
1991
Gallus gallus
Manually annotated by BRENDA team
Van Damme, M.P.I.; Moss, J.M.; Murphy, W.H.; Preston, B.N.
Binding properties of glycosaminoglucans to lysozyme - Effect of salt and molecular weight
Arch. Biochem. Biophys.
310
16-24
1994
Gallus gallus
Manually annotated by BRENDA team
Fischer, B.; Summer, I.; Goodenough, P.
Analysis of catalytic properties of hen egg white lysozyme during renaturation from denatured and reduced material
Arch. Biochem. Biophys.
298
361-364
1992
Gallus gallus
Manually annotated by BRENDA team
Denton, M.E.; Scheraga, H.A.
Spectroscopic, immunochemical, and thermodynamic properties of carboxymethyl(Cys6, Cys127)-hen egg white lysozyme
J. Protein Chem.
10
213-232
1991
Gallus gallus
Manually annotated by BRENDA team
Spencer, A.; Morozow-Roche, L.; Noppe, W.; MacKenzie, D.A.; Jeenes, D.J.; Joniau, M.; Dobson, C.M.; Archer, D.B.
Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: Comparisons with the production of hen and human lysozymes
Protein Expr. Purif.
16
171-180
1999
Gallus gallus, Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Kato, A.; Tanimoto, S.; Muraki, Y.; Kobayashi, K.; Kumagai, I.
Structural and functional properties of hen egg-white lysozyme deamidated by protein engineering
Biosci. Biotechnol. Biochem.
56
1424-1428
1992
Gallus gallus
Manually annotated by BRENDA team
Deshpande, A.; Nimsadkar, S.; Mande, S.C.
Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols
Acta Crystallogr. Sect. D
61
1005-1008
2005
Gallus gallus (P00698)
Manually annotated by BRENDA team
Pechkova, E.; Sivozhelezov, V.; Tropiano, G.; Fiordoro, S.; Nicolini, C.
Comparison of lysozyme structures derived from thin-film-based and classical crystals
Acta Crystallogr. Sect. D
61
803-808
2005
Gallus gallus
Manually annotated by BRENDA team
Brinkmann, C.; Weiss, M.S.; Weckert, E.
The structure of the hexagonal crystal form of hen egg-white lysozyme
Acta Crystallogr. Sect. D
62
349-355
2006
Gallus gallus
Manually annotated by BRENDA team
Lopez-Jaramillo, F.J.; Perez-Banderas, F.; Hernandez-Mateo, F.; Santoyo-Gonzalez, F.
Production, crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme
Acta Crystallogr. Sect. F
61
435-438
2005
Gallus gallus
Manually annotated by BRENDA team
Xu, X.; Kashima, O.; Saito, A.; Azakami, H.; Kato, A.
Structural and functional properties of chicken lysozyme fused serine-rich heptapeptides at the C-terminus
Biosci. Biotechnol. Biochem.
68
1273-1278
2004
Gallus gallus
Manually annotated by BRENDA team
Ohkuri, T.; Imoto, T.; Ueda, T.
Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds
Biosci. Biotechnol. Biochem.
69
1206-1208
2005
Gallus gallus
Manually annotated by BRENDA team
Callewaert, L.; Masschalck, B.; Deckers, D.; Nakimbugwe, D.; Atanassova, M.; Aertsen, A.; Michiels, C.W.
Purification of Ivy, a lysozyme inhibitor from Escherichia coli, and characterization of its specificity for various lysozymes
Enzyme Microb. Technol.
37
205-211
2005
Anser sp., Tequatrovirus T4, Brassica oleracea, Gallus gallus
-
Manually annotated by BRENDA team
Nakimbugwe, D.; Masschalck, B.; Deckers, D.; Callewaert, L.; Aertsen, A.; Michiels, C.W.
Cell wall substrate specificity of six different lysozymes and lysozyme ihibitory activity of bacterial extracts
FEMS Microbiol. Lett.
259
41-46
2006
Anser sp., Lambdavirus lambda, Tequatrovirus T4, Brassica oleracea, Gallus gallus, Streptomyces globisporus
Manually annotated by BRENDA team
Higman, V.A.; Boyd, J.; Smith, L.J.; Redfield, C.
Asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings
J. Biomol. NMR
30
327-346
2004
Gallus gallus (P00698)
Manually annotated by BRENDA team
Curcio, E.; Simone, S.; di Profio, G.; Drioli, E.; Cassetta, A.; Lamba, D.
Membrane crystallization of lysozyme under forced solution flow
J. Membr. Sci.
257
134-143
2005
Gallus gallus
-
Manually annotated by BRENDA team
van de Weert, M.; Andersen, M.B.; Frokjaer, S.
Complex coacervation of lysozyme and heparin: complex characterization and protein stability
Pharm. Res.
21
2354-2359
2004
Gallus gallus
Manually annotated by BRENDA team
Su, C.; Chiang, B.H.
Partitioning and purification of lysozyme from chicken egg white using aqueous two-phase system
Proc. Biochem.
41
257-263
2006
Gallus gallus
-
Manually annotated by BRENDA team
Park, W.K.; Chung, J.W.; Kim, Y.K.; Chung, S.C.; Kho, H.S.
Influences of animal mucins on lysozyme activity in solution and on hydroxyapatite surfaces
Arch. Oral Biol.
51
861-869
2006
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Smeller, L.; Meersman, F.; Heremans, K.
Refolding studies using pressure: the folding landscape of lysozyme in the pressure-temperature plane
Biochim. Biophys. Acta
1764
497-505
2006
Gallus gallus
Manually annotated by BRENDA team
Desai, A.; Lee, C.; Sharma, L.; Sharma, A.
Lysozyme refolding with cyclodextrins: structure-activity relationship
Biochimie
88
1435-1445
2006
Gallus gallus
Manually annotated by BRENDA team
Cheng, Y.C.; Lobo, R.F.; Sandler, S.I.; Lenhoff, A.M.
Kinetics and equilibria of lysozyme precipitation and crystallization in concentrated ammonium sulfate solutions
Biotechnol. Bioeng.
94
177-188
2006
Gallus gallus (P00698)
Manually annotated by BRENDA team
Razavet, M.; Artero, V.; Cavazza, C.; Oudart, Y.; Lebrun, C.; Fontecilla-Camps, J.C.; Fontecave, M.
Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein
Chem. Commun. (Camb. )
27
2805-2807
2007
Gallus gallus
Manually annotated by BRENDA team
Manas, P.; Munoz, B.; Sanz, D.; Condon, S.
Inactivation of lysozyme by ultrasonic waves under pressure at different temperatures
Enzyme Microb. Technol.
39
1177-1182
2006
Gallus gallus
Manually annotated by BRENDA team
Yaghoubi, H.; Khajeh, K.; Hosseinkhani, S.; Ranjbar, B.; Naderi-Manesh, H.
Application of zero-length cross-linking to form lysozyme, horseradish peroxidase and lysozyme-peroxidase dimers: Activity and stability
Int. J. Biol. Macromol.
41
624-630
2007
Gallus gallus
Manually annotated by BRENDA team
Nakimbugwe, D.; Masschalck, B.; Atanassova, M.; Zewdie-Bosuener, A.; Michiels, C.W.
Comparison of bactericidal activity of six lysozymes at atmospheric pressure and under high hydrostatic pressure
Int. J. Food Microbiol.
108
355-363
2006
Anser sp., Lambdavirus lambda, Tequatrovirus T4, Brassica oleracea, Gallus gallus, Streptomyces globisporus
Manually annotated by BRENDA team
Chhabra, S.; Sachdeva, V.; Singh, S.
Influence of end groups on in vitro release and biological activity of lysozyme from a phase-sensitive smart polymer-based in situ gel forming controlled release drug delivery system
Int. J. Pharm.
342
72-77
2007
Gallus gallus
Manually annotated by BRENDA team
Shashilov, V.A.; Lednev, I.K.
2D Correlation deep UV resonance Raman spectroscopy of early events of lysozyme fibrillation: kinetic mechanism and potential interpretation pitfalls
J. Am. Chem. Soc.
130
309-317
2008
Gallus gallus
Manually annotated by BRENDA team
Hirakawa, H.; Kawahara, Y.; Ochi, A.; Muta, S.; Kawamura, S.; Torikata, T.; Kuhara, S.
Construction of enzyme-substrate complexes between hen egg-white lysozyme and N-acetyl-D-glucosamine hexamer by systematic conformational search and molecular dynamics simulation
J. Biochem.
140
221-227
2006
Gallus gallus (P00698)
Manually annotated by BRENDA team
Nohara, D.; Hizikata, H.; Asami, O.
Enhancement of the activity of renatured lysozyme by protein disulfide isomerase
J. Biosci. Bioeng.
104
235-237
2007
Gallus gallus
Manually annotated by BRENDA team
Altintas, E.B.; Tuezmen, N.; Candan, N.; Denizli, A.
Use of magnetic poly(glycidyl methacrylate) monosize beads for the purification of lysozyme in batch system
J. Chromatogr. B
853
105-113
2007
Gallus gallus
Manually annotated by BRENDA team
Lerbret, A.; Bordat, P.; Affouard, F.; Hedoux, A.; Guinet, Y.; Descamps, M.
How do trehalose, maltose, and sucrose influence some structural and dynamical properties of lysozyme? Insight from molecular dynamics simulations
J. Phys. Chem. B
111
9410-9420
2007
Gallus gallus
Manually annotated by BRENDA team
Zhang, G.; Darius, S.; Smith, S.R.; Ritchie, S.J.
In vitro inhibitory effect of hen egg white lysozyme on Clostridium perfringens type A associated with broiler necrotic enteritis and its alpha-toxin production
Lett. Appl. Microbiol.
42
138-143
2006
Gallus gallus
Manually annotated by BRENDA team
Chang, Y.; Chu, L.; Tsai, J.; Chiu, S.
Kinetic study of immobilized lysozyme on the extrudate-shaped NaY zeolite
Process Biochem.
41
1864-1874
2006
Gallus gallus
-
Manually annotated by BRENDA team
Yang, G.; Gao, Y.; Feng, J.; Huang, Y.; Li, S.; Liu, Y.; Liu, C.; Fan, M.; Shen, B.; Shao, N.
C-terminus of TRAP in Staphylococcus can enhance the activity of lysozyme and lysostaphin
Acta Biochim. Biophys. Sin.
40
452-458
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Chen, F.F.; Tang, Y.N.; Wang, S.L.; Gao, H.W.
Binding of brilliant red compound to lysozyme: insights into the enzyme toxicity of water-soluble aromatic chemicals
Amino Acids
36
399-407
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Yum, S.; Kim, M.J.; Xu, Y.; Jin, X.L.; Yoo, H.Y.; Park, J.W.; Gong, J.H.; Choe, K.M.; Lee, B.L.; Ha, N.C.
Structural basis for the recognition of lysozyme by MliC, a periplasmic lysozyme inhibitor in Gram-negative bacteria
Biochem. Biophys. Res. Commun.
378
244-248
2009
Gallus gallus (P00698), Gallus gallus
Manually annotated by BRENDA team
Maroufi, B.; Ranjbar, B.; Khajeh, K.; Naderi-Manesh, H.; Yaghoubi, H.
Structural studies of hen egg-white lysozyme dimer: comparison with monomer
Biochim. Biophys. Acta
1784
1043-1049
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Wu, X.; Narsimhan, G.
Effect of surface concentration on secondary and tertiary conformational changes of lysozyme adsorbed on silica nanoparticles
Biochim. Biophys. Acta
1784
1694-1701
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Kumar, S.; Ravi, V.K.; Swaminathan, R.
Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose
Biochim. Biophys. Acta
1794
913-920
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Kawamura, S.; Chijiiwa, Y.; Minematsu, T.; Fukamizo, T.; Varum, K.M.; Torikata, T.
The role of Arg114 at subsites E and F in reactions catalyzed by hen egg-white lysozyme
Biosci. Biotechnol. Biochem.
72
823-832
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Desfougeres, Y.; Lechevalier, V.; Pezennec, S.; Artzner, F.; Nau, F.
Dry-heating makes hen egg white lysozyme an efficient foaming agent and enables its bulk aggregation
J. Agric. Food Chem.
56
5120-5128
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Annunziata, O.; Payne, A.; Wang, Y.
Solubility of lysozyme in the presence of aqueous chloride salts: common-ion effect and its role on solubility and crystal thermodynamics
J. Am. Chem. Soc.
130
13347-13352
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Goto, T.; Ohkuri, T.; Shioi, S.; Abe, Y.; Imoto, T.; Ueda, T.
Crystal structures of K33 mutant hen lysozymes with enhanced activities
J. Biochem.
144
619-623
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Takezawa, A.; Ohshima, Y.; Sudo, T.; Asami, O.; Nohara, D.
Renaturation of lysozyme with a protein disulfide isomerase chaperone results in enzyme super activity
J. Biosci. Bioeng.
106
503-506
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Wang, S.S.; Chao, H.S.; Liu, H.L.; Liu, H.S.
Stability of hen egg white lysozyme during denaturation is enhanced by pretreatment with supercritical carbon dioxide
J. Biosci. Bioeng.
107
355-359
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Kyomuhendo, P.; Nilsen, I.W.; Brandsdal, B.O.; Smalas, A.O.
Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme
J. Mol. Model.
14
777-788
2008
Salmo salar, Gallus gallus (P00698), Anser anser (P00718)
Manually annotated by BRENDA team
Iwai, W.; Yagi, D.; Ishikawa, T.; Ohnishi, Y.; Tanaka, I.; Niimura, N.
Crystallization and evaluation of hen egg-white lysozyme crystals for protein pH titration in the crystalline state
J. Synchrotron Radiat.
15
312-315
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Chaudhary, N.; Nagaraj, R.
Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles
Mol. Cell. Biochem.
328
209-215
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Callewaert, L.; Aertsen, A.; Deckers, D.; Vanoirbeek, K.G.; Vanderkelen, L.; Van Herreweghe, J.M.; Masschalck, B.; Nakimbugwe, D.; Robben, J.; Michiels, C.W.
A new family of lysozyme inhibitors contributing to lysozyme tolerance in gram-negative bacteria
PLoS Pathog.
4
e1000019
2008
Gallus gallus (P00698)
Manually annotated by BRENDA team
Caldarini, M.; Vasile, F.; Provasi, D.; Longhi, R.; Tiana, G.; Broglia, R.A.
Identification and characterization of folding inhibitors of hen egg lysozyme: an example of a new paradigm of drug design
Proteins
74
390-399
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Wang, G.; Dong, X.; Sun, Y.
The role of disulfide bond formation in the conformational folding kinetics of denatured/reduced lysozyme
Biochem. Eng. J.
46
7-11
2009
Gallus gallus
-
Manually annotated by BRENDA team
Matsuoka, T.; Hamada, H.; Matsumoto, K.; Shiraki, K.
Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding
Biotechnol. Prog.
25
1515-1524
2009
Gallus gallus
Manually annotated by BRENDA team
Raccosta, S.; Manno, M.; Bulone, D.; Giacomazza, D.; Militello, V.; Martorana, V.; Biagio, P.
Irreversible gelation of thermally unfolded proteins: structural and mechanical properties of lysozyme aggregates
Eur. Biophys. J.
39
1007-1017
2010
Gallus gallus
Manually annotated by BRENDA team
Wolman, F.; Copello, G.; Mebert, A.; Targovnik, A.; Miranda, M.; Navarro del Canizo, A.; Diaz, L.; Cascone, O.
Egg white lysozyme purification with a chitin-silica-based affinity chromatographic matrix
Eur. Food Res. Technol.
231
181-188
2010
Gallus gallus
Manually annotated by BRENDA team
da Silva Freitas, D.; Abrahao-Neto, J.
Biochemical and biophysical characterization of lysozyme modified by PEGylation
Int. J. Pharm.
392
111-117
2010
Gallus gallus
Manually annotated by BRENDA team
Ganguli, S.; Yoshimoto, K.; Tomita, S.; Sakuma, H.; Matsuoka, T.; Shiraki, K.; Nagasaki, Y.
Regulation of lysozyme activity based on thermotolerant protein/smart polymer complex formation
J. Am. Chem. Soc.
131
6549-6553
2009
Gallus gallus (P00698)
Manually annotated by BRENDA team
Subbaraman, L.N.; Jones, L.
Kinetics of lysozyme activity recovered from conventional and silicone hydrogel contact lens materials
J. Biomat. Sci. Polym. Ed.
21
343-358
2010
Gallus gallus
Manually annotated by BRENDA team
Chakraborti, S.; Chatterjee, T.; Joshi, P.; Poddar, A.; Bhattacharyya, B.; Singh, S.P.; Gupta, V.; Chakrabarti, P.
Structure and activity of lysozyme on binding to ZnO nanoparticles
Langmuir
26
3506-3513
2010
Gallus gallus
Manually annotated by BRENDA team
Byrne, N.; Angell, C.A.
The solubility of hen lysozyme in ethylammonium nitrate/H2O mixtures and a novel approach to protein crystallization
Molecules
15
793-803
2010
Gallus gallus
Manually annotated by BRENDA team
Ansari, M.A.; Zubair, S.; Atif, S.M.; Kashif, M.; Khan, N.; Rehan, M.; Anwar, T.; Iqbal, A.; Owais, M.
Identification and characterization of molten globule-like state of hen egg-white lysozyme in presence of salts under alkaline conditions
Protein Pept. Lett.
17
11-17
2010
Gallus gallus
Manually annotated by BRENDA team
Ito, L.; Shiraki, K.; Yamaguchi, H.
Amino acids and glycine ethyl ester as new crystallization reagents for lysozyme
Acta Crystallogr. Sect. F
66
750-754
2010
Gallus gallus
Manually annotated by BRENDA team
Krupyanskii, Y.; Knox, P.; Loiko, N.; Abdulnasirov, E.; Korotina, O.; Stepanov, S.; Zakharova, N.; Nikolaev, Y.; El-Registan, G.; Rubin, A.
Influence of chemical chaperones on the properties of lysozyme and the reaction center protein from Rhodobacter sphaeroides
Biofizika
56
8-23
2011
Gallus gallus
Manually annotated by BRENDA team
Moghadam, T.T.; Ranjbar, B.; Khajeh, K.; Etezad, S.M.; Khalifeh, K.; Ganjalikhany, M.R.
Interaction of lysozyme with gold nanorods: conformation and activity investigations
Int. J. Biol. Macromol.
49
629-636
2011
Gallus gallus
Manually annotated by BRENDA team
Evran, S.; Yasa, I.; Telefoncu, A.
Modification of lysozyme with oleoyl chloride for broadening the antimicrobial specificity
Prep. Biochem. Biotechnol.
40
316-325
2010
Gallus gallus
Manually annotated by BRENDA team
Calderon, C.; Abuin, E.; Lissi, E.; Montecinos, R.
Effect of human serum albumin on the kinetics of 4-methylumbelliferyl-beta-D-N-N'-N'' triacetylchitotrioside hydrolysis catalyzed by hen egg white lysozyme
Protein J.
30
367-373
2011
Gallus gallus
Manually annotated by BRENDA team
Held, J.; van Smaalen, S.
The active site of hen egg-white lysozyme: flexibility and chemical bonding
Acta Crystallogr. Sect. D
70
1136-1146
2014
Gallus gallus (P00698)
Manually annotated by BRENDA team
Liburdi, K.; Straniero, R.; Benucci, I.; Vittoria Garzillo, A.M.; Esti, M.
Lysozyme immobilized on micro-sized magnetic particles: kinetic parameters at wine pH
Appl. Biochem. Biotechnol.
166
1736-1746
2012
Gallus gallus
Manually annotated by BRENDA team
Dang, L.P.; Fang, W.Z.; Li, Y.; Wang, Q.; Xiao, H.Z.; Wang, Z.Z.
Ionic liquid-induced structural and activity changes in hen egg white lysozyme
Appl. Biochem. Biotechnol.
169
290-300
2013
Gallus gallus
Manually annotated by BRENDA team
Ernest, V.; Gajalakshmi, S.; Mukherjee, A.; Chandrasekaran, N.
Enhanced activity of lysozyme-AgNP conjugate with synergic antibacterial effect without damaging the catalytic site of lysozyme
Artif. Cells Nanomed. Biotechnol.
42
336-343
2014
Gallus gallus
Manually annotated by BRENDA team
Sziegat, F.; Silvers, R.; Haehnke, M.; Jensen, M.R.; Blackledge, M.; Wirmer-Bartoschek, J.; Schwalbe, H.
Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme
Biochemistry
51
3361-3372
2012
Gallus gallus
Manually annotated by BRENDA team
Navarra, G.; Troia, F.; Militello, V.; Leone, M.
Characterization of the nucleation process of lysozyme at physiological pH: primary but not sole process
Biophys. Chem.
177-178
24-33
2013
Gallus gallus
Manually annotated by BRENDA team
Moghadam, T.T.; Ranjbar, B.; Khajeh, K.
Conformation and activity of lysozyme on binding to two types of gold nanorods: a comparative study
Int. J. Biol. Macromol.
51
91-96
2012
Gallus gallus
Manually annotated by BRENDA team
Derde, M.; Guerin-Dubiard, C.; Lechevalier, V.; Cochet, M.F.; Jan, S.; Baron, F.; Gautier, M.; Vie, V.; Nau, F.
Dry-heating of lysozyme increases its activity against Escherichia coli membranes
J. Agric. Food Chem.
62
1692-1700
2014
Gallus gallus
Manually annotated by BRENDA team
Lian, Z.; Ma, Z.; Wei, J.; Liu, H.
Preparation and characterization of immobilized lysozyme and evaluation of its application in edible coatings
Process Biochem.
47
201-208
2012
Gallus gallus
-
Manually annotated by BRENDA team
Atakisi, H.; Moreau, D.; Thorne, R.
Effects of protein-crystal hydration and temperature on side-chain conformational heterogeneity in monoclinic lysozyme crystals
Acta Crystallogr. Sect. D
74
264-278
2018
Gallus gallus
Manually annotated by BRENDA team
Tihonov, M.M.; Milyaeva, O.Y.; Noskov, B.A.
Dynamic surface properties of lysozyme solutions. Impact of urea and guanidine hydrochloride
Colloids Surf. B Biointerfaces
129
114-120
2015
Gallus gallus
Manually annotated by BRENDA team
Matano, M.; Nakajima, K.; Kashiwagi, Y.; Udaka, S.; Maehashi, K.
Sweetness characterization of recombinant human lysozyme
Comp. Biochem. Physiol. B
188
8-14
2015
Gallus gallus (P00698), Gallus gallus, Homo sapiens (P61626), Homo sapiens
Manually annotated by BRENDA team
Wu, T.; Jiang, Q.; Wu, D.; Hu, Y.; Chen, S.; Ding, T.; Ye, X.; Liu, D.; Chen, J.
What is new in lysozyme research and its application in food industry? A review
Food Chem.
274
698-709
2019
Gallus gallus
Manually annotated by BRENDA team
Guan, Y.F.; Lai, S.Y.; Lin, C.S.; Suen, S.Y.; Wang, M.Y.
Purification of lysozyme from chicken egg white using diatom frustules
Food Chem.
286
483-490
2019
Gallus gallus
Manually annotated by BRENDA team
Sheng, L.; Wang, J.; Huang, M.; Xu, Q.; Ma, M.
The changes of secondary structures and properties of lysozyme along with the egg storage
Int. J. Biol. Macromol.
92
600-606
2016
Gallus gallus
Manually annotated by BRENDA team
Oliveira Silva, C.; Petersen, S.B.; Pinto Reis, C.; Rijo, P.; Molpeceres, J.; Vorum, H.; Neves-Petersen, M.T.
Lysozyme photochemistry as a function of temperature. The protective effect of nanoparticles on lysozyme photostability
PLoS ONE
10
e0144454
2015
Gallus gallus
Manually annotated by BRENDA team
Floros, S.; Liakopoulou-Kyriakides, M.; Karatasos, K.; Papadopoulos, G.E.
Frequency dependent non-thermal effects of oscillating electric fields in the microwave region on the properties of a solvated lysozyme system A molecular dynamics study
PLoS ONE
12
e0169505
2017
Gallus gallus (P00698)
Manually annotated by BRENDA team
Yang, T.; Lesnierowski, G.
Changes in selected physicochemical properties of lysozyme modified with a new method using microwave field and oxidation
PLoS ONE
14
e0213021
2019
Gallus gallus
Manually annotated by BRENDA team
Sharma, P.; Verma, N.; Singh, P.K.; Korpole, S.; Ashish, S.
Characterization of heat induced spherulites of lysozyme reveals new insight on amyloid initiation
Sci. Rep.
6
22475
2016
Gallus gallus (P00698)
Manually annotated by BRENDA team
Tegl, G.; Oehlknecht, C.; Vielnascher, R.; Rollett, A.; Hofinger-Horvath, A.; Kosma, P.; Guebitz, G.
Cellobiohydrolases produce different oligosaccharides from chitosan
Biomacromolecules
17
2284-2292
2016
Gallus gallus (P00698)
Manually annotated by BRENDA team