Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.17 - lysozyme and Organism(s) Homo sapiens and UniProt Accession Q86SG7

for references in articles please use BRENDA:EC3.2.1.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q86SG7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
g-type lysozyme
-
Goose-type lysozyme
-
lysozyme g-like 2
-
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
-
-
-
-
hLYZ
-
-
L-7001
-
-
-
-
lambda lysozyme
-
-
Late protein gp15
-
-
-
-
Lysis protein
-
-
-
-
Lysosyme
-
-
-
-
Lysozyme
-
-
-
-
lysozyme g
-
-
-
-
mucopeptide glucohydrolase
-
-
-
-
mucopeptide N-acetylmuramoylhydrolase
-
-
-
-
muramidase
MV1 lysin
-
-
-
-
N,O-diacetylmuramidase
-
-
-
-
Outer wedge of baseplate protein
-
-
-
-
P13
-
-
-
-
Peptidoglycan hydrolase
-
-
-
-
PR1-lysozyme
-
-
-
-
Protein gp17
-
-
-
-
Protein gp19
-
-
-
-
Protein Gp25
-
-
-
-
Protein Gp5
-
-
-
-
Protein gp54
-
-
-
-
Protein gpK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
?
show the reaction diagram
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + 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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
activates, best at 75 mM
Ca2+
-
binding sites
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alginate
-
inactivation of the wild-type enzyme at high concentrations
DNA
-
inactivation of the wild-type enzyme at high concentrations
F-actin
-
inhibition of the wild-type enzyme
-
Hewli
-
-
-
lysozyme inhibitory protein Ivy
-
homodimeric antitoxin, inhibitor of vertebrate lysozyme, from Escherichia coli
-
mucin
-
inactivation of the wild-type enzyme at high concentrations
-
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
-
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
recombinant enzyme
5 - 6
-
-
5.9
-
wild-type enzyme, lytic activity against Micrococcus lysodeikticus
6
-
native enzyme and mutant enzyme _K1insN
6 - 7
-
the optimal pH of rHLZ varies with salt concentration of the buffer, recombinant enzyme
6.5
-
two-active site lysozyme, lytic activity against Micrococcus lysodeikticus
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
activity range, recombinant enzyme
5.4 - 7.2
-
wild-type and two-active site lysozyme both retain over 80% activity as determined by assaying the lysis of Micrococcus lysodeikticus cells over a pH range of 5.3 to 7.2
6.5 - 8.5
-
from pH 6.5-8.5, the rising of the pH results in decrease in lytic activity of native enzyme and mutant _K1insK, but not _K1insK
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
recombinant enzyme
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
weak enzyme expression in the conjuctival sample, strong expression in the lacrimal gland sample
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
leukemia patients
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
lysozyme plays an important role in human innate immunity by causing bacterial cell lysis. Recombinant HlysG2 inhibits Gram-positive bacterial growth, but does not inhibit Gram-negative bacterial and Candida albicans growth. HLysG2 is a potent antibacterial protein that may play a role in the innate immunity of the human eye
physiological function
additional information
-
the modified bovine milk is a possible substitute for human milk
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYG2_HUMAN
212
0
23498
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21508
x * 21508, sequence calculation
14000 - 16000
-
sedimentation velocity, short-column sedimentation equilibrium, amino acid analysis
14672
-
x * 14672, calculated
15000 - 17000
-
analytical ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 21508, sequence calculation
additional information
-
peptide mass fingerprinting of recombinant enzymes, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A83K/Q86D/A92D
-
decreased lytic activity at 1 mM CaCl2, but increased activity at 10 mM CaCl2
A92D
-
decreased lytic activity at 1 mM CaCl2
D102G
the mutant has 53% lytic activity and 47% chitinase activity compared to the wild type enzyme
D53N
the mutant shows complete loss of lytic and chitinase activities
E35Q
the mutant shows complete loss of lytic and chitinase activities
Q86D
-
decreased lytic activity at 1 mM CaCl2
Q86D/A92D
-
decreased lytic activity at 1 mM CaCl2, but increased activity at 10 mM CaCl2
R101D/R115H
-
the charge engineered variant's two mutated amino acids exhibit stabilizing interactions with adjacent native residues, the mutant shows severalfold increased activity compared to the wild-type enzyme, the mutations cause no gross structural perturbations or loss of stability, but dramatically expand the negative electrostatic potential that, in the wild-type enzyme, is restricted to a small region near the catalytic residues. Reduction in the overall strength of the engineered enzyme's electrostatic potential field, the specific nature of this remodeled field underlies the variant’s reduced susceptibility to inhibition by anionic biopolymers, overview. The double mutant lyses bacteria effectively at alginate, mucin and DNA concentrations that inactivate wild-type enzyme. The mutations does not substantially impair the enzyme’s Vmax or Km, has no effect on its in vitro anti-pseudomonal activity, and does not reduce lytic function
W109Q
the mutant has 55% lytic activity and 64% chitinase activity compared to the wild type enzyme
Y63Q
the mutant has 24% lytic activity and no chitinase activity compared to the wild type enzyme
_K1insA
-
the pH-profile is almost the same as that of native enzyme
_K1insK
-
the optimal pH-range is extended to higher pH-values in comparison to wild-type enzyme and mutant enzyme _K1insN. The mutant enzyme has significantly higher activity than native enzyme and _K1insN in higher ionic strength and in 150 mM NaCl. The mutant enzyme may be a useful antimicrobial agent
_K1insL
-
the pH-profile is almost the same as that of native enzyme
_K1insN
-
the pH-profile is almost the same as that of native enzyme
_K1insV
-
the pH-profile is almost the same as that of native enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 11
-
the recombinant enzyme retains more than 80% activity after 20 min at pH 2.0-11.0
751934
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
purified recombinant enzyme, 10 min, 50% activity remaining
37
-
35% residual activity after 4 days, pH 4
60
-
purified recombinant enzyme, 45 min, 95% activity remaining
60 - 100
-
15 min of treatment at 100°C disrupts almost all the antibacterial activity of the recombinant enzyme. Under 80°C, the recombinant enzyme can maintain about 60% of its activity for 15 min, and quickly loses the antibacterial activity after that. After incubation at 60°C for 45 min, the recombinant enzyme keeps 60% of its activity
additional information
-
human lysozyme more resistant to heat than chicken
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
no significant loss of the activity after 6 months of frozen storage for both wild-type and two-active site lysozyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Pichia pastoris strain GS115 by chitin affinity chromatography and gel filtration to homogeneity
CM-Sepharose column chromatography
leukemia lysozyme
-
recombinant enzyme from eggs of transgenic chicken, Hiscreen SP column chromatography, Mono S column chromatography, and Superdex 75 gel filtration
-
recombinant enzyme from transgenic cow milk, from which fat and casein has been removed for purification of the enzyme, by cation exchange chromatography and gel filtration to over 95% purity
-
recombinant enzyme fron Escherichia coli, molecular interactions between lysozyme and a His-tagged inhibitor Ivy allows for one-step purification by immobilized nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the mature peptide-coding region in Pichia pastoris strain GS115
2 different kinds of transgenic mice containing human lysozyme genomic DNA-based constructs with different signal peptide DNA are respectively established as system models
-
expressed in Gallus gallus eggs
-
expressed in Pichia pastoris
expression in goat at 67% of human breast milk
-
expression in Pichia pastoris
-
expression in Saccharomyces cerevisiae
-
expression of the enzyme in transgenic cattle, Bos taurus, as secreted enzyme in milk using the pBC2-HLY-NEOR transgene vector
-
gene hlyz, cloning in Escherichia coli strain JM105, optimization and evaluation of an efficient expression system capable of producing folded, soluble and functional human lysozyme in Escherichia coli, simultaneously co-expression of multiple protein folding chaperones as well as harnessing of the lysozyme inhibitory protein, Ivy, overview
-
lysozyme is amplified from bacteriophage lambda cDNA, recombinant enzyme expression in Escherichia coli strain DH5alpha
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
characterization of oligomers obtained after 5 days incubation at pH 3.0 and 60°C. Oligomers are misfolded species when compared to monomeric lysozyme, with a prevalence of random structure but with significant elements of the beta-sheet structure that is characteristic of the mature fibrils. The oligomeric lysozyme aggregates are more susceptible to proteolysis with pepsin than both the monomeric protein and the mature fibrils
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
establishment of a precise fluorimetric assay for determination and characterisation of lysozyme activity immobilised in the initial in situ formed pellicle. For in situ pellicle formation, bovine enamel slabs were fixed on maxillary splints and carried by six subjects for different times on buccal and palatal sites. The mean immobilised activity over all samples amounted to 68.67 U/cm2. The enzyme activity exposed at the pellicles' surfaces increases in a time-dependant manner and shows a Michaelis-Menten kinetic. Chlorhexidine and black tea reduce lysozyme activity of the in situ pellicle significantly
medicine
-
establishment of a precise fluorimetric assay for determination and characterisation of lysozyme activity immobilised in the initial in situ formed pellicle. For in situ pellicle formation, bovine enamel slabs were fixed on maxillary splints and carried by six subjects for different times on buccal and palatal sites. The mean immobilised activity over all samples amounted to 68.67 U/cm2. The enzyme activity exposed at the pellicles' surfaces increases in a time-dependant manner and shows a Michaelis-Menten kinetic. Chlorhexidine and black tea reduce lysozyme activity of the in situ pellicle significantly
nutrition
-
feeding of pigs with a diet of solid food and goat's milk of transgenic animals expressing human lysozyme results in fewer total coliforms and Escherichia coli in the ileum and in a greater duodenal width after infection with Escherichia coli. Control pigs receiving transgenic milk have fewer intraepithelial lymphocytes per micron of villi weight than animlas receiving control milk
synthesis
-
production of secreted recombinant human lysozyme by use of overexpression vector pPIC3.5k, carrying the strong promoter AOX1 of aldehyde oxidase 1, the HSA signal peptide, the enterokinase recognition motif, and the lysozyme gene. Mature protein is identical with native human lysozyme. It exhibits in vitro bacteriolytic activity against the Gram-positive bacterium Micrococcus lysodeikticus and the Gram-negative bacterium Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Castanon, M.J.; Spevak, W.; Adolf, G.R.; Chlebowicz-Sledziewska, E.; Sledtiewski, A.
Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae
Gene
66
223-234
1988
Homo sapiens
Manually annotated by BRENDA team
Hayakawa, T.; Toibana, A.; Marumoto, R.; Nakahama, K.; Kikuchi, M.; Fujimoto, K.; Ikehara, M.
Expression of human lysozyme in an insoluble form in yeast
Gene
56
53-59
1987
Homo sapiens
Manually annotated by BRENDA team
Wang, Ch.S.; Kloer, H.U.
Purification of human lysozyme from milk and pancreatic juice
Anal. Biochem.
139
224-227
1984
Homo sapiens
Manually annotated by BRENDA team
Yoshimoto, T.; Tobiishi, M.; Tsuru, D.
Affinity chromatographic purification of human lysozyme, with special reference to human leukemia lysozyme
J. Biochem.
80
703-709
1976
Homo sapiens
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
Barel, A.O.; Prieels, J.P.; Maes, E.; Looze, Y.; Leonis, J.
Comparative physicochemical studies of human alpha-lactalbumin and human lysozyme
Biochim. Biophys. Acta
257
288-296
1972
Homo sapiens
Manually annotated by BRENDA team
Canfield, R.E.; Kammerman, S.; Sobel, J.H.; Morgan, F.J.
Primary structure of lysozymes from man and goose
Nature New Biol.
232
16-17
1971
Anser sp., Homo sapiens
Manually annotated by BRENDA team
Balekjian, A.Y.; Hoerman, K.C.; Berzinskas, V.J.
Lysozyme of the human parotid gland secretion: its purification and physicochemical properties
Biochem. Biophys. Res. Commun.
35
887-894
1969
Homo sapiens
Manually annotated by BRENDA team
Parry, R.M.; Chandan, R.C.; Shahani, K.M.
Isolation and Characterization of human milk lysozyme
Arch. Biochem. Biophys.
103
59-65
1969
Homo sapiens
Manually annotated by BRENDA team
Kuroki, R.; Yutani, K.
Structural and thermodynamic responses of mutations at a Ca2+ binding site engineered into human lysozyme
J. Biol. Chem.
273
34310-34315
1998
Homo sapiens
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
Kikuchi, M.; Ikehara, M.
From genesis to function of proteins: investigation of general principles by engineering human lysozyme
Protein Eng.
7
735-742
1994
Homo sapiens
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
Li, S.; Li, B.; Fei, Y.; Jiang, D.; Sheng, Y.; Sun, Y.; Zhang, J.
Exon grafting yields a "two active-site" lysozyme
Biochem. Biophys. Res. Commun.
358
997-1001
2007
Homo sapiens
Manually annotated by BRENDA team
Leon-Sicairos, N.; Lopez-Soto, F.; Reyes-Lopez, M.; Godinez-Vargas, D.; Ordaz-Pichardo, C.; de la Garza, M.
Amoebicidal activity of milk, apo-lactoferrin, sIgA and lysozyme
Clin. Med. Res.
4
106-113
2006
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Yu, Z.; Meng, Q.; Yu, H.; Fan, B.; Yu, S.; Fei, J.; Wang, L.; Dai, Y.; Li, N.
Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice
J. Dairy Sci.
89
2911-2918
2006
Homo sapiens
Manually annotated by BRENDA team
Tsuchiya, Y.; Morioka, K.; Yoshida, K.; Shirai, J.; Kokuho, T.; Inumaru, S.
Effect of N-terminal mutation of human lysozyme on enzymatic activity
Nucleic Acids Symp. Ser.
51
465-466
2007
Homo sapiens
Manually annotated by BRENDA team
Lin, K.C.; Wey, M.T.; Kan, L.S.; Shiuan, D.
Characterization of the interactions of lysozyme with DNA by surface plasmon resonance and circular dichroism spectroscopy
Appl. Biochem. Biotechnol.
158
631-641
2009
Homo sapiens (P61626), Homo sapiens
Manually annotated by BRENDA team
Xiong, R.; Chen, J.; Chen, J.
Secreted expression of human lysozyme in the yeast Pichia pastoris under the direction of the signal peptide from human serum albumin
Biotechnol. Appl. Biochem.
51
129-134
2008
Homo sapiens
Manually annotated by BRENDA team
Hannig, C.; Spitzmueller, B.; Hannig, M.
Characterisation of lysozyme activity in the in situ pellicle using a fluorimetric assay
Clin. Oral Investig.
13
15-21
2009
Homo sapiens
Manually annotated by BRENDA team
Frare, E.; Mossuto, M.F.; de Laureto, P.P.; Tolin, S.; Menzer, L.; Dumoulin, M.; Dobson, C.M.; Fontana, A.
Characterization of oligomeric species on the aggregation pathway of human lysozyme
J. Mol. Biol.
387
17-27
2009
Homo sapiens
Manually annotated by BRENDA team
Brundige, D.R.; Maga, E.A.; Klasing, K.C.; Murray, J.D.
Lysozyme transgenic goats milk influences gastrointestinal morphology in young pigs
J. Nutr.
138
921-926
2008
Homo sapiens
Manually annotated by BRENDA team
Huang, P.; Li, W.S.; Xie, J.; Yang, X.M.; Jiang, D.K.; Jiang, S.; Yu, L.
Characterization and expression of HLysG2, a basic goose-type lysozyme from the human eye and testis
Mol. Immunol.
48
524-531
2011
Homo sapiens (Q86SG7), Homo sapiens
Manually annotated by BRENDA team
Gill, A.; Scanlon, T.C.; Osipovitch, D.C.; Madden, D.R.; Griswold, K.E.
Crystal structure of a charge engineered human lysozyme having enhanced bactericidal activity
PLoS ONE
6
e16788
2011
Homo sapiens
Manually annotated by BRENDA team
Yang, B.; Wang, J.; Tang, B.; Liu, Y.; Guo, C.; Yang, P.; Yu, T.; Li, R.; Zhao, J.; Zhang, L.; Dai, Y.; Li, N.
Characterization of bioactive recombinant human lysozyme expressed in milk of cloned transgenic cattle
PLoS ONE
6
e17593
2011
Homo sapiens
Manually annotated by BRENDA team
Lamppa, J.W.; Tanyos, S.A.; Griswold, K.E.
Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme
J. Biotechnol.
164
1-8
2013
Homo sapiens
Manually annotated by BRENDA team
Pham, E.; Truong, K.
Engineered regulation of lysozyme by the SH3-CB1 binding interaction
Protein Eng. Des. Sel.
25
307-311
2012
Homo sapiens
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, H.; Cao, D.; Liu, T.; Zhao, J.; Hu, X.; Li, N.
Purification and characterization of recombinant human lysozyme from eggs of transgenic chickens
PLoS ONE
10
e0146032
2015
Homo sapiens
Manually annotated by BRENDA team