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
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3.2.1.17
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albumin
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immunoglobulin
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lactoferrin
-
lytic
-
neutrophil
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phagocytic
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staphylococcus
-
lymphocyte
-
bacteriophage
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streptococcus
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leukocyte
-
aureus
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bactericidal
-
saliva
-
amyloid
-
iga
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nanoparticles
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myeloperoxidase
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ribonuclease
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phagocytosis
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fibril
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humoral
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film
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histiocytic
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micrococcus
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aeromonas
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tear
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myoglobin
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granulocyte
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chitosan
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hydrophila
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polymorphonuclear
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hydrogel
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mucus
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aquaculture
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probiotic
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immune-related
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alpha-lactalbumins
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pneumococcal
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carp
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hemocytes
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methacrylate
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amyloidosis
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sarcoidosis
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tilapia
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penicillin-binding
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lactoperoxidase
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amyloidogenic
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phenoloxidase
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1-antitrypsin
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agriculture
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industry
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analysis
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nutrition
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food industry
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synthesis
-
medicine
- 3.2.1.17
- albumin
- immunoglobulin
- lactoferrin
-
lytic
- neutrophil
- phagocytic
- staphylococcus
- lymphocyte
- bacteriophage
- streptococcus
- leukocyte
- aureus
-
bactericidal
- saliva
-
amyloid
- iga
- nanoparticles
- myeloperoxidase
- ribonuclease
-
phagocytosis
-
fibril
-
humoral
-
film
- histiocytic
- micrococcus
- aeromonas
- tear
- myoglobin
- granulocyte
- chitosan
- hydrophila
-
polymorphonuclear
- hydrogel
- mucus
-
aquaculture
-
probiotic
-
immune-related
- alpha-lactalbumins
- pneumococcal
- carp
- hemocytes
- methacrylate
- amyloidosis
- sarcoidosis
- tilapia
-
penicillin-binding
- lactoperoxidase
-
amyloidogenic
- phenoloxidase
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1-antitrypsin
- agriculture
- industry
- analysis
- nutrition
- food industry
- synthesis
- medicine
Reaction
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
3.2.1.17 lysozymeAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.17 - lysozyme
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(GlcNAc)6 + H2O
(GlcNAc)3
-
-
and smaller amounts of (GlcNAc)2 and (GlcNAc)4 endo-splitting, hydrolyzes preferentially the third glycosidic linkage from the nonreducing end
-
?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by mass and NMR spectrometry
-
-
?
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotetraose + chitotriose
-
amount in descending order, binding kinetics with chitotriose, overview
-
?
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotriose + chitotetraose
-
amount in descending order, binding kinetics with chitotriose, overview
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + (GlcNAc)2
-
-
main products
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ?
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
-
-
?
L-gamma-glutamine-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
substrate for isopeptidase activity of isoform cLys3
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
eight amino acid residues interact with the N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose oligomer: Arg73, Gly102, Asn103, Leu56, Ala107, Val109, Ala110, and Lys33
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose
-
wild-type protein hydrolyzes N,N',N'',N''',N''''-pentaacetylchitopentaose almost completely on 140 min reaction. N,N',N'',N'''-tetraacetylchitotetraose is is hydrolyzed mainly to N,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose with much less cleavage into GlcNAc + N,N',N'',N'''-tetraacetylchitotetraose
-
-
?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
?
-
-
-
-
?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
-
a synthetic fluorogenic substrate
-
-
?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
-
a synthetic fluorogenic substrate
-
-
?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
-
a synthetic fluorogenic substrate
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
-
-
-
-
?
cell wall of Micrococcus luteus + H2O
?
-
substrate for muramidase activity of isoform cLys3
-
-
?
chitohexaose + H2O
chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
chitohexaose + H2O
chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
chitohexaose + H2O
chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
the enzyme shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila
-
-
?
peptidoglycan + H2O
?
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Pseudomonas aeruginosa, Escherichia coli, Salmonella typhimurium and Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Shigella flexneri become sensitive to lysozyme under high pressure, Salmonella typhimurium and E. coli 0157:H7 remain completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Escherichia coli, Micrococcus lysodeikticus, Salmonella typhimurium and Pseudomonas aeruginosa
-
-
?
peptidoglycan + H2O
?
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli 0157:H7 become sensitive to lysozyme under high pressure. Salmonella typhimurium and Shigella flexneri remain completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
-
enzyme displays lytic activity against Micrococcus lysodeikticus, Staphylococcus aureus and Escherichia coli
-
-
?
peptidoglycan + H2O
?
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
-
cell wall of Micrococcus luteus. Tyr34, Tyr45, Pro47, Pro102, and Asn114 are the amino acids contributing to the substrate binding
-
-
?
peptidoglycan + H2O
?
-
the enzyme shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila
-
-
?
peptidoglycan + H2O
?
-
murein hydrolase, highly specific towards cell walls of Clostridium perfringens strains, endolysin Ply3626 has an N-terminal N-acetylmuramoyl-L-alanine amidase domain and a unique C-terminal portion, which might be responsible for the specific lytic range of enzyme
-
-
?
peptidoglycan + H2O
?
-
enzyme displays lytic activity against Lactococcus garvieae, Enterococcus sp., Vibrio vulnificus and Escherichia coli. The growth of Aeromonas hydrophila is inhibited only at a high concentration of 0.4 mg/ml. No growth inhibition of Streptococcus iniae and Aeromonas hydrophila
-
-
?
peptidoglycan + H2O
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Micrococcus lysodeikticus, Salmonella typhimurium, Yersinia enterolitica, Pseudomonas aeruginosa and Escherichia coli
-
-
?
peptidoglycan + H2O
?
-
lytic activity against Micrococcus lysodeiktikus cells
-
-
?
peptidoglycan + H2O
?
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Escherichia coli 0157:H7 and Yersinia enterolytica become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
-
the enzyme cleaves the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine of bacterial cell wall peptidoglycans
-
-
?
peptidoglycan + H2O
?
-
lytic activity against Micrococcus lysodeiktikus cells
-
-
?
peptidoglycan + H2O
?
-
LysgaY lysed over 20 heated Gram-positive bacterial species as the substrates, including lactobacilli, lactococci, enterococci, micrococci, and staphylococci
-
-
?
peptidoglycan + H2O
?
AcmB is an N-acetylglucosaminidase autolysin, three-domain modular structure, hydrolyzes peptidoglycans of several Gram-positive bacteria including Lactococcus lactis, AcmB hydrolyzes the peptidoglycan bonds in Bacillus subtilis HR vegetative cells between N-acetylglucosamine and N-acetylmuramic acid thus being an N-acetylglucosaminidase
-
-
?
peptidoglycan + H2O
?
Lambdavirus lambda
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Salmonella typhimurium, Pseudomonas aeruginosa, Escherichia coli and Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
Lambdavirus lambda
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica, Shigella flexneri and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
-
the enzyme form SSTL A shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila
-
-
?
peptidoglycan + H2O
?
-
the enzyme form SSTL B shows lytic activity against several species of bacteria, such as Micrococcus luteus and Vibrio cholerae, but shows only weak activity to Pseudomonas aeruginosa and lacks activity towards Aeromonas hydrophila
-
-
?
peptidoglycan + H2O
?
-
the Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. The Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity
-
-
?
peptidoglycan + H2O
?
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Escherichia coli, Pseudomonas aeruginosa, Salmonella typhimurium, Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium and Shigella flexneri remain completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
-
lytic activity against Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
Tequatrovirus T4
-
cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
-
-
?
peptidoglycan + H2O
?
Tequatrovirus T4
-
enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Salmonella typhimurium, Micrococcus lysodeikticus, Pseudomonas aeruginosa and Escherichia coli
-
-
?
peptidoglycan + H2O
?
Tequatrovirus T4
-
lytic activity with cells of Gram-positive bacteria: Enterococcus faecalis, Bacillus subtilis, Listeria innocua, Staphylococcus aureus and Micrococcus lysodeikticus cells. No activity on Gram-negative bacteria. Pseudomonas aeruginosa, Yersinia enterolytica and Escherichia coli become sensitive to lysozyme under high pressure. Salmonella typhimurium remains completely insensitive to lysozyme
-
-
?
peptidoglycan + H2O
?
the enzyme is active against both Xanthomonas and Stenotrophomonas maltophilia. Only a minor portion of the Escherichia coli cells is lysed. Cells of Micococcus lysodeikticus, Bacillus subtilis, Agrobacterium tumefaciens, and Psuedomonas fluorescens exhibit no signifiant lysis
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
Tequatrovirus T4
-
-
C3 and C6 muropeptides
?
additional information
?
-
-
the enzyme also has isopeptidase activity with 4-nitroanilide-L-gamma-glutamic acid
-
-
?
additional information
?
-
-
the purified recombinant enzyme shows antibacterial activity against several different strains, e.g. Aspergillus oryzae, Bacillus subtilis 168, Bacillus cereus, Clostridium sporogenes, Micrococcus luteus, Micrococcus lysodeikticus, Pseudomonas aeruginosa, Salmonella typhimurium, Saccharomyces cerevisiae, Staphyloccocus aureus, and Streptococcus pneumoniae
-
-
?
additional information
?
-
-
the purified recombinant enzyme shows antibacterial activity against several different strains, e.g. Aspergillus oryzae, Bacillus subtilis 168, Bacillus cereus, Clostridium sporogenes, Micrococcus luteus, Micrococcus lysodeikticus, Pseudomonas aeruginosa, Salmonella typhimurium, Saccharomyces cerevisiae, Staphyloccocus aureus, and Streptococcus pneumoniae
-
-
?
additional information
?
-
-
lysozyme has inhibitory effects on the proliferation of vascular endothelial cell in vitro
-
-
?
additional information
?
-
-
lysozyme is able to kill Entamoeba histolytica trophozoites
-
-
?
additional information
?
-
-
cell walls of Clostridium acetobulyticum, not: Micrococcus cells, beta-N-acetyl chitotetraoside
-
-
?
additional information
?
-
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
-
-
?
additional information
?
-
-
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
-
-
?
additional information
?
-
-
lysozyme inhibits Clostridium perfringens type A and its alpha-toxin production
-
-
?
additional information
?
-
measurement of activity by lytic activity against Micrococcus luteus
-
-
?
additional information
?
-
-
antimicrobial activities of lysozyme derivatives are tested against Staphylococcus aureus ATCC 121002 and Escherichia coli ATCC 29998, as gram-positive and gram-negative representatives, respectively. The enzyme is activa against Staphylococcus aureus, but only poorly against Escherichia coli, overview
-
-
?
additional information
?
-
-
a suspension of Micrococcus lysodeikticus is used as a substrate
-
-
?
additional information
?
-
-
interaction between gold nanorods and lysozyme as moddel protein, the enzyme retains a high fraction of its native structure with a slight increase in the helical content at the expense of beta-turns. Comparison of the gold nanorod treated lysozyme with free enzyme reveals higher thermodynamic stability under denaturing condition. The enzyme's integrity gains more conformational stability in the vicinity of gold nanorods while its lytic activity does not show any undesirable change
-
-
?
additional information
?
-
-
Micrococcus luteus cells in the exponential growth phase are used as substrate
-
-
?
additional information
?
-
-
dry-heated lysozyme has increased activity against Escherichia coli membranes compared to native lysozyme, overview. The latter only delays bacterial growth, while dry-heated lysozyme causes an early-stage population decrease. Escherichia coli K-12 strain MG1655 Ivy::Cm, which lacks the periplasmic lysozyme inhibitor Ivy, is utilized
-
-
?
additional information
?
-
-
a commercial cell suspension of Oenococcus oeni, an oenological strain involved in the winemaking process, is utilized as enzyme substrate
-
-
?
additional information
?
-
-
the enzyme is lytically active on Micrococcus luteus suspension
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
-
the enzyme shows antibacterial activity by growth inhibition of a target organism Planococcus citreus
-
-
?
additional information
?
-
-
substrate are lyophilized Micrococcus lysodeikticus cell walls on lysoplates
-
-
?
additional information
?
-
recombinantly expressed enzyme shows strong lytic activity against Micrococcus lysodeikticus, isopeptidase activity, and antibacterial activity against several Gram-positive and Gram-negative bacteria
-
-
?
additional information
?
-
-
recombinantly expressed enzyme shows strong lytic activity against Micrococcus lysodeikticus, isopeptidase activity, and antibacterial activity against several Gram-positive and Gram-negative bacteria
-
-
?
additional information
?
-
-
i-type lysozyme isoform iLys2 does not exhibit muramidase, isopeptidase or serine hydrolase activities
-
-
?
additional information
?
-
-
the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
-
-
?
additional information
?
-
-
the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
-
-
?
additional information
?
-
-
the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
-
-
?
additional information
?
-
-
lysozyme is able to kill Entamoeba histolytica trophozoites
-
-
?
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. Lysozyme may represent part of the innate immune system with a very broad protective spectrum
-
-
?
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. Lysozyme may represent part of the innate immune system with a very broad protective spectrum
-
-
?
additional information
?
-
a suspension of Micrococcus lysodeikticus is used as a substrate for HLysG2
-
-
?
additional information
?
-
-
a suspension of Micrococcus lysodeikticus is used as a substrate for HLysG2
-
-
?
additional information
?
-
-
lysis of Micrococcus luteus bacteria, the double mutant lyses bacteria effectively at alginate, mucin and DNA concentrations that inactivate wild-type enzyme
-
-
?
additional information
?
-
-
the enzyme shows lytic activity against freeze-dried Micrococcus luteus cells
-
-
?
additional information
?
-
recombinant CC-Lys-g produced in Escherichia coli expression system exhibits significant lytic activity against Gram-positive Micrococcus lysodeikticus and Gram-negative Aeromonas hydrophila
-
-
?
additional information
?
-
-
recombinant CC-Lys-g produced in Escherichia coli expression system exhibits significant lytic activity against Gram-positive Micrococcus lysodeikticus and Gram-negative Aeromonas hydrophila
-
-
?
additional information
?
-
enzyme substrate is lyophilized Micrococcus lysodeikticus
-
-
?
additional information
?
-
-
enzyme substrate is lyophilized Micrococcus lysodeikticus
-
-
?
additional information
?
-
AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis
-
-
?
additional information
?
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AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis
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?
additional information
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LycGL may be involved in antibacterial immune response activated by bacterial vaccine as an accute-phase molecule
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?
additional information
?
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Lederbergvirus P22
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gram-negative bacteria better substrate than gram-positive bacteria
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?
additional information
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the enzyme shows also chitinase activity on glycol chitin as substrate, but no transglycosylation activity, and a higher number of subsites compared to hen egg-white enzyme
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?
additional information
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the enzyme shows lytic activity towards Micrococcus lysodeikticus
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?
additional information
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the enzyme shows lytic activity towards Micrococcus lysodeikticus
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?
additional information
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recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria
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?
additional information
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comparison of the lytic activities of three recombinant g-type lysozyme isozymes, OHLysG1, OHLysG2 and OHLysG3 against Aeromonas hydrophila, Aeromonas sobria, Vibrio fluvialis, Micrococcus lysodeikticus and Escherichia coli, overview
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?
additional information
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not: p-nitrophenyl-N-acetylglucosaminide
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?
additional information
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enzyme exhibits potent lytic activities against fish pathogens
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?
additional information
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enzyme exhibits potent lytic activities against fish pathogens
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?
additional information
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the recombinant enzyme displays the lytic activity of g-type lysozyme with other organisms against Micrococcus lysodikicus
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?
additional information
?
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the recombinant enzyme displays the lytic activity of g-type lysozyme with other organisms against Micrococcus lysodikicus
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?
additional information
?
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pyocinogenic: no activity towards intact cells of gram-negative and gram-positive bacteria, lysis of chloroform-killed gram-negative and gram-positive bacteria
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?
additional information
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Glu18 and Asp30 are the catalytic residues of TJL. The catalytic mechanism of TJL is a retaining mechanism that proceeds through a covalent sugar-enzyme intermediate
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?
additional information
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the enzyme shows lytic activity against Micrococcus lysodeikticus, the recombinant enzyme shows antibacterial activity against both Gram-positive and Gram-negative bacteria, including Vibrio alginolyticus, Vibrio harveyi, Vibrio anguillarum, Escherichia coli, Bacillus subtilis, and Micrococcus lysodeikticus
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?
additional information
?
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the enzyme shows lytic activity against Micrococcus lysodeikticus, the recombinant enzyme shows antibacterial activity against both Gram-positive and Gram-negative bacteria, including Vibrio alginolyticus, Vibrio harveyi, Vibrio anguillarum, Escherichia coli, Bacillus subtilis, and Micrococcus lysodeikticus
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?
additional information
?
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Tequatrovirus T4
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phage T4: e lysozyme more specific than hen egg-white lysozyme, e lysozyme: hydrolysis of murein chains in which N-acetylmuraminic acid is substituted by peptide side chains L-Ala-D-Glu-meso-diaminopimelic acid-D-Ala
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?
additional information
?
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Tequatrovirus T4
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cell walls of Micrococcus lysodeikticus, are a substrate, while those of Xanthomonas campestris pv. malvacearum and Xanthomonas oryzae pv. oryzae are no substrates
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?
additional information
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enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
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?
additional information
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Thermus virus IN93 phiIN93
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
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?
