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(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
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
cell wall of Bacillus subtilis + H2O
?
-
-
-
-
?
cell wall of Escherichia coli + H2O
?
cell wall of Micrococcus luteus + H2O
?
cell wall of Micrococcus lysodeikticus + H2O
?
cell wall of Streptococcus agalactiae + H2O
?
-
-
-
-
?
cell wall of Vibrio alginolyticus + H2O
?
-
-
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by mass and NMR spectrometry
-
-
?
chitohexaose + H2O
?
-
-
-
?
chitohexaose + H2O
chitobiose + chitotetraose
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
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA48
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
colloidal chitin + H2O
?
-
-
-
-
?
ethylene glycol chitin + H2O
?
ethylene glycol chitin + H2O
sugars
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
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
L-gamma-glutamine-4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
-
substrate for isopeptidase activity of isoform cLys3
-
-
?
lyophilized cell wall of Micrococcus luteus + H2O
?
lyophilized cell walls of Micrococcus lysodiekticus + H2O
?
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
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',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
-
-
?
NodRm-IV + H2O
NodRm-II + NodRm-III
-
-
-
?
NodRm-IV(Ac,S) + H2O
NodRm-II + NodRm-III
-
-
-
?
NodRm-IV(S) + H2O
NodRm-II + NodRm-III
-
-
-
?
NodRm-V(S) + H2O
NodRm-II + NodRm-III
-
-
-
?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
?
-
-
-
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
peptidoglycan + H2O
N-acetylaminosaccharides
additional information
?
-
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

?
-
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
-
-
-
-
?
cell wall of Escherichia coli + H2O

?
-
-
-
-
?
cell wall of Escherichia coli + H2O
?
-
-
-
-
?
cell wall of Micrococcus luteus + H2O

?
-
-
-
?
cell wall of Micrococcus luteus + H2O
?
-
-
-
?
cell wall of Micrococcus luteus + H2O
?
-
substrate for muramidase activity of isoform cLys3
-
-
?
cell wall of Micrococcus luteus + H2O
?
-
-
-
?
cell wall of Micrococcus luteus + H2O
?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O

?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
-
-
-
-
?
cell wall of Micrococcus lysodeikticus + H2O
?
-
-
-
-
?
chitin + H2O

sugars
-
-
-
-
?
chitin + H2O
sugars
-
-
reducing
?
chitohexaose + H2O

chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
chitohexaose + H2O
chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
chitohexaose + H2O
chitobiose + chitotetraose
-
-
mass spectrometry analysis
-
?
chitopentaose + H2O

?
-
-
-
?
chitopentaose + H2O
?
-
-
-
-
?
chitotetraose + H2O

chitotriose + N-acetylglucosamine
-
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
-
-
-
?
colloidal chitin

sugars
-
-
-
-
?
colloidal chitin
sugars
-
-
-
-
?
ethylene glycol chitin + H2O

?
-
-
-
?
ethylene glycol chitin + H2O
?
-
-
-
?
ethylene glycol chitin + H2O

sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
-
-
reducing
?
glycol chitin + H2O

?
-
-
-
-
?
glycol chitin + H2O
?
-
-
-
?
glycol chitin + H2O

chitin oligosaccharides
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
-
-
reducing
?
lyophilized cell wall of Micrococcus luteus + H2O

?
-
-
-
?
lyophilized cell wall of Micrococcus luteus + H2O
?
-
-
-
?
lyophilized cell wall of Micrococcus luteus + H2O
?
-
-
-
?
lyophilized cell wall of Micrococcus luteus + H2O
?
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O

?
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
-
-
-
-
?
Micrococcus lysodeikticus cell wall + H2O
?
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O

?
-
-
-
-
?
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
?
-
-
-
-
?
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
?
-
-
-
?
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
?
-
lyophilized cell wall of Micrococcus luteus
-
-
?
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
?
-
Micrococcus lysodeikticus cells
-
-
?
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
?
-
-
-
-
?
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
?
-
-
-
?
peptidoglycan + H2O
?
-
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
?
-
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
?
-
cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
-
-
?
peptidoglycan + H2O
?
-
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
?
-
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
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
?
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
?
-
lysis of Micrococcus lysodeikticus cells
-
-
?
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
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
?
peptidoglycan + H2O
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
anti-tumor activity
-
-
?
peptidoglycan + H2O
?
-
involvement in host defence
-
-
?
peptidoglycan + H2O
?
-
anti-metastatic activity
-
-
?
peptidoglycan + H2O
?
-
lytic activity against Micrococcus lysodeikticus
-
-
?
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
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
peptidoglycan + H2O
?
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
-
digestive enzyme
-
-
?
peptidoglycan + H2O
?
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
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
?
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
-
lytic activity against Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
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
-
-
C3 and C6 muropeptides
?
peptidoglycan + H2O
N-acetylaminosaccharides
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
-
-
-
-
?
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
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
often acts as chitinase: EC 3.2.1.14
-
-
?
additional information
?
-
-
lysozyme is able to kill Entamoeba histolytica trophozoites
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
high chitinase activity
-
-
?
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
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-
?
additional information
?
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-
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
-
-
?
additional information
?
-
-
Micrococcus luteus
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
cell walls of Micrococcus lysodeikticus, are a substrate, while those of Xanthomonas campestris pv. malvacearum and Xanthomonas oryzae pv. oryzae are no substrates
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus luteus
-
-
?
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
?
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-
lysis of Micrococcus lysodeikticus
-
-
?
additional information
?
-
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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
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus luteus
-
-
?
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
?
-
-
AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis
-
-
?
additional information
?
-
-
LycGL may be involved in antibacterial immune response activated by bacterial vaccine as an accute-phase molecule
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
not: Micrococcus luteus cells
-
-
?
additional information
?
-
the enzyme shows lytic activity towards Micrococcus lysodeikticus
-
-
?
additional information
?
-
-
the enzyme shows lytic activity towards Micrococcus lysodeikticus
-
-
?
additional information
?
-
recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
not: p-nitrophenyl-N-acetylglucosaminide
-
-
?
additional information
?
-
-
Micrococcus luteus
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
enzyme exhibits potent lytic activities against fish pathogens
-
-
?
additional information
?
-
-
enzyme exhibits potent lytic activities against fish pathogens
-
-
?
additional information
?
-
the recombinant enzyme displays the lytic activity of g-type lysozyme with other organisms against Micrococcus lysodikicus
-
-
?
additional information
?
-
-
the recombinant enzyme displays the lytic activity of g-type lysozyme with other organisms against Micrococcus lysodikicus
-
-
?
additional information
?
-
-
pyocinogenic: no activity towards intact cells of gram-negative and gram-positive bacteria, lysis of chloroform-killed gram-negative and gram-positive bacteria
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
gram-negative bacteria better substrate than gram-positive bacteria
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filĆfformis
-
-
?
additional information
?
-
Thermus virus IN93 phiIN93
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filĆfformis
-
-
?
additional information
?
-
-
often acts as chitinase: EC 3.2.1.14
-
-
?
additional information
additional information
-
cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues
formation of a 1,6-anhydromuramoyl product
-
?
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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-[(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
Ag+
-
0.01 mM, 7% inhibition
alginate
-
inactivation of the wild-type enzyme at high concentrations
Bacillus subtilis DNA
-
in presence of 0-50 mM NaCl
-
c-type inhibitor Ivy
complete inhibition
-
Ca2+
34% activation at 5 mM, 150% activation at 10 mM, 280% at 5 mM of recombinant enzyme. 58% Inhibition at 10 mM, 97% at 50 mM of native enzyme, 66% inhibition at 20 mM, 97% at 50 mM of recombinant enzyme; 87% inhibition at 5 mM, 93% at 10 mM
F-actin
-
inhibition of the wild-type enzyme
-
g-type inhibitor PliG
complete inhibition
-
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
-
inhibitor of vertebrate lysozyme
-
lipoprotein
-
lipoprotein in bound form, in presence of 0-5 mM NaCl
-
lysozyme inhibitory protein Ivy
-
homodimeric antitoxin, inhibitor of vertebrate lysozyme, from Escherichia coli
-
mucin
-
inactivation of the wild-type enzyme at high concentrations
-
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
N-bromosuccinimide
-
pH 4
Na+
14% inhibition at 10 mM, 81% at 100 mM; activates the native enzyme 3.43fold at 50 mM, the recombinant enzyme 4.3fold at 100 mM, inhibition of native, not recombinant, enzyme at 200 mM
Nuclear lysozyme inhibitor
-
other subcellular lysozymes except nuclear are unaffected
-
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
-
PliI
-
periplasmic lysozyme inhibitor of the I-type lysozyme from Aeromonas hydrophila has a high affinity for I-type lysozyme, but does not bind or inhibit vertebrate C- or G-type lysozymes
-
poly-alpha,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
poly-gamma,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
potassium hyaluronate
-
in presence of 0-5 mM NaCl
RNA
-
yeast RNA in presence of 0-50 mM NaCl
Sodium citrate
-
above 0.1 M
(GlcNAc)3

-
chitotetraose

-
-
CoCl2

-
10 mM
CuSO4

-
10 mM
DNA

-
DNA from herring sperm, in presence of 0-50 mM NaCl
DNA
-
inactivation of the wild-type enzyme at high concentrations
EDTA

-
-
EDTA
at 10 and 20 mM causes 15% and 43% reduction of the enzyme activity
Hewli

-
-
-
histamine

Ficus sp.
-
-
inhibitor of vertebrate lysozyme

Escherichia coli inhibitor of vertebrate lysozyme. Electrostatic interactions makes a dominant contribution to inhibition. Weaker binding mode between Ivy and goose lysozyme compared to hen lysozyme
-
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
-
Ivy

-
lysozyme inhibitor from Escherichia coli, strong inhibition
-
Ivy
-
lysozyme inhibitor from Escherichia coli, strong inhibition
-
Ivy
-
lysozyme inhibitor from Escherichia coli, strong inhibition
-
MgCl2

-
-
MliC

i.e. membrane bound lysozyme inhibitor of C-type lysozyme, crystallization data in complex with chicken egg white lysozyme. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues
-
MliC
i.e. membrane bound lysozyme inhibitors of c-type lysozyme, isolated from Escherichia coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in Escherichia coli. Related to a group of proteins with a common conserved COG3895 domain
-
Mn2+

-
0.01 M, 17% inhibition
N-acetylglucosamine

-
-
N-acetylglucosamine
Ficus sp.
-
-
NaCl

-
almost complete inhibition at 0.8 M
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
-
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
-
ZnCl2

-
10 mM
ZnCl2
-
inhibits at 2-30 mM
additional information

-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
the purified recombinant enzyme is resistant to pepsin and trypsin to some extent at 40°C
-
additional information
-
the enzyme shows resistance to proteolysis
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Grame-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
study on the inhibitory effect on the enzymatic activity of lysozyme of a number of peptides each containing about 10 amino acids and overlapping exhaustively the protein sequence. A small fraction of them are able to inhibit the biological activity of the protein with micromolar efficiency. The peptide displaying the same sequence of segment 91-100 of the protein, and essentially corresponding to the last three turns of helix C, is the most efficient. The inhibitory mechanism is nonconventional. Local elementary structures formed in the denatured state, drive the folding process and selected peptides compete with these structures in binding complementary regions of the protein, preventing the formation of the native state
-
additional information
-
interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM
-
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
-
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
-
additional information
-
design and construction, based on the protein structures of lambda lysozyme and the SH3 domain of human Crk, of a synthetic protein switch that controls the activity of lysozyme by sterically hindering its active cleft through the binding of SH3 to its CB1 peptide-binding partner, i.e. fusion proteins Venus-CB1-lysozyme, Venus-CB1-lysozyme-CB1, Venus-CB1 and His-nSH3C. Modelling of fusion protein designs with lysozyme and CB1, in the absence of SH3, the lysozyme-CB1 fusion protein functions normally. In the presence of SH3, the lysozyme activity is inhibited and with the addition of excess CB1 peptides to compete for SH3 binding, the lysozyme activity is restored
-
additional information
-
bacterial membrane proton motive force regulates the lytic activity of the secreted endolysin Lys44 from Oenococcus oeni phage fOg44. Cytoplasmic membrane voltage dissipation is necessary but not sufficient for the full sensitization of cells to Lys44
-
additional information
-
Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory
-
additional information
no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG
-
additional information
no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG
-
additional information
-
no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
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