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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
?
-
-
-
-
?
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
?
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
?
-
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
?
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
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
Tequatrovirus T4
-
-
C3 and C6 muropeptides
?
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
-
-
?
additional information
?
-
-
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
?
-
-
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
?
-
-
lysis of Micrococcus lysodeikticus
-
-
?
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
?
-
-
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
?
-
Lederbergvirus P22
-
gram-negative bacteria better substrate than gram-positive bacteria
-
-
?
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
?
-
-
Micrococcus lysodeikticus cells
-
-
?
additional information
?
-
Tequatrovirus T4
-
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
?
-
Tequatrovirus T4
-
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
?
-
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
?
additional information
?
-
Thermus virus IN93 phiIN93
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
?
additional information
?
-
-
often acts as chitinase: EC 3.2.1.14
-
-
?
additional information
additional information
-
Phikzvirus phiKZ
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
-
KCl
Lederbergvirus P22
-
-
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
Tequatrovirus T4
-
lysozyme inhibitor from Escherichia coli, strong inhibition
-
MgCl2
Lederbergvirus P22
-
-
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
NaCl
Lederbergvirus P22
-
-
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
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
Lambdavirus lambda
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
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
-
additional information
Tequatrovirus T4
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
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evolution
-
evolutionary relationships of isozymes OHLysG1, OHLysG2 and OHLysG3 with other animal lysozymes, and phylogenetic tree
evolution
phylogenetic analysis, the enzyme shares a similar origin with the bacterial phage-type lysozyme group
evolution
the conservative structure domains share high homology with other molluscan g-type lysozymes including the SLT domain, the substrate binding sites, the catalytic residues, three alpha-helices structures and six molluscan specific cysteines
physiological function
-
human lysozyme is a key component of the innate immune system. But the wild type protein fails to participate effectively in clearance of certain infections due to inherent functional limitations. For example, wild type lysozymes are subject to electrostatic sequestration and inactivation by anionic biopolymers in the infected airway. A charge engineered variant of human lysozyme possesses improved antibacterial activity in the presence of disease associated inhibitory molecules
physiological function
-
influence of the chemical chaperones 4-hexylresorcinol, and 5-methylresorcinol on the structure, equilibrium fluctuations, and functional activity of the hydrophilic enzyme lysozyme, molecular dynamics, overview
physiological function
-
lysozyme activates Enterococcus faecium to induce necrotic cell death in macrophages in vitro and in vivo. Pretreatment of Enterococcus faecium with lysozyme and subsequently with broad spectrum protease considerably reduces cell death, suggesting that a bacterial surface protein is causative for cell death induction.
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
goose-type lysozyme in channel catfish shows activity and efficacy as plasmid DNA immunostimulant against Aeromonas hydrophila infection, overview
physiological function
-
lysozyme can act as a natural antibiotic
physiological function
lysozyme is a key component of the innate immune system and plays an important role in antibacterial infection, the c-type lysozyme participate in innate immune defense against extracellular bacterial pathogens, in particular those of Gram-positive nature, e.g. Edwardsiella tarda TX1, Pseudomonas fluorescens TSS, and Vibrio anguillarum C312. The enzyme is able to inhibit the growth of several fish bacterial pathogens in a manner that depended on the dose of the protein
physiological function
lysozymes represent important innate immune components against bacteria
physiological function
-
purified refolded recombinant enzyme exhibits antibacterial activity against Bacillus megaterium and Micrococcus luteus
physiological function
-
the enzyme causes cell lysis by cleaving the beta-(1-4) glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in the peptidoglycan layer of Gram-positive bacteria
physiological function
-
the enzyme, free or immobilized on silver nanoparticles, shows antibacterial activity against Escherichia coli strain 2809
physiological function
-
isoform lysc is involved in the whitefly immune system while isoforms lysi1 and lysi2 play a role in digestion or nutrition absorption
physiological function
-
isoforms LysG and LysC have the potential for immune defense system against bacterial infection
physiological function
the enzyme activates the human sweet taste receptor T1R2/T1R3
physiological function
the enzyme activates the human sweet taste receptor T1R2/T1R3
physiological function
-
the enzyme is the important molecule in shrimp antimicrobial and antiviral response
physiological function
-
the enzyme serves as an important innate immunity factor and plays a key defense role during host-pathogen interactions in sea cucumbers
physiological function
-
the high efficiency of lysozyme in inhibiting gram-positive bacteria is caused by its ability to cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine of bacterial cell wall peptidoglycans
physiological function
-
lysozyme can act as a natural antibiotic
-
additional information
-
comparison of the structure, surface charge, dissociation constants, and pH optimum of the fly enzyme with the enzyme from egg white, overview
additional information
-
the active site of lysozyme contains two catalytic residues, Glu35 and Asp52, which lie in a cleft to the vicinity of the largest pocket and harbor the substrate binding site
additional information
-
the modified bovine milk is a possible substitute for human milk
additional information
-
the reaction follows a Michaelis-Menten mechanism
additional information
-
a nucleation process leads to the formation of non-fibrillar aggregates of lysozyme at physiological pH and 25°C, and 56°C heat-induced aggregation process of hen egg white lysozyme at pH 7.4 and mechanisms underlying aggregation, analysis by atomic force microscopy, Fourier transform infrared absorption and dynamic light scattering, overview. Occurence of a nucleation process simultaneous to a non-nucleative mechanism not leading to formation of lysozyme fibrillar aggregates but to amorphous aggregates composed of high molecular weight oligomers
additional information
active site structure and chemical interactions analysis using the crystal structure, PDB ID 2vb1, overview. Information on chemical interactions is contained in the topological properties of static electron densities, where the latter are electron densities after the removal of all thermal motion, topological and electron-density analysis and structure modelling. Glu35 and Asp52 residues are essential parts of the active site of the enzyme, reaction mechanism, overview
additional information
catalytic sites of lytic activity are Glu30 and Asp41, and for isopeptidase activity His107, the enzyme contains ten cysteine residues, three-dimensional homology model of the enzyme, overview
additional information
-
catalytic sites of lytic activity are Glu30 and Asp41, and for isopeptidase activity His107, the enzyme contains ten cysteine residues, three-dimensional homology model of the enzyme, overview
additional information
-
comparison of the levels of lysozyme, and peptidoglycan-lysing activity in salivary gland secretions of three species of the medicinal leech, overview
additional information
-
comparison of the levels of lysozyme, and peptidoglycan-lysing activity in salivary gland secretions of three species of the medicinal leech, overview
additional information
-
comparison of the levels of lysozyme, and peptidoglycan-lysing activity in salivary gland secretions of three species of the medicinal leech, overview
additional information
conserved three residues essential for catalytic activity in phage-type lysozyme are Glu20, Asp29, and Thr35. Comparison of the three-dimensional models of Ruditapes philippinarum and Coxiella burnetii lysozymes
additional information
-
conserved three residues essential for catalytic activity in phage-type lysozyme are Glu20, Asp29, and Thr35. Comparison of the three-dimensional models of Ruditapes philippinarum and Coxiella burnetii lysozymes
additional information
rates of cleavage of glycosidic linkages, transglycosylation, and hydration, enzyme reaction modelling, overview
additional information
-
rates of cleavage of glycosidic linkages, transglycosylation, and hydration, enzyme reaction modelling, overview
additional information
rates of cleavage of glycosidic linkages, transglycosylation, and hydration, enzyme reaction modelling, overview
additional information
-
rates of cleavage of glycosidic linkages, transglycosylation, and hydration, enzyme reaction modelling, overview
additional information
structure-function relationhip of two isozymes of the invertebrate i-type lysozyme, active site residues are Glu18 and Asp30, substrate interaction via residues P44, Y45, Y47, H94, and p98, overview
additional information
the conserved residues E50 and D67 form the putative catalytic site
additional information
-
the conserved residues E50 and D67 form the putative catalytic site
additional information
-
two catalytic residues in the active site of lysozyme, Glu35 and Asp52, lie in a cleft, close to the largest pocket, harboring the active site. Lysozymes interaction with two types of rod-shaped gold nanostructures reveals that the structure, lytic activity, and stability of the enzyme has not undergone any undesirable change. Once the protein is adsorbed onto the surface of gold nanorod/gold nanorice, it gains a more regular structure, retaining lytic activity and stability, kinetics, overview
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?
x * 15000, SDS-PAGE
?
x * 14860, calculated, mature protein
?
x * 15880, calculated, mature protein
?
-
x * 14300, calculated from amino acid sequence
?
-
x * 32200, Thioredoxin-His-S-tagged enzyme, SDS-PAGE
?
x * 20010, calculated from sequence
?
-
x * 16464, matrix-assisted laser desorption ionization time-of-flight mass spectrometry
?
-
x * 22000, calculated from amino acid sequence
?
-
x * 14745, calculated from sequence
?
-
x * 17771.5, two potential forms of enzyme: 17771.5 Da and 17861 Da, MALDI-MS
?
x * 18200, calculated from amino acid sequence
?
-
x * 14300, calculated from amino acid sequence
?
-
x * 14400, calculated from amino acid sequence
?
-
x * 14000, about, SDS-PAGE
?
x * 12300, about, sequence calculation
?
x * 15600, calculated and SDS-PAGE of recombinant protein
?
-
x * 16000 + x * 28000 + x * 44000, SDS-PAGE, recombinant isoform mlDL-Ds3 forms stable oligomeric complexes
?
-
x * 14672, calculated
?
-
x * 14679.14, mass spectrometry
?
x * 21508, sequence calculation
?
-
x * 14679, recombinant enzyme, MALDI-TOF mass spectrometry
?
-
x * 14700, recombinant enzyme, SDS-PAGE
?
x * 28000, recombinant enzyme, SDS-PAGE
?
x * 57100, sequence calculation
?
-
x * 21300, calculated from sequence
?
x * 16320, calculated, x * 16000, SDS-PAGE
?
-
x * 18070, calculated from amino acid sequence
?
x * 21000, SDS-PAGE, x * 21200, about, sequence calculation
?
x * 17460, sequence calculation
?
x * 15700, recombinant His-tagged enzyme, SDS-PAGE
?
x * 33000, SDS-PAGE, x * 33141, calculated
?
Thermus virus IN93 phiIN93
-
x * 33000, SDS-PAGE, x * 33141, calculated
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dimer
-
formation of covalent bonds between lysozyme molecules by zero-length cross-linking. Approximately one-third of the total lysozyme becomes cross-linked. The enzymatic activity of cross-linked lysozyme dimer is the same as monomer. The activity of lysozyme dimer remains constant up to 10 min at 80°C. Lysozyme possess a compact structure in the dimer form
dimer
-
2 * 30000, SDS-PAGE
monomer
-
4 isoforms, 1 * 14100-15000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 16000, SDS-PAGE
monomer
-
CHIT36, SDS-PAGE
monomer
-
CHIT24, 1 * 24000, SDS-PAGE
monomer
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
monomer
-
FII, 1 * 32000, SDS-PAGE
monomer
-
1 * 15700, SDS-PAGE
monomer
Tequatrovirus T4
-
1 * 18700
additional information
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quantitative characterization of the kinetic mechanism of tertiary and secondary structural evolution of hen egg white lysozyme at the early stages of its fibrillation using the new 2D simulation-aided deep UV resonance Raman spectroscopy
additional information
-
secondary structure of lysozyme, free and bound to gold nanorods, no significant change in the secondary structure occurs upon binding, overview
additional information
-
Fourier transform infrared spectroscopy reveals that alpha-helix and beta-sheet are the major secondary structures for lysozyme
additional information
-
secondary structure of lysozyme, overview
additional information
-
the mechanism driving the aggregation process of lysozyme at physiological pH is nucleation, conformational changes of the secondary and tertiary structures accompanying the early stages of the lysozyme aggregation process, overview
additional information
three-dimensional homology model of the enzyme, overview
additional information
-
three-dimensional homology model of the enzyme, overview
additional information
-
peptide mass fingerprinting of recombinant enzymes, overview
additional information
the enzyme shows no dimerization like the enzyme of bivalve Venerupis philippinarum due to the lack of residue Lys108 responsible of dimerization in the other organism
additional information
-
structure analysis of MdL1 and MdL2, overview. Residues S106-T107 delimit a polar pocket around E32, as catalytic acid/base, and N46 contributes to the positioning of D50, as catalytic nucleophile
additional information
three-dimensional structure comparison, overview
additional information
-
three-dimensional structure comparison, overview
additional information
structure homology modeling, overview
additional information
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structure homology modeling, overview
additional information
the enzyme contains an N-terminal signal peptide sequence (residues 1-15) followed by a c-type lysozyme/alpha-lactalbumin domain (residues 16-142). Residues C21 and C141, C45 and C129, C79 and C94, and C90 and 108 are predicted to form disulfide bonds
additional information
-
the enzyme contains an N-terminal signal peptide sequence (residues 1-15) followed by a c-type lysozyme/alpha-lactalbumin domain (residues 16-142). Residues C21 and C141, C45 and C129, C79 and C94, and C90 and 108 are predicted to form disulfide bonds
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hanging drop vapor diffusion method, using 100 mM NH4H2PO4, 100 mM Tris pH 8.8, 45% 2-methyl-2,4-pentanediol
using 200xa0mM MgCl2, 100xa0mM Tris (pHxa08.0) and 20% (w/v) PEG 6000
modeling of complex with GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
hanging drop vapor diffusion method
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recombinant bovine stomach lysozyme 2, to 1.5 A resolution. Space group P212121. Stability may be due to negatively charged surfaces, a shortened loop and slat bridges
crystal structure of mutant N44Q/N47Q/N49Q/N68Q/N103Q is substantially identical to that of the wild type, and the substitutions of Asn to Gln are appropriate for the folding and structural analyses of this protein
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comparison of native and A-states
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phage T4 induced: study of structural basis of thermal stability
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hanging drop vapor diffusion method
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asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings
atomic and molecular displacements
-
crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme
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crystallization conditions
-
crystallization data in complex with membrane bound lysozyme inhibitor of C-type lysozyme MliC. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues
crystallographic studies of denaturation and renaturation
-
determinatipon of crystallization phase diagrams at pH 2.5, pH 6.0, and pH 7.5. At pH values below 4.5, the border between the metastable region and the nucleation region shifts to the lower precipitant concentration in the phase diagramm and at pH values above 4.5, the border shifts to higher precipitant concentrations. The qualities of crystals at different pH values are more or less equivalent
hanging drop method and nanotemplate crystallization method. Crystals grown by the nanostructured template method appear radiation-resistant
-
hanging drop method, crystals of native enzyme and enzyme in complex with various alcohols (ethanol, 1-butanol, 1-pentanol, 2-propanol or TFE). Although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound water. Increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein
hanging drop vapor diffusion method, using 2.8-3.0% (w/v) (about 0.35 M) sodium nitrate
-
hexagonal crystal crystallize from a saturated sodium nitrate solution at pH 8.4, crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. 1.46 A resolution
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in complex with arginine and benzyl alcohol, at 45°C, hanging drop vapor diffusion method
kinetics and thermodynamics of lysozyme precipitation in ammonium sulfate solutions at pH 4 and 8 and room temperature. If sufficient time is allowed, microcrystals develop following an induction period after initial lysozyme precipitation, even up to ionic strengths of 8 M and at acidic pH, where lysozyme is refractory to crystallization in ammonium sulfate
measurement of lysozyme solubility in aqueous solutions as a function of NaCl, KCl, and NH4Cl concentrations at 25°C and pH 4.5. Simple model for the crystalline phase based on salt partitioning between solution and the hydrated protein crystal
membrane crystallization of lysozyme under forced solution flow
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mutants K33A and K33N. The side chain of K33 in wild-type hydrogen bonds with N37 involved in the substrate-binding region. Orientation of N37 differs in mutants K33A and K33N
pure enzyme, hanging drop vapour diffusion method, 50 or 150 mg/ml enzyme in 0.1 M sodium acetate, pH 4.5, sodium phosphate, pH 6.5, or Tris-HCl, pH 8.5, mixing of 0.0015 ml of protein solution and 0.0015 ml of reservoir solution, equilibration against 0.5 ml of reservoir solutiom, 20°C, crystallization method evaluation using Gly, Ser, Asp, Glu, Arg, ornithine, Lys and glycine ethyl ester as precipitants at pH 4.5, 6.5 and 8.5, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
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purified enzyme in complex with 1-butyl-3-methylimidazoliumtetrafluoroborate, 1-butyl-3-methylimidazolium chloride, 1-butyl-3-methylimidazolium bromide, and 1,3-dimethylimidazolium iodine, 8% protein in 5% NaCl and 0.1 M sodium acetate, pH 4.5, ligands are injected into the protein solution. Supersaturated solutions are obtained by mixing protein stock solutions with precipitant solutions, 4°C, X-ray diffraction structure determination and analysis
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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
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purified recombinant MdL2, sitting drop vapour diffusion method, 18°C, precipitant solution containing 28% isopropanol, 21% PEG 4000, and 0.115 M sodium citrate pH 4.2, addition of 0.2 M ammonium acetate, 30% 2-methyl-2,2-pentanediol, 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 1 crystals belong to the monoclinic space group P2(1), unit-cell parameters a = 36.52, b = 79.44, c = 45.20 A, beta = 102.97°
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 2 crystals belong to the orthorhombic space group P2(1)2(1)2, unit-cell parameters are a = 73.90, b = 96.40, c = 33.27 A
vapour-diffusion sitting-drop method, structure of lysozyme c in native form and complexed form with (N-acetylglucosamine)3
1.9 A resolution, space group P212121. Positions of P104 in the substrate subsite A and other amino acids in the subsites E and F differ from those of hen egg white, while the overall stuctures are very similar
the x-ray structure of the lytic transglycosylase gp144 is determined to 2.5 A resolution, in complex with chitotetraose, (N-acetylglucosamine)4, to 2.6 A resolution
Phikzvirus phiKZ
vapor diffusion hanging drop method, crystal structure of the enzyme complexed with a trimer of N-acetylglucosamine to 1.6 A resolution
-
purified enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 150 mM NaCl and 50 mM HEPES, pH 7.25, is mixed with 0.001 ml of reservoir solutions containing 43-45% ammonium sulfate, 0.01 M cobalt chloride, and 0.1 M MES, pH 6.25-6.5, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 1.75 A resolution
hangingdrop and sitting-drop vapour-diffusion methods
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in complex with Ni2+ ions, sitting drop vapor diffusion method, using 20% (w/v) PEG 6000, 100 mM MES pH 5.0
Tequatrovirus T4
the crystal structure of the switch mutant L20/R63A liganded to both methyl- and ethylguanidinium ions is determined at resolutions of 1.7 A and 1.8 A, respectively
Tequatrovirus T4
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F34Y
site-directed mutagenesis at the substrate subsite E, the mutant shows a slightly altered product pattern compared to the wild-type enzyme
F34Y/N37G
site-directed mutagenesis at the substrate subsites E/F, the mutant shows a slightly altered product pattern compared to the wild-type enzyme
F34Y/N37G/G71R
site-directed mutagenesis, the mutant shows altered time course data compared to the wild-type enzyme
G71R
site-directed mutagenesis, the mutant shows altered time course data compared to the wild-type enzyme
N37G
site-directed mutagenesis at the substrate subsite F, the mutant shows a slightly altered product pattern compared to the wild-type enzyme
N44Q/N47Q/N49Q/N103Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites
N44Q/N47Q/N49Q/N68Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites
N44Q/N47Q/N49Q/N68Q/N103Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites. Decrease in lytic activity by a factor 20 compared with wild-type
N44Q/N47Q/N68Q/N103Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites
N44QN49Q/N68Q/N103Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites
N47Q/N49Q/N68Q/N103Q
-
mutant construcuted for study of charge heterogeneity caused by asparaginyl deamidation. Residues Asn 44, 47, 49, and 68 are the deamidation sites
K33A
140% of wild-type lytic activity, 116% of wild-type activity on glycol chitin
K33N
130% of wild-type lytic activity, 111% of wild-type activity on glycol chitin
N103D
-
increased structural flexibility and surface functional properties
N106D
-
increased structural flexibility and surface functional properties
R114A
decrease in activity toward substrate glycol chitin to 80.5%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta is about 50% of wild-type. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123
R114H
decrease in activity toward substrate glycol chitin to 79%. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta. Structural changes induced by the mutation are extended to aromatic side chains of F34 and W123
R114L
no decrease in activity toward substrate glycol chitin. Reduction of binding free enrgies of E-F sites and the rate constant of transglycosylation for substrate GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
R21T/G49N
-
better emulsifying properties
W108GA
-
site-directed mutagenesis
W111GA
-
site-directed mutagenesis
W123G
-
site-directed mutagenesis
W28GA
-
site-directed mutagenesis
W62GA
-
site-directed mutagenesis
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 variants 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 enzymes 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
D12A
-
cell-lytic activity is strongly reduced
D12A/E33A
-
no cell-lytic activity
D12G
-
cell-lytic activity isstrongly reduced
D198A
-
cell-lytic activity is slightly reduced
D36A
-
cell-lytic activity is similar to wild-type enzyme
D96A
-
cell-lytic activity is strongly reduced
E237A
-
cell-lytic activity is similar to wild-type enzyme
E238A
-
cell-lytic activity is similar to wild-type enzyme
E33A
-
cell-lytic activity isstrongly reduced
E88D
-
cell-lytic activity is similar to wild-type enzyme
E98A
-
no cell-lytic activity
G10S
-
cell-lytic activity is strongly reduced
G253A
-
cell-lytic activity is similar to wild-type enzyme
G267A
-
cell-lytic activity is similar to wild-type enzyme
G281A
-
cell-lytic activity is similar to wild-type enzyme
G292A
-
cell-lytic activity is similar to wild-type enzyme
H60R
-
cell-lytic activity is strongly reduced
K142E
-
cell-lytic activity is similar to wild-type enzyme
K142R
-
cell-lytic activity is similar to wild-type enzyme
K207A
-
cell-lytic activity is similar to wild-type enzyme
K211A
-
cell-lytic activity is similar to wild-type enzyme
K25T
-
cell-lytic activity is similar to wild-type enzyme
L132P
-
cell-lytic activity is strongly reduced
L264A
-
cell-lytic activity is slightly reduced
M1I
-
cell-lytic activity is reduced
M1K
-
cell-lytic activity is reduced
N67K
-
cell-lytic activity is similar to wild-type enzyme
P212A
-
cell-lytic activity is similar to wild-type enzyme
P216A
-
cell-lytic activity is similar to wild-type enzyme
R109L
-
cell-lytic activity is similar to wild-type enzyme
R251A
-
cell-lytic activity is slightly reduced
V124M
-
cell-lytic activity is slightly reduced
V79F
-
cell-lytic activity is similar to wild-type enzyme
W284A
-
cell-lytic activity is strongly reduced
W284G
-
cell-lytic activity is strongly reduced
Y272A
-
cell-lytic activity is strongly reduced
Y61H
-
cell-lytic activity is stronly reduced
N46D/S106V/T107A
-
site-directed mutagenesis of isozyme MdL2, the mutant pKas are increased compared to the wild-type pKas
D30A
-
mutant exhibits no lysozyme activity
E18A
-
mutant exhibits no lysozyme activity
E50A/D67A
site-directed mutagenesis, mutation of catalytic residues, the mutant shows drastically reduced bacteriolytic activity compared to the wild-type enzyme
C18S/C29S
-
deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability
C4S/C18S/C29S/C60S
-
deletion of both disulfide bonds. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability. Optimum temperature of catalytic activity is dow-shifted by about 20 degrees
C4S/C60S
-
deletion of disulfide bond. No rearkable difference to wild-type in secondary structure or catalytic activity, but decrease in stability
E73A
-
no hydrolysis of N,N',N'',N''',N''''-pentaacetylchitopentaose at 50°C for 48 h. Decrease in Tm-value is 3.2°C as compared to wild-type value
E73D
-
detectable level of activity, but lytic activity against Micrococcus lysodeikticus is drastically reduced as compared to wild-type activity. Decrease in Tm-value is 6.1°C as compared to wild-type value
E73Q
-
no hydrolysis of N,N',N'',N''',N''''-pentaacetylchitopentaose at 50°C for 48 h. Decrease in Tm-value is 4.0°C as compared to wild-type value
A98L
Tequatrovirus T4
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume
I3C/C54T
Tequatrovirus T4
-
reduction leads to destabilization
I3C/C54V
Tequatrovirus T4
-
reduction leads to destabilization
K60H/L13D
Tequatrovirus T4
-
destabilization
K83H/A112D
Tequatrovirus T4
-
destabilization
L99A
Tequatrovirus T4
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume
L99G/E108V
Tequatrovirus T4
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume
N144E
Tequatrovirus T4
-
increased stability
Q123E
Tequatrovirus T4
-
increased stability
S90H/Q122D
Tequatrovirus T4
-
destabilization
T115E
Tequatrovirus T4
-
increased stability
V149G
Tequatrovirus T4
study on denatured state and its stabilization by high pressure. At pH 3.0, the magnitudes of the volume changes of denaturation for L99A, L99G/E108V, A98L, and V149G T4 lysozyme positively correlate with the total cavity volume
additional information
-
constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes
additional information
-
constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes
additional information
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two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme. The bactericidal activity against Escherichia coli of S6L-lysozyme and S7-lysozyme is greatly increased
additional information
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the lytic activities of the oligomannosyl lysozyme (a core-type oligomannose chain (Man14GlcNAc2)-linked lysozyme and) and the polymannosyl lysozymes (a large polymannose (Man310GlcNAc2) chain-linked lysozyme) are 70.4% and 5.1%, respectively, of the wild-type lysozyme when Micrococcus lysodeikticus cells are used as the substrate. The enzymatic activity of the oligomannosyl lysozyme is totally conserved for the glycolysis assay with a soluble substrate, glycol chitin, whereas that of the polymannosyl lysozyme is not. After heating the sample up to 95 °C at pH 7.0 where no visible protein coagulation is observed, thermostability of the enzymatic activity of the oligomannosyl lysozyme is drastically improved with more than 60% of residual lytic activity. Emulsifying properties of the protein also are highly improved by the oligomannosylation, in which the emulsifying activity is 3.2 times higher than that of the wild-type protein. Corresponding to the increase of the surface functionalities, the surface tension of the oligomannosyl protein exhibits a significantly lower value compared to that of the wild-type
additional information
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a oleyl group is covalently bound to free amino groups, N-terminal amino group and epsilon-amino groups of lysine residues, on lysozyme. No decrease in the activity of lysozyme derivatives occurs compared to native lysozyme, but the oleyl group, as a hydrophobic compound, facilitated the interaction of lysozyme with the bacterial membrane through hydrophobic interaction
additional information
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conjugation of silver nanoparticles with the enzyme resulting in enhanced activity of lysozyme-AgNP conjugates with synergic antibacterial effect without damaging the catalytic site of lysozyme, surface plasmon resonance and fluorescence and circular dichroism spectroscopy analysis, overview. Maximum immobilization efficiency of 98% is achieved at 0.01:1 ratio of enzyme:AgNP
additional information
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covalent immobilization of the enzyme on two different micro-size magnetic particles, i.e. tosyl-activated and carboxylated, at pH 3.2, 37°C for 20 h under rotation
additional information
-
development of a process for immobilizing lysozyme acting as an edible coating onto a chitosan powder surface (deacetylation degree of 90%), method evaluation, overview. The immobilized enzyme retains 72.50% of the specific activity of free enzyme with the covalent attachment procedure. The covalently immobilized lysozyme exhibits remarkable characteristics on optimum pH and temperature, and storage stability compared to the free enzyme. The active coating is effective in inhibiting the growth of Escherichia coli O157:H7 CICC 21530 and Staphylococcus aureus CICC 21600 for a week
additional information
-
site-directed mutagenesis to modulate conformation and dynamic properties of the enzyme in non-native unfolded state, random-coil structure, modelling, and comprehensive analysis of non-native states of wild-type and mutant forms of the model protein lysozyme by nuclear magnetic resonance spectroscopy
additional information
-
review about engineering of human lysozyme
additional information
-
a strategy to engineer an additional active site for human lysozyme: grafting the entire human lysozyme exon 2, which encodes the catalytically competent domain, into the gene at a position corresponding to an exposed loop region in the translated protein. Exon 2 grafting creates a novel lysozyme with twice the activity of the wild type enzyme, equal activity came from each of the two active sites. The thermal stability and pH-stability of wild-type and two-active site lysozyme is similar
additional information
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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
additional information
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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. 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
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deletion analysis demonstrates that the beta/alphagaY domain of N-terminal 216 residues is the core enzyme portion, although the cell-lytic ability is lower than that of LysgaY. These mutational experiments suggest that beta/alphagaY (in which two acidic residues of D12 and E98 likely act as catalytic residues) is responsible for cell-lytic activity, and SH3bgaY promotes beta/alphagaY possibly through cell-wall binding function
additional information
acmB deletion/insertion mutants with lower autolysis rate/extend
additional information
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acmB deletion/insertion mutants with lower autolysis rate/extend
additional information
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introduction of six basic residues onMdL1 surface increases by 1 unit the pH optimum for the activity upon bacterial walls
additional information
Tequatrovirus T4
L20 is a mutant with a molecular switch in a T4 lysozyme construct that promotes a large-scale (about 20 A) translocation of an alpha-helix but is unrelated to the function of the protein. The design is based in part on the use of a duplicated helical sequenc. When Arg63 is truncated to Ala (in mutant L20/R63A), the stability of the protein is reduced by 6.1°C relative to L20. In high salt buffer similar to that used for crystallization, the melting temperature of L20/R63A is increased by 2.2°C in the presence of either 200 mM methylguanidinium or 200 mM ethylguanidinium ion
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10 - 40
-
the enzyme remains stable for 30 min at 10-40°C, activity sharply decreases to about 15% after 30 min at 50°C
120
-
at 2 bar, 20 min, 79% loss of activity
20 - 70
-
unaffected, 10 min, pH 5.0
20 - 90
-
stable temperature-range
25
-
pH 3.2, half-life for the free enzyme is 39 h, for the enzyme immobilized on tosyl-activated and carboxylated micro-size magnetic particles is 280 h and 134 h, respectively
25.3
-
loss of 50% activity
30
10 min, 14% loss of activity
45
Tequatrovirus T4
-
inactivation above, 10 min
45.3
-
melting temperature, mutant C4S/C18S/C29S/C60S
45.4
-
thermal denaturation of the catalytic module
46.2
-
melting temperature, reduced wild-type
51.1
-
melting temperature, mutant C4S/C60S
54.3
-
melting temperature, mutant C18S/C29S
57
-
Tm-value for mutant E73A is 57.4°C. Tm-value for mutant E73Q is 56.6°C
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
60 - 70
-
10 min, about 40% loss of activity
60.6
-
melting temperature, wild-type
61
-
Tm-value for wild-type enzyme is 60.6°C
76
-
mid-transition temperature is 76.3°C for S6K-lysozyme and 76.0°C for S7-lysozyme
77
-
mid-transition temperature of wild-type enzyme
78 - 90
melting temperature at pH 3.0. The enzyme hydrolyzes at 90°C
85
-
purified enzyme, pH 6.2, inactivation after 60 min
95
1 h, 38.6% residual activity in absence of 2-mercaptoethanol, 93.8% residual activity in presence of 2-mercaptoethanol
100
the recombinant enzyme retains16% bacteriolytic activity after being heated to 100°C for 50 min
100
-
stable for 60 min at pH 3
100
-
purified recombinant enzyme, 10 min, 50% activity remaining
100
-
2 h, 74% loss of activity
100
-
purified enzyme, pH 6.0, loss of 60% activity after 10 min, inactivation after 30 min
20
-
30 min, about 10% loss of activity
20
-
purified enzyme, pH 6.0, 10-30 min, stable at
20
10 min, 3% loss of activity
20 - 30
-
10 min, stable
37
-
35% residual activity after 4 days, pH 4
40
Lederbergvirus P22
-
no loss of activity up to, 5 min
40
-
10 min, about 20% loss of activity
40
-
purified enzyme, pH 6.0, 10-30 min, loss of 25-30% activity
40
-
10 min, about 15% loss of activity
40
10 min, 25% loss of activity
50
-
FI unaffected, 10 min
50
-
10 min, about 30% loss of activity
50
10 min, 30% loss of activity
55
-
Tm-value for mutant enzyme E73S is 54.5°C
55
10 min, 66% loss of activity
60
-
purified commercial enzyme, pH 6.2, 60 min, inactivation
60
-
purified recombinant enzyme, 45 min, 95% activity remaining
60
-
FII, unaffected, 10 min
60
-
10 min, about 25% loss of activity
70
-
30 min, about 15% loss of activity
70
Lederbergvirus P22
-
90% loss of activity after 5 min
70
-
10 min, about 30% loss of activity
70
Tequatrovirus T4
-
80% loss of activity after 10 min
80
-
30 min, about 60% of maximal activity
80
-
the activity of lysozyme dimer remains constant up to 10 min
80
-
83% of activity of that at 25°C, more stable than hen lysozyme
80
-
10 min, about 45% loss of activity
80
-
purified enzyme, pH 6.0, 10-30 min, loss of 45% activity
80
-
10 min, about 50% loss of activity
90
-
180 min, about 35% loss of activity
90
-
60 min, about 60% loss of activity
90
-
30 min, 11% loss of activity
90
-
30 min, 69% loss of activity
90
-
30 min, 72% loss of activity
90
-
3 h, about 45% loss of activity, isoenzyme SSTL A
90
-
90 min, about 70% loss of activity, isoenzyme SSTL B
90
-
about 60% loss of activity after 60 min, about 80% loss of activity after180 min
90
-
3 h, 70% loss of activity
90
-
30 min, 55% loss of activity
90
-
about 60% loss of activity after 60 min, about 80% loss of activity after180 min
additional information
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broad thermal stability
additional information
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temperature induced transitions in equine lysozyme
additional information
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lysozyme's interaction with two types of rod-shaped gold nanostructures reveals that the structure, lytic activity, and stability of the enzyme has not undergone any undesirable change. Once the protein is adsorbed onto the surface of gold nanorod/gold nanorice, it gains a more regular structure, retaining lytic activity and stability, kinetics, overview
additional information
-
human lysozyme more resistant to heat than chicken
additional information
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lysozyme more stable than hen lysozyme
additional information
unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Rapid and irreversible inactivation takes place during heating at high enzyme concentration
additional information
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unfolding and potential refolding analysis due to cold adaptation and heat treatment, differential scanning calorimetry. Recombinant SalG has a melting temperature of 36.8°C under thermal denaturation conditions and regains activity after returning to permissive (low) temperature. Rapid and irreversible inactivation takes place during heating at high enzyme concentration
additional information
-
-
additional information
Tequatrovirus T4
-
mutant and wild-type, study of structural basis of thermal stability
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2 different kinds of transgenic mice containing human lysozyme genomic DNA-based constructs with different signal peptide DNA are respectively established as system models
-
a C-terminal hexahistidine tail Lys44 is overproduced in Escherichia coli
-
a large polymannose (Man310GlcNAc2) chain-linked lysozyme is predominantly expressed in Saccharomyces cerevisiae accompanied by small amounts of a core-type oligomannose chain (Man14GlcNAc2)-linked lysozyme in the yeast medium where the extracellular pH is kept at 3.5 or above, while an oligomannose chain lysozyme is preferentially expressed in the yeast medium where the pH is less than 3
-
acmB gene, AcmB devoid of its N-terminal domain, expression in Escherichia coli M15(pREP4), sequencing
amino acid Ser at the N-terminus
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3) and Bacillus subtilis strain WB800, subcloning in Escherichia coli strain DH5alpha
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, expression of enzyme mutants in Pichia pastoris, subcloning in Escherichia coli strain JM109
expressed in Escherichia coli BL21 Star cells
Tequatrovirus T4
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Gallus gallus eggs
-
expressed in Pichia pastoris
expression in Escherichia coli
expression in goat at 67% of human breast milk
-
expression in human cell lines HeLa and MCF-7
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expression in Pichia pastoris
expression in Saccharomyces cerevisiae
expression of 253 C-terminal residues in Escherichia coli
-
expression of enzyme mutants in Escherichia coli strain BL21(DE3) in inclusion bodies
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expression of recombinant protein in Saccharomyces cerevisiae
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expression of the enzyme in transgenic cattle, Bos taurus, as secreted enzyme in milk using the pBC2-HLY-NEOR transgene vector
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expression of wild-type and engineered enzyme in Saccharomyces cerevisiae
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gene abLysI, DNA and amino acid sequence determination and analysis, sequence comparison and phylogeny analysis, enzyme overexpression in Escherichia coli strain BL21(DE3)
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
-
gene RpLysPh, DNA and amino acid sequence determination and analysis, phylogenetic analysis and real-time quantitative RT-PCR expression analysis
genomic library construction, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression in Spodoptera frugiperda Sf9 cells using the baculovrisu transfection system via host Escherichia coli strain coli DH10Bac
into the pQE-30 vector for expression in Escherichia coli cells
Phikzvirus phiKZ
isozyme OHLysG1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis
-
isozyme OHLysG2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis
-
isozyme OHLysG3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis
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lysozyme is amplified from bacteriophage lambda cDNA, recombinant enzyme expression in Escherichia coli strain DH5alpha
-
overexpression in Escherichia coli
-
overexpression of GST-tagged enzyme in inclusion body in Escherichia coli with induction of the fusion protein
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ply3626 gene, expression in Escherichia coli JM109
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recombinant enzyme expression in Spodoptera frugiperda cells via baculovirus transfection method
recombinant enzyme expression in sugarcane stalks, Saccharum spp. hybrid, process evaluation and optimization, overview
-
recombinant expression of the mature peptide-coding region in Pichia pastoris strain GS115
recombinant expression of wild-type and mutant MdL1 and MdL2 in Pichia pastoris
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sequence comparisons, phylogenetic tree
sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
T4 lysozyme is cloned into the yeast expression vector pPIC9K under the control of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase promoter and expressed at high level in Hansenula polymorpha strain A16, the enzyme is secreted
Tequatrovirus T4
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Tapes japonica lysozyme (TjL) is recombinantly produced using Pichia pastoris YJT46
-
the fragment is expressed in both BL21 (DE3) and B834 (DE3) Escherichia coli cells
-
the gene coding for lysozyme in banana prawn (Fenneropenaeus merguiensis) is cloned, sequenced and expressed in pET-32a vector (Escherichia coli)
-
the gene encoding the Bacillus anthracis GH25 enzyme, BaGH25c, is expressed in Escherichia coli
-
the His-tagged protein Lys411H is expressed in Escherichia coli mostly in inclusion bodies
the mature peptide coding region is heterologously expressed in Escherichia coli
-
two serine-rich heptapeptides, Ser-Ser-Ser-Lys-Ser-Ser-Ser (S6K) and Ser-Ser-Ser-Ser-Ser-Ser-Ser (S7) are fused to the C-terminus of chicken lysozyme by genetic modification. The cDNAs of S6K-lysozyme and S7-lysozyme are inserted into the expression vector of Pichia pastoris and secreted in the yeast cultivation medium. The secretion amounts of S6K-lysozyme and S7-lysozyme are about 60% of that of wild-type lysozyme
-
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Pichia pastoris
-
expressed in Pichia pastoris
expressed in Pichia pastoris
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Colitis bacteriophage
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Pichia pastoris
-
expression in Pichia pastoris
-
expression in Pichia pastoris
-
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
recombinant enzyme expression in Spodoptera frugiperda cells via baculovirus transfection method
-
recombinant enzyme expression in Spodoptera frugiperda cells via baculovirus transfection method
-
recombinant enzyme expression in Spodoptera frugiperda cells via baculovirus transfection method
-
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