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Information on EC 3.2.1.17 - lysozyme
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3.2.1.17 lysozymeIUBMB Comments
cf. also EC 3.2.1.14 chitinase.
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Word Map
- 3.2.1.17
- albumin
- fish
-
adsorption
- immunoglobulin
- lactoferrin
- neutrophil
-
lytic
- polymer
- phagocytic
- staphylococcus
- leukocyte
-
adsorb
- aureus
- streptococcus
- superoxide
- bacteriophage
- lymphocyte
-
bactericidal
- milk
- saliva
- iga
- myeloperoxidase
-
humoral
- nanoparticles
-
phagocytosis
-
fibril
- micrococcus
- ribonuclease
-
amyloid
- monocyte
- granulocyte
- myoglobin
- histiocytic
- tear
- chitosan
- aeromonas
- hydrophila
-
polymorphonuclear
- alpha-lactalbumins
- hydrogel
- pneumococcal
- mucus
- sarcoidosis
- amyloidosis
- defensins
- methacrylate
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penicillin-binding
- lactoperoxidase
- phenoloxidase
-
1-antitrypsin
- industry
- synthesis
- agriculture
- medicine
- nutrition
- analysis
- food industry
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
1,4-beta-N-acetylmuramidase, 1,4-beta-N-acetylmuramidase 1, 1,4-beta-N-acetylmuramidase A/C, 1,4-beta-N-acetylmuramidase M1, 1,4-beta-N-acetylmuramoylhydrolase, 1,4-N-acetylmuramidase, abLysI, AcmB, ASTL, Autolysin, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-N-acetylmuramidase
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1,4-beta-N-acetylmuramidase A/C
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1,4-beta-N-acetylmuramidase M1
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1,4-beta-N-acetylmuramoylhydrolase
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1,4-N-acetylmuramidase
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Autolysin
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c-type lysozyme
chicken-type lysozyme
CP-1 lysin
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CP-7 lysin
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CP-9 lysin
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CPL
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destabilase-lysozyme
endolysin
g-type lysozyme
globulin G
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globulin G1
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Goose-type lysozyme
i-type lysozyme
invertebrate lysozyme
L-7001
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Late protein gp15
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lysC
Lysis protein
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Lysosyme
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Lysozyme
lysozyme g
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Mdl1
mucopeptide glucohydrolase
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mucopeptide N-acetylmuramoylhydrolase
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muramidase
MV1 lysin
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N,O-diacetylmuramidase
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Outer wedge of baseplate protein
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P13
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Peptidoglycan hydrolase
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PR1-lysozyme
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Protein gp17
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Protein gp19
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Protein Gp25
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Protein Gp5
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Protein gp54
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Protein gpK
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SalG
endolysin
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Goose-type lysozyme
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Lysozyme
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muramidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
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Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
crystallization data and molecular dynamics simulations indicate that lysozyme is an inverting enzyme, and Asp97 acts as a second carboxylate and that the narrow space of the binding cleft at subsites E–G in GEL may prohibit the sugar chain to bind alternative site that might be essential for transglycosylation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
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hydrolysis
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cleaving the beta-1,4 glycosidic bond between N-acetyl-D-glucosamine (NAG) and N-acetylmuramic acid (NAM) in the peptidoglycan layer
hydrolysis
hydrolyze the beta-1,4-glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine of peptidoglycan
hydrolysis
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lysozyme has a potent antimicrobial effect due to the hydrolysis of the beta-linkage between muramic acid and N-acetyl glucosamine present in the microbial walls
hydrolysis
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lysozyme kills bacteria by hydrolyzing beta-1,4-glycosidic linkages between N-acetylglucosamine and N-acetylmuramic acid of the peptidoglycan layer in the bacterial cell wall
hydrolysis
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lysozyme hydrolyses 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan
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SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
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CAS REGISTRY NUMBER
COMMENTARY
9001-63-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(GlcNAc)6 + H2O
(GlcNAc)3
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and smaller amounts of (GlcNAc)2 and (GlcNAc)4 endo-splitting, hydrolyzes preferentially the third glycosidic linkage from the nonreducing end
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?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotetraose + chitotriose
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amount in descending order, binding kinetics with chitotriose, overview
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?
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotriose + chitotetraose
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amount in descending order, binding kinetics with chitotriose, overview
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?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + (GlcNAc)2
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main products
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?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ?
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?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
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?
L-gamma-glutamine-4-nitroanilide + H2O
L-gamma-glutamine + 4-nitroaniline
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substrate for isopeptidase activity of isoform cLys3
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?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
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eight amino acid residues interact with the N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose oligomer: Arg73, Gly102, Asn103, Leu56, Ala107, Val109, Ala110, and Lys33
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose
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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
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?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
?
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?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
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a synthetic fluorogenic substrate
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?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
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a synthetic fluorogenic substrate
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?
4-methylumbelliferyl tetra N-acetyl-beta-chitotetraoside + H2O
4-methylumbelliferol + tetra N-acetyl-beta-chitotetraose
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a synthetic fluorogenic substrate
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?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
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?
cell wall of Micrococcus luteus + H2O
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substrate for muramidase activity of isoform cLys3
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?
chitohexaose + H2O
chitobiose + chitotetraose
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mass spectrometry analysis
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?
chitohexaose + H2O
chitobiose + chitotetraose
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mass spectrometry analysis
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?
chitohexaose + H2O
chitobiose + chitotetraose
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mass spectrometry analysis
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?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
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?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
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?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
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enzyme displays lytic activity against Micrococcus lysodeikticus, Staphylococcus aureus and Escherichia coli
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?
peptidoglycan + H2O
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lyophilized cell wall of Micrococcus luteus
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?
peptidoglycan + H2O
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cell wall of Micrococcus luteus. Tyr34, Tyr45, Pro47, Pro102, and Asn114 are the amino acids contributing to the substrate binding
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?
peptidoglycan + H2O
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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
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?
peptidoglycan + H2O
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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
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?
peptidoglycan + H2O
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
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peptidoglycan + H2O
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
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Micrococcus lysodeikticus cells
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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lytic activity against Micrococcus lysodeiktikus cells
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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the enzyme cleaves the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine of bacterial cell wall peptidoglycans
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?
peptidoglycan + H2O
?
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lytic activity against Micrococcus lysodeiktikus cells
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?
peptidoglycan + H2O
?
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LysgaY lysed over 20 heated Gram-positive bacterial species as the substrates, including lactobacilli, lactococci, enterococci, micrococci, and staphylococci
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?
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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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enzyme is active on extraction of the following bacteria (in order of decreasing activity): Yersinia enterolitica, Escherichia coli, Pseudomonas aeruginosa, Salmonella typhimurium, Micrococcus lysodeikticus
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?
peptidoglycan + H2O
?
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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
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?
peptidoglycan + H2O
?
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lytic activity against Micrococcus lysodeikticus
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?
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
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?
peptidoglycan + H2O
N-acetylaminosaccharides
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C3 and C6 muropeptides
?
additional information
?
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the enzyme also has isopeptidase activity with 4-nitroanilide-L-gamma-glutamic acid
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additional information
?
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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
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additional information
?
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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
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additional information
?
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lysozyme has inhibitory effects on the proliferation of vascular endothelial cell in vitro
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additional information
?
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lysozyme is able to kill Entamoeba histolytica trophozoites
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additional information
?
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cell walls of Clostridium acetobulyticum, not: Micrococcus cells, beta-N-acetyl chitotetraoside
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additional information
?
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the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
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additional information
?
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I6ZIX7
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
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additional information
?
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phage T4: e lysozyme more specific than hen egg-white lysozyme, e lysozyme: hydrolysis of murein chains in which N-acetylmuraminic acid is substituted by peptide side chains L-Ala-D-Glu-meso-diaminopimelic acid-D-Ala
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additional information
?
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cell walls of Micrococcus lysodeikticus, are a substrate, while those of Xanthomonas campestris pv. malvacearum and Xanthomonas oryzae pv. oryzae are no substrates
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additional information
?
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lysozyme inhibits Clostridium perfringens type A and its alpha-toxin production
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additional information
?
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measurement of activity by lytic activity against Micrococcus luteus
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additional information
?
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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
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additional information
?
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a suspension of Micrococcus lysodeikticus is used as a substrate
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additional information
?
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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
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additional information
?
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Micrococcus luteus cells in the exponential growth phase are used as substrate
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additional information
?
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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
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additional information
?
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a commercial cell suspension of Oenococcus oeni, an oenological strain involved in the winemaking process, is utilized as enzyme substrate
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additional information
?
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the enzyme is lytically active on Micrococcus luteus suspension
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additional information
?
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the enzyme shows antibacterial activity by growth inhibition of a target organism Planococcus citreus
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additional information
?
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substrate are lyophilized Micrococcus lysodeikticus cell walls on lysoplates
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additional information
?
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recombinantly expressed enzyme shows strong lytic activity against Micrococcus lysodeikticus, isopeptidase activity, and antibacterial activity against several Gram-positive and Gram-negative bacteria
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additional information
?
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recombinantly expressed enzyme shows strong lytic activity against Micrococcus lysodeikticus, isopeptidase activity, and antibacterial activity against several Gram-positive and Gram-negative bacteria
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additional information
?
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i-type lysozyme isoform iLys2 does not exhibit muramidase, isopeptidase or serine hydrolase activities
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additional information
?
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the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
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additional information
?
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the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
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additional information
?
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the destabilase-lysozyme is a bifunctional enzyme, which combines isopeptidase and lysozyme activities
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additional information
?
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lysozyme is able to kill Entamoeba histolytica trophozoites
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-
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additional information
?
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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
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additional information
?
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a suspension of Micrococcus lysodeikticus is used as a substrate for HLysG2
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-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
gram-negative bacteria better substrate than gram-positive bacteria
-
-
-
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
additional information
-
cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues
formation of a 1,6-anhydromuramoyl product
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
peptidoglycan + H2O
?
-
cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
-
-
-
peptidoglycan + H2O
?
-
the enzyme cleaves the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine of bacterial cell wall peptidoglycans
-
-
?
additional information
?
-
-
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
-
-
-
additional information
?
-
I6ZIX7
the enzyme exhibits bacteriolytic activity against Escherichia coli, Aeromonas hydrophila, Staphyloccocus aureus, Bacillus subtilis, Streptococcus sp. and Staphylococcus epidermidis
-
-
-
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
?
-
-
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
?
-
-
the enzyme shows antibacterial activity by growth inhibition of a target organism Planococcus citreus
-
-
-
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
?
-
P61626
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
?
-
-
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
?
-
R4UMR3
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
?
-
-
AcmB expression is modulated during cell growth, AcmB is not involved in cell separation but contributes to cellular autolysis
-
-
-
additional information
?
-
Q8KKF9
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
?
-
B3GQR5
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
?
-
Q8IT75
enzyme exhibits potent lytic activities against fish pathogens
-
-
-
additional information
?
-
G8CYM6
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
?
-
Q859R8
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
Q859R8
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
-
additional information
additional information
-
Q8SD18
cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues
formation of a 1,6-anhydromuramoyl product
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
Cu2+
Mg2+
MgCl2
Mn
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
Na+
NaCl
Ni
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
additional information
no increase in activity at high ionic strength
Ca2+
-
required, strong temperature dependences of apparent affinities to Ca2+ due to low thermal stability of the apoform, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site, Ca2+-binding sites are generally able to bind Mg2+., overview
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
Mg2+
-
required, strong temperature dependences of apparent affinities to Mg2+ due to low thermal stability of the apoform and relatively high unfavorable enthalpies of Mg2+ association, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site. The Ca2+/Mg2+ selectivity of Mg2+-site of EQL is below an order of magnitude. The enzyme exhibits a distinct Mg2+-specific site, probably arising as an adaptation to the extracellular environment, overview
Na+
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
NaCl
-
activity increases as the NaCl concentration is increased from 0 to 0.1 M and then decreases from its maximum activity at 0.1 M NaCl with further increase in NaCl concentrations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
-
lysozyme inhibitory protein Ivy
-
homodimeric antitoxin, inhibitor of vertebrate lysozyme, from Escherichia coli
-
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
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
-
EDTA
at 10 and 20 mM causes 15% and 43% reduction of the enzyme activity
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
-
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
-
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
-
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
-
as yet unknown lysozyme inhibitors may exist in some Grame-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
additional information
-
study on the inhibitory effect on the enzymatic activity of lysozyme of a number of peptides each containing about 10 amino acids and overlapping exhaustively the protein sequence. A small fraction of them are able to inhibit the biological activity of the protein with micromolar efficiency. The peptide displaying the same sequence of segment 91-100 of the protein, and essentially corresponding to the last three turns of helix C, is the most efficient. The inhibitory mechanism is nonconventional. Local elementary structures formed in the denatured state, drive the folding process and selected peptides compete with these structures in binding complementary regions of the protein, preventing the formation of the native state
-
additional information
-
interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM
-
additional information
-
lysozyme and its derived peptides are able to bind biotin-labeled pUC19 plasmid DNA. The nonpeptide RAWVAWRNR, amino acids 107-115 of lysozyme, binds DNA with a KD value comparable to histones. Binding results in conformational changes
-
additional information
-
design and construction, based on the protein structures of lambda lysozyme and the SH3 domain of human Crk, of a synthetic protein switch that controls the activity of lysozyme by sterically hindering its active cleft through the binding of SH3 to its CB1 peptide-binding partner, i.e. fusion proteins Venus-CB1-lysozyme, Venus-CB1-lysozyme-CB1, Venus-CB1 and His-nSH3C. Modelling of fusion protein designs with lysozyme and CB1, in the absence of SH3, the lysozyme-CB1 fusion protein functions normally. In the presence of SH3, the lysozyme activity is inhibited and with the addition of excess CB1 peptides to compete for SH3 binding, the lysozyme activity is restored
-
additional information
-
bacterial membrane proton motive force regulates the lytic activity of the secreted endolysin Lys44 from Oenococcus oeni phage fOg44. Cytoplasmic membrane voltage dissipation is necessary but not sufficient for the full sensitization of cells to Lys44
-
additional information
-
Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory
-
additional information
no inhibition by c-type inhibitor Ivy; no inhibition by g-type inhibitor PliG
-
additional information
-
as yet unknown lysozyme inhibitors may exist in some Gram-negative bacteria, including Salmonella typhimurium and Pseudomonas aeruginosa
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hexylresorcinol
-
activates at low concentrations, up to 10-15 molcules of hexylresorcinol per protein globule, but inhibits at higher concentrations, at above 100 molecules of hexylresorcinol per protein globule the activity is abolished
5-methylresorcinol
-
interacts with the surface of lysozyme directly, not via water hydrogen bonds. This leads to a decrease in the denaturation temperature and an increase in the amplitude of equilibrium fluctuations, allowing it to be a powerful activator
choline
-
the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalent. Coupling between choline binding and folding indicates a high conformational plasticity that could correlate with the unusual alternation of short and long choline-binding repeats present in this enzyme. It can contribute to regulate enzymic activity
Protein disulfide isomerase
-
enhances activity of the activity of renatured lysozyme
-
TRAP
-
i.e. target of RNAIII activating protein , membrane-associated protein from Staphylococcus aureus. TRAP can specifically bind lysozyme and lysostaphin through its C-terminus and enhance lysozymal activities in vitro
-
additional information
-
practically inactive in absence of Triton X-100, hydrolysis of murein catalysed only when in contact with lipophilic components
-
additional information
-
ionic liquids influence protein crystal morphology, size, polymorph, crystal quality, and modify solution properties, possible mechanisms, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
-
human serum albumin-bound enzyme, pH 5.2, 37°C
0.001
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
-
free enzyme, pH 5.2, 37°C
additional information
additional information
-
Michaelis-Menten curve of lysozyme in the presence and absence of gold nanorods
-
additional information
additional information
-
the reaction follows a Michaelis-Menten mechanism
-
additional information
additional information
-
binding constants and thermodynamics of Ca2+ and Mg2+ binding, overview
-
additional information
additional information
-
Michaelis-Menten kinetics with cell suspension of Oenococcus oeni at pH 3.2 and pH 4.5 of free and immobilized enzyme, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of adsorbed on rod-shaped gold nanostructures and free enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.387
-
substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
4.32
-
substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
12500
purified enzyme, pH 6.0, temperature not specified in the publication
18800
purified enzyme, pH 6.0, temperature not specified in the publication
37600
-
purified native enzyme, substrate Micrococcus lysodeikticus cell walls, pH 6.0, 25°C
48330
purified recombinant enzyme, pH 6.0, 22°C, substrate lyophilized Micrococcus lysodeikticus
additional information
additional information
-
63 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C
additional information
-
58 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C
additional information
-
one unit lysozyme activity is defined as the amount of enzyme causing a decrase of 0.001 optical density value per minute at 25°C and pH 7.0. Specific activity of the eluted lysozyme (62580 U/mg) is higher than that obtained with a commercially available pure lysozyme Sigma (60000 U/mg)
additional information
-
isoenzyme SSTL A: 45 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C; isoenzyme SSTL B: 85 units per mg. One unit is defined as the amount of enzyme causing a decrease of 0.1 absorbance unit at 540 nm in 3 min of reaction at 25°C
additional information
7400 U/mg. One unit of enzyme is defined as the amounts that caused the decrease of 0.001 units of absorbance at 550 nM per min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
5.2
5.5
5.5
6 - 7
-
the optimal pH of rHLZ varies with salt concentration of the buffer, recombinant enzyme
6.2
6.4
6.5
6.6
the optimal assay conditions determined for the recombinant His-tagged protein are in 0.1M potassium phosphate buffer, pH 6.6 containing 1 mM CuCl2 at 25°C
additional information
-
the acidic pH optimum for MdL2 and MdL1 activities upon methylumbelliferylchitotrioside is determined by the presence of N46, S106 and T107 in the environment of their catalytic residues, which favors pKas reduction. The acidic pH optimum upon bacterial walls is determined by a low concentration of positive charges on the MdL2 and MdL1 surfaces
6
-
isoenzyme SSTL A, ionic strength 0.1; isoenzyme SSTL B, ionic strength 0.1
6.5
-
two-active site lysozyme, lytic activity against Micrococcus lysodeikticus
6.5
substrate lyophilized cell wall of Micrococcus luteus, isozyme lysozyme A
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
around 40-50% activity at pH 3.0-7.0, 100% activity at pH 8.0, about 20% activity at pH 9.0
3 - 5
-
pH 3: about 65% of maximal activity, pH 5: about 40% of maximal activity, substrate: (GlcNAc)5
3.3 - 4.7
-
pH 3.3: about 70% of maximal activity, pH 4.7: about 50% of maximal activity, substrate: N,N',N''-triacetyl chitotrioside
3.4 - 6.5
-
pH 3.4: about 40% of maximal activity, pH 6.5: about 40% of maximal activity, lytic activity towards Micrococcus lysodeikticus
4.5 - 8
-
pH 4.5: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
4.5 - 5.5
-
pH 4.5: about 60% of maximal activity, pH 5.5: about 70% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
4.5 - 6
-
pH 4.5: about 40% of maximal activity, pH 6.0: about 65% of maximal activity, at ionic strength 0.1
5 - 7
-
pH 5.0: about 50% of maximal activity, pH 7.0: about 90% of maximal activity, ionic strength 0.1
5 - 6.5
-
pH 5: about 60% of maximal activity, pH 6.5: about 50% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
5 - 7.5
5 - 7
5 - 9
5 - 7
-
pH 5.0: about 45% of maximal activity, pH 7.0: about 75% of maximal activity, isoenzyme SSTL B, ionic strength 0.1; pH 5.0: about 60% of maximal activity, pH 7.0: about 35% of maximal activity, isoenzyme SSTL A, ionic strength 0.1
5 - 6.5
-
pH 5: about 45% of maximal activity, pH 6.5: about 50% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
5.4 - 7.2
-
wild-type and two-active site lysozyme both retain over 80% activity as determined by assaying the lysis of Micrococcus lysodeikticus cells over a pH range of 5.3 to 7.2
6 - 7
pH 6.0: about 60% of maximal activity, pH 7.0: about 55% of maximal activity
6.5 - 8.5
-
from pH 6.5-8.5, the rising of the pH results in decrease in lytic activity of native enzyme and mutant _K1insK, but not _K1insK
6.5 - 7.5
-
pH 6.5: about 55% of maximal activity, pH 7.5: about 20% of maximal activity, at ionic strength 0.03
5 - 7.5
-
pH 5.0: about 75% of maximal activity, pH 7.5: about 40% of maximal activity
5 - 7
-
pH 5.0: wild-type enzyme shows about 80% of maximal activity, S6K-lysozyme and S7-lysozyme shows about 60% of maximal activity, pH 7.0: about 40% of maximal activity, wild-type enzyme, S6K-lysozyme and S7-lysozyme, lysis of Micrococcus lysodeikticus cells
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
40
42
50
60
25
assay at, lytic activity, substrate lyophilized cell wall of Micrococcus luteus
25
the optimal assay conditions determined for the recombinant His-tagged protein are in 0.1M potassium phosphate buffer, pH 6.6 containing 1 mM CuCl2 at 25°C
42
-
assay at, substrate 4-methylumbelliferyl-tetra N-acetyl-beta-chitotetraoxide
42
-
assay at, substrate 4-methylumbelliferyl-tetra N-acetyl-beta-chitotetraoxide
42
-
assay at, substrate 4-methylumbelliferyl-tetra N-acetyl-beta-chitotetraoxide
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 70
n-SalC lysozyme displays a sigmoidally increasing activity profile from 4°C to 70°C
5 - 50
10 - 60
-
10°C: about 60% of maximal activity, 60°C: about 60% of maximal activity
20 - 60
-
20°C: about 95% of maximal activity, 60°C: about 65% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
20 - 90
-
20°C: about 50% of maximal activity, 90°C: about 30% of maximal activity
20 - 60
-
20°C: about 85% of maximal activity, 60°C: about 75% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
22 - 60
native g-type lysozyme activity slowly increases from a relatively high lytic activity at 4°C (45% of maximum) to peak lytic activity at 60°C. The recombinant enzyme reaches maximum activity at 22°C, high catalytic activity at 4°C and no activity at 60°C
25 - 50
25°C: maximal activity, 45°C: about 90% of maximal activity, 50°C: about 40% of maximal activity
30 - 60
-
about 80% activity at 30°C, 100% activity at 40°C, about 40% activity at 50°C, about 15% activity at 60°C, no activity at 10, 20 or 70°C
5 - 50
-
5°C: about 55% of maximal activity, 50°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.1
9.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
murein hydrolase, endolysin Ply3626 of dual lysis system consisting of holin and endolysin
-
-
brenda
i-type lysozyme, two isozymes lysozyme A and lysozyme B
UniProt
brenda
isozyme OHLysG1, OHLysG2 and OHLysG3; isozyme OHLysG2; isozyme OHLysG3
-
-
brenda
collected from Xiaoyue River, Chaoyang district, Beijing
UniProt
brenda
T2, N20F, lambda, F1,F5, Kp, 2, Pf15, A-22, F12,13,14, P1,P14, N1 and others
-
-
brenda
bacteriophage of Xanthomonas oryzae pv. oryzae
SwissProt
brenda