Information on EC 3.2.1.17 - lysozyme

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The expected taxonomic range for this enzyme is: Viruses

EC NUMBER
COMMENTARY
3.2.1.17
-
RECOMMENDED NAME
GeneOntology No.
lysozyme
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis
-
cleaving the beta-1,4 glycosidic bond between N-acetyl-D-glucosamine (NAG) and N-acetylmuramic acid (NAM) in the peptidoglycan layer
hydrolysis
Q17005
hydrolyze the beta-1,4-glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine of peptidoglycan
hydrolysis
-
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
-
catalyzes the hydrolysis of bacterial cell walls
hydrolysis
-
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
-
lysozyme hydrolyses 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan
hydrolysis of O-glycosyl bond
-
-
-
-
hyrolysis of O-glycosyl bond
Q8SD18
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,4-beta-N-acetylmuramidase
-
-
-
-
1,4-beta-N-acetylmuramidase 1
Q7YT16
-
1,4-beta-N-acetylmuramidase A/C
-
-
-
-
1,4-beta-N-acetylmuramidase M1
-
-
-
-
1,4-beta-N-acetylmuramoylhydrolase
-
-
-
-
1,4-N-acetylmuramidase
-
-
-
-
AcmB
Q8KKF9
-
Autolysin
-
-
-
-
BA-lysozyme
Bufo andrewsi
-
-
c-type lysozyme
-
-
CP-1 lysin
-
-
-
-
CP-7 lysin
-
-
-
-
CP-9 lysin
-
-
-
-
CPL
-
-
-
-
Endolysin
-
-
-
-
equine lysozyme
-
-
fOg44 endolysin
-
-
g-lysozyme
-
-
g-type lysozyme
-
-
g-type lysozyme
Q86SG7
-
g-type lysozyme
-
-
GEWL
-
-
globulin G
-
-
-
-
globulin G1
-
-
-
-
goose type lysozyme
-
-
Goose-type lysozyme
-
-
-
-
Goose-type lysozyme
Q075V3
-
Goose-type lysozyme
Q86SG7
-
Goose-type lysozyme
-
-
Goose-type lysozyme
-
-
Goose-type lysozyme
A6PZ97
-
HLysG2
Q86SG7
-
i-type lysozyme
-
-
L-7001
-
-
-
-
Late protein gp15
-
-
-
-
Lys-rich lysozyme 2
Q7YT17
-
Lysis protein
-
-
-
-
Lysosyme
-
-
-
-
lysozym
-
-
Lysozyme
-
-
-
-
Lysozyme
-
-
lysozyme 1
Q7YT16
precursor
lysozyme 1 precursor
Q7YT16
-
lysozyme c
Q7YT16
-
lysozyme c-1
-
-
lysozyme g
-
-
-
-
lysozyme g-like 2
Q86SG7
-
lysozyme SP0987
-
-
Mdl1
Q7YT16
-
mucopeptide glucohydrolase
-
-
-
-
mucopeptide N-acetylmuramic acid hydrolase
-
-
mucopeptide N-acetylmuramoylhydrolase
-
-
-
-
muramidase
-
-
-
-
muramidase
-
-
muramidase
-
-
MV1 lysin
-
-
-
-
N,O-diacetylmuramidase
-
-
-
-
N-acetylglucosaminidase autolysin
Q8KKF9
-
Outer wedge of baseplate protein
-
-
-
-
P13
-
-
-
-
Peptidoglycan hydrolase
-
-
-
-
phiKZ endolysin
Q8SD18
-
Ply3626
-
endolysin of bacteriophage phi3626
PR1-lysozyme
-
-
-
-
Protein gp17
-
-
-
-
Protein gp19
-
-
-
-
Protein Gp25
-
-
-
-
Protein Gp5
-
-
-
-
Protein gp54
-
-
-
-
Protein gpK
-
-
-
-
SalG
-
-
SalG
A6PZ97
-
transglycosylase
Q8SD18
-
VpLYZ
-
invertebrate type lysozyme
CAS REGISTRY NUMBER
COMMENTARY
9001-63-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Kaki and wild-type; multiple forms; Peking-duck
-
-
Manually annotated by BRENDA team
Peking-duck
-
-
Manually annotated by BRENDA team
isoform Lys i-1
UniProt
Manually annotated by BRENDA team
isoform Lys i-2
A4ZWD2
UniProt
Manually annotated by BRENDA team
goose
-
-
Manually annotated by BRENDA team
4 isoforms
-
-
Manually annotated by BRENDA team
gastric mucosa: 3 lysozymes c, other tissues: no lysozyme c, low levels of another lysozyme, g class
-
-
Manually annotated by BRENDA team
Bufo andrewsi
-
-
-
Manually annotated by BRENDA team
dipterous
-
-
Manually annotated by BRENDA team
murein hydrolase, endolysin Ply3626 of dual lysis system consisting of holin and endolysin
-
-
Manually annotated by BRENDA team
Colitis bacteriophage
-
-
-
Manually annotated by BRENDA team
expressed from Escherichia coli TG-1 carrying plasmid pHDM10
-
-
Manually annotated by BRENDA team
synthesized in Escherichia coli
-
-
Manually annotated by BRENDA team
enzyme induced in Salmonella typhimurium
-
-
Manually annotated by BRENDA team
enzyme is product of e gene for lysis from within, or gene 5 for lysis from without
-
-
Manually annotated by BRENDA team
wild-type and mutant
-
-
Manually annotated by BRENDA team
expression of recombinant Ca2+-binding lysozyme in Aspergillus niger
-
-
Manually annotated by BRENDA team
phage T4 induced
-
-
Manually annotated by BRENDA team
Ficus sp.
-
-
-
Manually annotated by BRENDA team
101-succinimide lysozyme
-
-
Manually annotated by BRENDA team
expression of recombinant Ca2+-binding lysozyme in Aspergillus niger
-
-
Manually annotated by BRENDA team
human cell lines HeLa and MCF-7
-
-
Manually annotated by BRENDA team
two domains crosslinked between Trp62 and Asp101
-
-
Manually annotated by BRENDA team
wild-type and engineered enzyme expressed in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
expression of recombinant Ca2+-binding lysozyme in Aspergillus niger
-
-
Manually annotated by BRENDA team
gene expression in: Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
subsp. cremoris, strain MG1363
SwissProt
Manually annotated by BRENDA team
strain XL 1
-
-
Manually annotated by BRENDA team
Lysobacter sp. XL 1
strain XL 1
-
-
Manually annotated by BRENDA team
2 forms CHIT24 and CHIT3
-
-
Manually annotated by BRENDA team
digestive lysozymes 1 and 2, i.e. MdL1 and MdL2
-
-
Manually annotated by BRENDA team
house fly
-
-
Manually annotated by BRENDA team
Lys-rich lysozyme 2 fragment
SwissProt
Manually annotated by BRENDA team
Cuvier tortoise
-
-
Manually annotated by BRENDA team
trout, c-type
-
-
Manually annotated by BRENDA team
K-187, two extracellular forms FI and FII
-
-
Manually annotated by BRENDA team
pyocinogenic
-
-
Manually annotated by BRENDA team
Pseudomonas bacteriophage
UniProt
Manually annotated by BRENDA team
-
A9LN31, A9LN32
UniProt
Manually annotated by BRENDA team
type c
-
-
Manually annotated by BRENDA team
ostrich
-
-
Manually annotated by BRENDA team
wheat, multiple electrophoretic forms
-
-
Manually annotated by BRENDA team
phiIN93
UniProt
Manually annotated by BRENDA team
T2, N20F, lambda, F1,F5, Kp, 2, Pf15, A-22, F12,13,14, P1,P14, N1 and others
-
-
Manually annotated by BRENDA team
unidentified phage phiIN93
phiIN93
UniProt
Manually annotated by BRENDA team
bacteriophage of Xanthomonas oryzae pv. oryzae
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Q86SG7
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
-
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(GlcNAc)5 + H2O
?
show the reaction diagram
-
-
-
-
?
(GlcNAc)6 + H2O
(GlcNAc)3
show the reaction diagram
-
-
and smaller amounts of (GlcNAc)2 and (GlcNAc)4 endo-splitting, hydrolyzes preferentially the third glycosidic linkage from the nonreducing end
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
chitin + H2O
sugars
show the reaction diagram
-
-
reducing
?
chitin + H2O
sugars
show the reaction diagram
-
not
-
-
-
chitopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
-
not
-
-
-
colloidal chitin
sugars
show the reaction diagram
-
-
-
-
?
colloidal chitin
sugars
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
-
reducing
?
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
not
-
-
-
ethylene glycol chitin + H2O
sugars
show the reaction diagram
-
not
-
-
-
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + (GlcNAc)2
show the reaction diagram
-
-
main products
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + ?
show the reaction diagram
-
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
show the reaction diagram
P00718
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-, P80189
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-, P80190
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
-
-
reducing
?
glycol chitin + H2O
sugars
show the reaction diagram
-
not
-
-
-
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose
show the reaction diagram
-
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
-
-
?
N,N',N''-triacetylchitotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
NodRm-IV + H2O
NodRm-II + NodRm-III
show the reaction diagram
-
-
-
?
NodRm-IV(Ac,S) + H2O
NodRm-II + NodRm-III
show the reaction diagram
-
-
-
?
NodRm-IV(S) + H2O
NodRm-II + NodRm-III
show the reaction diagram
-
-
-
?
NodRm-V(S) + H2O
NodRm-II + NodRm-III
show the reaction diagram
-
-
-
?
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
anti-tumor activity, involvement in host defence, anti-metastatic activity
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
digestive enzyme
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-, Q8KKF9
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
Bufo andrewsi
-
enzyme displays lytic activity against Micrococcus lysodeikticus, Staphylococcus aureus and Escherichia coli
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lyophilized cell wall of Micrococcus luteus
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lysis of Micrococcus lysodeikticus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
cell wall of Micrococcus luteus. Tyr34, Tyr45, Pro47, Pro102, and Asn114 are the amino acids contributing to the substrate binding
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
LysgaY lysed over 20 heated Gram-positive bacterial species as the substrates, including lactobacilli, lactococci, enterococci, micrococci, and staphylococci
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lytic activity against Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lytic activity against Micrococcus lysodeikticus
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
lytic activity against Micrococcus lysodeiktikus cells
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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, 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
?
show the reaction diagram
A1BPG9
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
N-acetylaminosaccharides
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
N-acetylaminosaccharides
show the reaction diagram
-
-
C3 and C6 muropeptides
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
Micrococcus lysodeikticus cells
-
-
-
additional information
?
-
-
cell walls of Clostridium acetobulyticum, not: Micrococcus cells, beta-N-acetyl chitotetraoside
-
-
-
additional information
?
-
-
not: p-nitrophenyl-N-acetylglucosaminide
-
-
-
additional information
?
-
-
not: Micrococcus luteus cells
-
-
-
additional information
?
-
-
Micrococcus luteus
-
-
-
additional information
?
-
-
Micrococcus luteus
-
-
-
additional information
?
-
-
high chitinase activity
-
-
-
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
?
-
-
gram-negative bacteria better substrate than gram-positive bacteria
-
-
-
additional information
?
-
-
phage T4: e lysozyme more specific than hen egg-white lysozyme, e lysozyme: hydrolysis of murein chains in which N-acetylmuraminic acid is substituted by peptide side chains L-Ala-D-Glu-meso-diaminopimelic acid-D-Ala
-
-
-
additional information
?
-
-
often acts as chitinase: EC 3.2.1.14
-
-
-
additional information
?
-
-
often acts as chitinase: EC 3.2.1.14
-
-
-
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
?
-
-
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
?
-
-
lysozyme has inhibitory effects on the proliferation of vascular endothelial cell in vitro
-
-
-
additional information
?
-
-
lysozyme inhibits Clostridium perfringens type A and its alpha-toxin production
-
-
-
additional information
?
-
-
lysozyme is able to kill Entamoeba histolytica trophozoites
-
-
-
additional information
?
-
-
the enzyme shows lytic activity towards Micrococcus lysodeikticus
-
-
-
additional information
?
-
Q8IT75
enzyme exhibits potent lytic activities against fish pathogens
-
-
-
additional information
?
-
Q859R8
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
-
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
?
-
B3GQR5
recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria
-
-
-
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, a suspension of Micrococcus lysodeikticus is used as a substrate
-
-
-
additional information
?
-
Q86SG7
a suspension of Micrococcus lysodeikticus is used as a substrate for HLysG2
-
-
-
additional information
?
-
-
cell walls of Micrococcus lysodeikticus, are a substrate, while those of Xanthomonas campestris pv. malvacearum and Xanthomonas oryzae pv. oryzae are no substrates
-
-
-
additional information
?
-
-
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
?
-
-
lysis of Micrococcus luteus bacteria, the double mutant lyses bacteria effectively at alginate, mucin and DNA concentrations that inactivate wild-type enzyme
-
-
-
additional information
?
-
-
Micrococcus luteus cells in the exponential growth phase are used as substrate
-
-
-
additional information
?
-
unidentified phage 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
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
anti-tumor activity, involvement in host defence, anti-metastatic activity
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
cell lysis from within, at the end of latent period, cell lysis from without, at the beginning of infection
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
digestive enzyme
-
-
-
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
?
-
Q8IT75
enzyme exhibits potent lytic activities against fish pathogens
-
-
-
additional information
?
-
Q859R8
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
-
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
?
-
B3GQR5
recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria
-
-
-
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
additional information
-
Q8SD18
cleaves the glycosidic linkage between N-acetylmuramoyl and N-acetylglucosaminyl residues
formation of a 1,6-anhydromuramoyl product
-
-
additional information
?
-
unidentified phage phiIN93
Q859R8
enzyme lyses specifically Thermus aquaticus cells, with 79% activity on Thermus fhermophilus HB8 and 76% activity on Thermus filífformis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no metal cofactor required
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
activates
Ca2+
-
activates
Ca2+
-
binding sites
Ca2+
-
binding sites
Ca2+
-
binding sites
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
CaCl2
-
activates, maximal activity at 0.035 M
Co2+
-
increases the formation of lysozyme dimers
Cu2+
-
activates
Cu2+
-
0.01 mM, activity is enhanced to 128% of control
Cu2+
A1BPG9
1.0 mM, activity is increased by 54%
Mg2+
-
no effect: ghost lysozyme
Mg2+
-
increases activity in phage T4 e lysozyme
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
MgCl2
-
activates, maximal activity at 0.035 M
Mn
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
Na+
Q86SG7
activates, best at 75 mM
NaCl
-
activates
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
Ni
-
the reaction of the covalent (Mn(CO)3(H2O)2)+–lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear Ni–Mn complexes
Zn2+
-
0.01 mM, activity is enhanced to 135% of control
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(GlcNAc)2
-
-
(GlcNAc)3
-
-
(GlcNAc)3
P80189
-
(GlcNAc)3
P80190
-
2-mercaptoethanol
-
-
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
-
DNA
-
DNA from herring sperm, in presence of 0-50 mM NaCl
DNA
-
inactivation of the wild-type enzyme at high concentrations
EDTA
-
above 0.1 mM
EDTA
A1BPG9
at 10 and 20 mM causes 15% and 43% reduction of the enzyme activity
F-actin
-
inhibition of the wild-type enzyme
-
glycol chitosan
-
-
-
histamine
Ficus sp.
-
-
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
-
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
-
lipoprotein
-
lipoprotein in bound form, in presence of 0-5 mM NaCl
-
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
-
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-acetylglucosamine
-
-
N-acetylglucosamine
-
-
N-acetylglucosamine
-
-
N-acetylglucosamine
-
-
N-acetylglucosamine
Ficus sp.
-
-
N-acetylglucosamine
-
-
N-acetylglucosamine
-
-
N-acetylmuramic acid
-
-
N-bromosuccinimide
-
pH 4
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
-
poly-L-lysine
-
-
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
-
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
Mn2+
-
0.01 M, 17% inhibition
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 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
-
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
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
-
additional information
-
Escherichia coli inhibitor of vertebrate lysozyme, Ivy, is not inhibitory
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
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
additional information
-
practically inactive in absence of Triton X-100, hydrolysis of murein catalysed only when in contact with lipophilic components
-
additional information
Q859R8
no activation by 2-mercaptoethanol
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0008
-
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
-
human serum albumin-bound enzyme, pH 5.2, 37°C
8.33
-
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
-
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.015
-
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
-
-
-
0.076
-
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.387
-
-
substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
2.98
-
-
substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
4.32
-
-
substrate: p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
31050
-
Q859R8
pH 7.0, 70°C
additional information
-
-
-
additional information
-
-
139.8 1/min * mg: decrease in absorbance
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
P80189
-
additional information
-
P80190
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
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
-
-
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
-
-
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
-
A1BPG9
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
Q8KKF9
assay at
4
-
-
substrate: (GlcNAc)5
4
-
-
lytic activity towards Micrococcus lysodeikticus
4.5
5.5
-
-
4.7
-
-
substrate: N,N',N''-triacetylchitotrioside
5
5.5
-
-
5
7
-
assay at
5
-
-
-
5
-
-
substrate: lyophilized cell wall of Micrococcus luteus
5.2
-
-
at ionic strength 0.1
5.2
-
-
assay at
5.5
-
P80189
assay at
5.5
-
P80190
assay at
5.5
-
-
-
5.5
-
-
substrate: lyophilized cell wall of Micrococcus luteus
5.9
-
-
wild-type enzyme, lytic activity against Micrococcus lysodeikticus
6
7
-
the optimal pH of rHLZ varies with salt concentration of the buffer, recombinant enzyme
6
-
-
lysis of Micrococcus lysodeikticus cells
6
-
-
substrate: lyophilized cell wall of Micrococcus luteus
6
-
Bufo andrewsi
-
-
6
-
-
ionic strength 0.1
6
-
-
dual pH-optimum at pH 6.0 and 8.0, ionic strength 0.1
6
-
-
isoenzyme SSTL A, ionic strength 0.1; isoenzyme SSTL B, ionic strength 0.1
6
-
-
native enzyme and mutant enzyme _K1insN
6
-
Q8IT75
-
6
-
Q86SG7
recombinant enzyme
6.2
-
-
assay at
6.4
-
-
-
6.5
-
-
-
6.5
-
-
two-active site lysozyme, lytic activity against Micrococcus lysodeikticus
6.5
-
-
lytic activity towards Micrococcus lysodleikticus
6.6
-
A1BPG9
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
6.8
-
-
at ionic strength 0.03
7
-
-
-
7
-
-
mutant _K1insK
7
-
-
assay at
7
-
-
assay at
8
-
-
dual pH-optimum at pH 6.0 and 8.0, ionic strength 0.1
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
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
5
-
pH 3: about 65% of maximal activity, pH 5: about 40% of maximal activity, substrate: (GlcNAc)5
3
7
-
-
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
3.5
7
-
-
4.4
6.4
-
pH 4.4 and pH 6.4: more than 50% 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
4.5
8
-
pH 4.5: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
4.8
5.6
-
pH 4.8 and pH 5.6: more than 50% of maximal activity
4.8
6.2
-
more than 50% activity in the pH range
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
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
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
5
7
-
pH 5.0: about 50% of maximal activity, pH 7.0: about 90% of maximal activity, ionic strength 0.1
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
7.5
-
60% of maximal activity within the range pH 5.0-7.5
5
7.5
Bufo andrewsi
-
pH 5.0: about 75% of maximal activity, pH 7.5: about 40% of maximal activity
5
9
-
activity range, recombinant enzyme
5.3
8
-
pH 5.3 and pH 8.0: more than 50% of maximal activity
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
A1BPG9
pH 6.0: about 60% of maximal activity, pH 7.0: about 55% of maximal activity
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
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
additional information
-
Q8KKF9
active at acidic pH
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
A1BPG9
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
25
-
-
assay at
30
40
-
substrate: lyophilized cell wall of Micrococcus luteus
30
-
-
-
30
-
-
-
30
-
Q86SG7
recombinant enzyme
35
-
-
lytic activity towards Micrococcus lysodleikticus
37
42
-
assay at
37
-
Q8KKF9
assay at
37
-
-
assay at
40
-
P80189
assay at
40
-
P80190
assay at
40
-
-
assay at
40
-
-
substrate: lyophilized cell wall of Micrococcus luteus
40
-
Q8IT75
-
40
-
-
recombinant enzyme
50
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
50
-
5°C: about 70% of maximal activity, 50°C: about 40% of maximal activity
5
50
-
5°C: about 55% of maximal activity, 50°C: about 65% of maximal activity
10
60
-
10°C: about 60% of maximal activity, 60°C: about 60% of maximal activity
15
70
-
-
20
60
-
20°C: about 95% of maximal activity, 60°C: about 65% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
20
60
-
20°C: about 85% of maximal activity, 60°C: about 75% 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
25
50
A1BPG9
25°C: maximal activity, 45°C: about 90% of maximal activity, 50°C: about 40% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-990
-
-
pI is greater than 9.5 as determined by isoelectric focusing
4.7
-
A4ZWD2, Q7QHB9
calculated
4.8
-
A4ZWD2, Q7QHB9
calculated
4.9
-
Q8KKF9
sequence calculation
6.4
-
-
isoelectric focusing
6.8
-
A9LN31, A9LN32
calculated
7.7
-
B3GQR5
calculated
7.88
-
-, Q075V3
calculated from sequence
8.44
-
-
theoretical pI
8.5
-
A9LN31, A9LN32
calculated
8.8
-
Q8IT75
calculated
9.1
-
Bufo andrewsi
-
calculated from sequence
9.1
-
-, Q19R28
calculated
9.3
-
-
-
additional information
-
-
greater than 10
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q86SG7
weak enzyme expression in the conjuctival sample, strong expression in the lacrimal gland sample
Manually annotated by BRENDA team
-
of larvae. 1 h after infection with Pseudomonas aeruginosa, increase in lysozyme content is detecable, with a significant decrease after a prolonged infection time
Manually annotated by BRENDA team
A4ZWD2, Q7QHB9
of adult female; of adult female
Manually annotated by BRENDA team
A9LN31, A9LN32
; predominant expression after injection of bacteria
Manually annotated by BRENDA team
-
3 lysozymes c
Manually annotated by BRENDA team
-
constitutively expressed
Manually annotated by BRENDA team
Q8IT75
high mRNA expression
Manually annotated by BRENDA team
-
constitutively expressed
Manually annotated by BRENDA team
-
of larvae. 1 h after infection with Pseudomonas aeruginosa, increase in lysozyme content is detecable, with a significant decrease after a prolonged infection time
Manually annotated by BRENDA team
Q8IT75
high mRNA expression
Manually annotated by BRENDA team
-
of larvae. Increase in lysozyme level during the first 30 h after infection with Pseudomonas aeruginosa
Manually annotated by BRENDA team
Q8IT75
high mRNA expression
Manually annotated by BRENDA team
-
constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine
Manually annotated by BRENDA team
-
constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine
Manually annotated by BRENDA team
-
salivary gland. Expression is not detected on day 0 of the fifth-instar, but reaches the highest level on day 1 and decreases thereafter. mRNA level is the highest from larva fed on tomato, followed by cotton and tobacco, with larvae fed on artificial diet being the lowest
Manually annotated by BRENDA team
Ficus sp.
-
-
Manually annotated by BRENDA team
-
constitutively expressed
Manually annotated by BRENDA team
A4ZWD2, Q7QHB9
of adult female
Manually annotated by BRENDA team
-
activity reaches highest level in 4-8 days old mosquitoes
Manually annotated by BRENDA team
A4ZWD2, Q7QHB9
blood feeding results in significantly increased transcript abundance; blood feeding results in significantly increased transcript abundance
Manually annotated by BRENDA team
B3GQR5
high protein expression
Manually annotated by BRENDA team
A9LN31, A9LN32
predominant expression after ingestion of Trypanosoma cruzi in a bloodmeal, or after injection of bacteria
Manually annotated by BRENDA team
-
equilibrium and kinetics of the folding and unfolding of lysozyme
Manually annotated by BRENDA team
-
of larva. Expression is not detected on day 0 of the fifth-instar, but reaches the highest level on day 1 and decreases thereafter. mRNA level is the highest from larva fed on tomato, followed by cotton and tobacco, with larvae fed on artificial diet being the lowest
Manually annotated by BRENDA team
-
activity reaches highest level in 4-8 days old mosquitoes
Manually annotated by BRENDA team
Bufo andrewsi
-
-
Manually annotated by BRENDA team
-
constitutively expressed, quickly up-regulated upon stimulation with trivalent bacterial vaccine
Manually annotated by BRENDA team
-
fundic region highest activity
Manually annotated by BRENDA team
-
leukemia patients
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-, Q19R28
gene expression is transiently enhanced at the onset of metamorphosis. Expression is up-regulated after the injection of Escherichia coli or entomopathogenic fungi, but shows different expression patterns
Manually annotated by BRENDA team
additional information
B3GQR5
low expression at embryo stage. MRNA is upregulated 2 h post bacterial challenge, maintained for 6 h, and slightly declines from 12 to 24 h post-injection
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Canis familiaris
Canis familiaris
Canis familiaris
Canis familiaris
Canis familiaris
Coturnix coturnix japonica
Escherichia coli (strain K12)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Venerupis philippinarum
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10000
-
-
gel filtration
11000
13000
-
Archibald sedimentation equilibrium method
14000
14850
-
4 isoforms, ion spray mass spectometry
14000
16000
-
sedimentation velocity, short-column sedimentation equilibrium, amino acid analysis
14000
-
-
MALDI-TOF mass spectrometry
14000
-
-
-
14120
-
-
MADI-TOF
14300
-
-
gel filtration
14310
-
-
FT-ICR mass spectroscopy
14400
-
-
gel filtration
14600
-
-
-
14660
-
-
ESI mass spectroscopy
15000
17000
-
analytical ultracentrifugation
15000
-
-
gel filtration
15000
-
-
gel filtration
15000
-
-
amino acid analysis
15000
-
-
12% SDS-PAGE
15400
-
-
sedimentation and diffusion coefficient values, low speed sedimentation, Archibald's method, amino, acid composition
17600
-
-
sedimentation analysis, sequential analysis
17900
-
-
sedimentation equilibrium data, sedimentation and diffusion coefficient
18500
-
-
ultracentrifugation
18600
-
-
amino acid composition
19000
-
-
low speed sedimentation, Archibald's method
20870
-
-
the ORF encoded a protein of 185 amino acid residues with a calculated molecular mass of 20.87 kDa
23200
-
-
gel filtration
24000
-
-
gel filtration
24000
-
-
CHIT24, gel filtration
25000
-
-
gel filtration
28800
-
Q8SD18
calculated molecular mass
29000
-
Ficus sp.
-
ultracentrifugation
30000
-
-
FII, gel filtration
36000
-
-
CHIT36, gel filtration
44000
-
-
gel filtration
60000
-
-
FI, gel filtration
200000
-
-
gel filtration
250000
-
-
ultracentrifugation
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 55000, SDS-PAGE
?
-
x * 14500, SDS-PAGE
?
-
x * 38800, SDS-PAGE
?
Q8KKF9
x * 57100, sequence calculation
?
-
x * 20884, SELDI-TOF
?
-
x * 17771.5, two potential forms of enzyme: 17771.5 Da and 17861 Da, MALDI-MS; x * 17861, MALDI-MS; x * 18400, SDS-PAGE
?
Bufo andrewsi
-
x * 14745, calculated from sequence; x * 15000, SDS-PAGE
?
-
x * 14400, SDS-PAGE
?
-
x * 15800, SDS-PAGE; x * 16464, matrix-assisted laser desorption ionization time-of-flight mass spectrometry
?
-
x * 21300, calculated from sequence
?
-
x * 12000, SDS-PAGE
?
-
x * 15800, SDS-PAGE
?
-, Q075V3
x * 20010, calculated from sequence
?
-, Q19R28
x * 15600, calculated and SDS-PAGE of recombinant protein
?
Q859R8
x * 33000, SDS-PAGE, x * 33141, calculated
?
-
x * 14672, calculated
?
A4ZWD2, Q7QHB9
x * 14860, calculated, mature protein; x * 15880, calculated, mature protein
?
B3GQR5
x * 13800, calculated
?
A9LN31, A9LN32
x * 15100, calculated; x * 15800, calculated
?
Q8IT75
x * 16320, calculated, x * 16000, SDS-PAGE
?
Q86SG7
x * 21508, sequence calculation
?
-
x * 14679.14, mass spectrometry
?
unidentified phage phiIN93
-
x * 33000, SDS-PAGE, x * 33141, calculated
-
dimer
-
2 * 30000, SDS-PAGE
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 remain