Information on EC 3.2.1.17 - lysozyme

New: Word Map on EC 3.2.1.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.17
-
RECOMMENDED NAME
GeneOntology No.
lysozyme
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
hyrolysis of O-glycosyl bond
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-63-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolated from soil
-
-
Manually annotated by BRENDA team
isolated from soil
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. botrytis
-
-
Manually annotated by BRENDA team
turnip
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
dipterous
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
ATCC 824
-
-
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
enzyme induced in Salmonella typhimurium
-
-
Manually annotated by BRENDA team
phage T4 induced
-
-
Manually annotated by BRENDA team
Ficus sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene abLysI
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
subsp. cremoris, strain MG1363
SwissProt
Manually annotated by BRENDA team
strain XL 1
-
-
Manually annotated by BRENDA team
strain XL 1
-
-
Manually annotated by BRENDA team
2 forms CHIT24 and CHIT3
-
-
Manually annotated by BRENDA team
turkey
-
-
Manually annotated by BRENDA team
i-type lysozyme, two isozymes lysozyme A and lysozyme B
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
annelid
-
-
Manually annotated by BRENDA team
Cuvier tortoise
-
-
Manually annotated by BRENDA team
isozyme OHLysG1, OHLysG2 and OHLysG3; isozyme OHLysG2; isozyme OHLysG3
-
-
Manually annotated by BRENDA team
trout, c-type
-
-
Manually annotated by BRENDA team
soft tick
-
-
Manually annotated by BRENDA team
baboon
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
collected from Xiaoyue River, Chaoyang district, Beijing
UniProt
Manually annotated by BRENDA team
Pseudomonas bacteriophage
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
type c
-
-
Manually annotated by BRENDA team
i.e. Pleuronectes maximus
UniProt
Manually annotated by BRENDA team
wheat, multiple electrophoretic forms
-
-
Manually annotated by BRENDA team
phiIN93
UniProt
Manually annotated by BRENDA team
bacteriophage of Xanthomonas oryzae pv. oryzae
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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-tetra N-acetyl-beta-chitotetraoxide + H2O
?
show the reaction diagram
chitin + H2O
sugars
show the reaction diagram
chitohexaose + H2O
?
show the reaction diagram
-
-
-
?
chitohexaose + H2O
chitobiose + chitotetraose
show the reaction diagram
chitopentaose + H2O
?
show the reaction diagram
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotetraose + chitotriose
show the reaction diagram
-
amount in descending order, binding kinetics with chitotriose, overview
-
?
chitopentaose + H2O
N-acetyl-D-glucosamine + chitobiose + chitotriose + chitotetraose
show the reaction diagram
-
amount in descending order, binding kinetics with chitotriose, overview
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
colloidal chitin
sugars
show the reaction diagram
ethylene glycol chitin + H2O
sugars
show the reaction diagram
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
-
-
-
?
glycol chitin + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
sugars
show the reaction diagram
lyophilized cell wall of Micrococcus luteus + H2O
?
show the reaction diagram
Micrococcus lysodeikticus cell wall + H2O
?
show the reaction diagram
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
peptidoglycan + H2O
?
show the reaction diagram
peptidoglycan + H2O
N-acetylaminosaccharides
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peptidoglycan + H2O
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no metal cofactor required
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
activates
Co2+
-
increases the formation of lysozyme dimers
Mn
-
the reaction of the covalent (Mn(CO)3(H2O)2)+lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear NiMn complexes
Ni
-
the reaction of the covalent (Mn(CO)3(H2O)2)+lysozyme adduct with NiS4 and NiN2S2 complexes generates binuclear NiMn complexes
Zn2+
-
0.01 mM, activity is enhanced to 135% of control
additional information
no increase in activity at high ionic strength
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(GlcNAc)2
-
-
(GlcNAc)3
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
-
c-type inhibitor Ivy
complete inhibition
-
Ca2+
34% activation at 5 mM, 150% activation at 10 mM, 280% at 5 mM of recombinant enzyme. 58% Inhibition at 10 mM, 97% at 50 mM of native enzyme, 66% inhibition at 20 mM, 97% at 50 mM of recombinant enzyme; 87% inhibition at 5 mM, 93% at 10 mM
chitotetraose
dithiothreitol
-
-
F-actin
-
inhibition of the wild-type enzyme
-
g-type inhibitor PliG
complete inhibition
-
glutathione
-
-
glycol chitosan
-
-
-
histamine
Human serum albumin
-
the catalytic rate constant decreases tenfold when the albumin concentration increases, while the Michaelis constant remains almost constant in the albumin concentration range employed. Theoretical modeling of the structure of the human serum albumin-lysozyme complex shows that the Glu35 and Asp52 residues located in the active site of lysozyme are oriented toward the human serum albumin surface. This conformation will inactivate lysozyme molecules bound to human serum albumin, molecular dynamic calculations, overview
-
inhibitor of vertebrate lysozyme
lipoprotein
-
lipoprotein in bound form, in presence of 0-5 mM NaCl
-
lysozyme inhibitory protein Ivy
-
homodimeric antitoxin, inhibitor of vertebrate lysozyme, from Escherichia coli
-
mucin
-
inactivation of the wild-type enzyme at high concentrations
-
N,N',N''-triacetylchitotriose
-
competitive. Preincubation at neutral pH impairs aggregation of lysozyme and fibrillogenesis at pH 12.2. Lysozyme-chitotriose complex at pH 12.2 displays reduced thioflavin T and 8-anilino-1-naphthalene sulfonic acid fluorescence, small oligomers but no amyloid fibrils, absence of large aggregates, marginally more helical content, and more than 70% of enzymatic activity after 24 h
N-acetylglucosamine
N-acetylmuramic acid
-
-
N-bromosuccinimide
-
pH 4
Na+
14% inhibition at 10 mM, 81% at 100 mM; activates the native enzyme 3.43fold at 50 mM, the recombinant enzyme 4.3fold at 100 mM, inhibition of native, not recombinant, enzyme at 200 mM
Nuclear lysozyme inhibitor
-
other subcellular lysozymes except nuclear are unaffected
-
PliC
-
i.e. periplasmic lysozyme inhibitor of c-type lysozyme, isolated by affinity chromatography from a periplasmic extract of Salmonella enteritidis and related to a group of proteins with a common conserved COG3895 domain
-
PliI
-
periplasmic lysozyme inhibitor of the I-type lysozyme from Aeromonas hydrophila has a high affinity for I-type lysozyme, but does not bind or inhibit vertebrate C- or G-type lysozymes
-
poly-alpha,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
poly-gamma,D-Na-glutamate
-
in presence of 0-100 mM NaCl
-
poly-L-lysine
-
-
porcine gastric 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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-dimethylimidazolium iodine
-
50% activation at 5%
-
1-butyl-3-methylimidazolium bromide
-
below 20% activation at 5%
-
1-butyl-3-methylimidazolium chloride
-
below 10% activation at 5%
-
1-butyl-3-methylimidazolium tetrafluoroborate
-
below 20% activation at 5%
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.001
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside
8.33
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
p-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta
Homo sapiens
-
-
-
0.076
p-nitrophenyl-N,N',N'',N''',N''''-pentaacetylchitopentaose
Liolophura japonica
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
620
purified lysozyme A, pH 7.0, 25C
1227
purified lysozyme B, pH 7.0, 25C
12500
purified enzyme, pH 6.0, temperature not specified in the publication
18800
purified enzyme, pH 6.0, temperature not specified in the publication
31050
pH 7.0, 70C
37600
-
purified native enzyme, substrate Micrococcus lysodeikticus cell walls, pH 6.0, 25C
40000
-
pH 6.2-6.3, 25C
48330
purified recombinant enzyme, pH 6.0, 22C, substrate lyophilized Micrococcus lysodeikticus
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
-
4.5 - 5.5
-
-
4.7
-
substrate: N,N',N''-triacetylchitotrioside
5 - 8
-
-
5 - 8
-
-
5 - 5.5
-
-
5 - 7
-
assay at
5 - 8
-
-
5.2 - 6
assay at; assay at
5.5 - 6
5.5
lytic activity against Micrococcus lysodeikticus
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
6.2
-
assay at
6.3
-
assay at
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 25C
6.8
-
at ionic strength 0.03
7.5 - 8.5
-
-
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
activity range
3 - 7
-
-
3 - 5
-
pH 3: about 65% of maximal activity, pH 5: about 40% of maximal activity, substrate: (GlcNAc)5
3 - 8
-
activity range, profile overview
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
-
-
3.5 - 8
-
immobilized enzyme, activity range, profile overview
4.4 - 6.4
-
pH 4.4 and pH 6.4: more than 50% of maximal activity
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 - 9.5
-
-
4.5 - 6
-
pH 4.5: about 40% of maximal activity, pH 6.0: about 65% of maximal activity, at ionic strength 0.1
4.8 - 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 - 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 - 9
-
activity range, recombinant enzyme
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
5.3 - 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
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
additional information
active at acidic pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
substrate: lyophilized cell wall of Micrococcus luteus
35
-
lytic activity towards Micrococcus lysodleikticus
37 - 42
-
assay at
40
assay at
65
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 70
n-SalC lysozyme displays a sigmoidally increasing activity profile from 4C to 70C
5 - 50
10 - 60
-
10C: about 60% of maximal activity, 60C: about 60% of maximal activity
15 - 70
-
-
20 - 60
-
activity range
20 - 80
-
immobilized enzyme, activity range, profile overview
20 - 60
-
20C: about 95% of maximal activity, 60C: about 65% of maximal activity, substrate: lyophilized cell wall of Micrococcus luteus
20 - 90
-
20C: about 50% of maximal activity, 90C: about 30% of maximal activity
20 - 60
-
20C: about 85% of maximal activity, 60C: 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 4C (45% of maximum) to peak lytic activity at 60C. The recombinant enzyme reaches maximum activity at 22C, high catalytic activity at 4C and no activity at 60C
25 - 50
25C: maximal activity, 45C: about 90% of maximal activity, 50C: about 40% of maximal activity
30 - 90
-
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-990
-
pI is greater than 9.5 as determined by isoelectric focusing
4.9
sequence calculation
6.38
sequence calculation
6.4
-
isoelectric focusing
7.1
sequence calculation
7.65
-
-
7.7
calculated
7.88
calculated from sequence
8.03
sequence calculation
8.44
-
theoretical pI
8.8
calculated
additional information
-
greater than 10
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
weak enzyme expression in the conjuctival sample, strong expression in the lacrimal gland sample
Manually annotated by BRENDA team
-
3 lysozymes c
Manually annotated by BRENDA team
-
11fold lower compared to expression in hepatopancreas; low expression level, 1736fold lower compared to expression in hepatopancreas; low expression level, 613fold lower compared to expression in hepatopancreas
Manually annotated by BRENDA team
-
unstimulated
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
leukemia patients
Manually annotated by BRENDA team
additional information