Information on EC 4.2.2.1 - hyaluronate lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.2.1
-
RECOMMENDED NAME
GeneOntology No.
hyaluronate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hyaluronan degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
hyaluronate lyase
The enzyme catalyses the degradation of hyaluronan by a beta-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
CAS REGISTRY NUMBER
COMMENTARY hide
37259-53-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
several different isozymes
-
-
Manually annotated by BRENDA team
different strains isolated from different host organisms, e.g. human, penguin, armadillo, and from dog food
-
-
Manually annotated by BRENDA team
strain 8325-4, gene hysA
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
prophage encoded
SwissProt
Manually annotated by BRENDA team
capsular and acapsular phenotype, contains 2 forms: a extracellular and a bacteriophage enzyme
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Streptomyces hyalurolytics
-
-
-
Manually annotated by BRENDA team
Streptomyces hyalurolyticus
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to PL subfamily 8, which has an overall alpha/alpha + beta architecture
malfunction
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
chondroitin
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine
show the reaction diagram
-
non-progressive mode
unsaturated disaccharide units
-
?
chondroitin 4-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
chondroitin 6-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
chondroitin sulfate
?
show the reaction diagram
chondroitin sulfate
GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)
show the reaction diagram
-
-
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-(beta-D-gluco-4-enepyranosyluronic acid)-glucose
show the reaction diagram
-
-
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
show the reaction diagram
-
from human umbilical cord
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
hyaluronan
?
show the reaction diagram
hyaluronan
fully O-sulfated oligosaccharides
show the reaction diagram
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, sodium salt, large scale depolymerization
chain length of 4-20, detection and composition analysis
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
hyaluronan + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate
show the reaction diagram
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, degradation
-
-
?
hyaluronan + H2O
oligosaccharides
show the reaction diagram
-
specific for, degradation
-
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
hyaluronan tetrasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
unsaturated disaccharide units
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
hyaluronate
?
show the reaction diagram
-
efficient degradation of hyaluronate
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
hyaluronate hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
unsaturated disaccharide
-
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
hyaluronic acid
?
show the reaction diagram
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
hyaluronic acid polymer
hyaluronic acid tetrasaccharide + hyaluronic acid hexasaccharide
show the reaction diagram
Streptomyces hyalurolyticus
-
hyaluronic acid purified from Mytilus galloprovincialis
-
-
?
tetrasaccharides with a 6-sulfated disaccharide at the reducing end
?
show the reaction diagram
-
-
-
-
?
unsulfated chondroitin
?
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
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
hyaluronan
?
show the reaction diagram
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
hyaluronate
?
show the reaction diagram
-
efficient degradation of hyaluronate
-
-
?
hyaluronic acid
?
show the reaction diagram
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
Streptomyces hyalurolyticus
-
-
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(13Z)-docos-13-enoic acid
(25S)-(+)-12alpha-hydroxy-3alpha-methylcarboxyacetate-24-methyllanosta-8,24(31)-diene-26-oic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0035 mM
(2E)-1-furan-2-yl-3-(4-nitrophenyl)prop-2-en-1-one
IC50 at enzyme optimum pH 5.0 is 0.31 mM, and 0.16 mM at physiological pH 7.4
(3-chlorophenyl)(2-thioxo-1H-benzo[d]imidazol-1-yl)methanone
-
-
(E)-3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)prop-2-en-1-one
-
36% inhibition
1,3-benzoxazole-2(3H)-thione
-
-
1,3-diacetyl-1H-benzo[d]imidazol-2(3H)-one
-
10% inhibition
1,3-diacetyl-benzimidazole-2-thione
IC50 at enzyme optimum pH 5.0 is 0.16 mM, and 0.005 mM at physiological pH 7.4
1,3-diacetylbenzimidazole-2-thione
-
-
1,3-dihydro-2H-benzimidazole-2-thione
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)butan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)ethanone
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)hexan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)propan-1one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)decan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexadecan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
-
-
1-(3-ethyl-1,2-dihydro-2-thioxobenzo[d]imidazole-1-yl)ethanone
-
-
1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate
-
-
1-decyl-2-(4-sulfamoyloxyphenyl)-1H-indol-6-yl sulfamate
-
inhibitor fits in the enzymatic active site via interactions resembling the binding mode of the natural hyaluronan substrate
1-ethyl-1H-benzo[d]imidazole-2(3H)-thione
-
28% inhibition
2,2'-benzene-1,4-diyldiacetic acid
IC50 at enzyme optimum pH 5.0 is 0.37 mM, and 0.90 mM at physiological pH 7.4
2,3-Butanedione
-
inactivation, arginine-specific reagent
2-phenoxy-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
2-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
3-acetylbenzo[d]oxazol-2(3H)-one
-
-
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
3-ethylbenzo[d]oxazole-2(3H)-thione
-
17% inhibition
3-hexanoylbenzo[d]oxazol-2(3H)-one
-
-
3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
3alpha-acetylpolyporenic acid A
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.040 mM
4-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)butan-1-one
-
-
arachidic acid
behenic acid
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
-
-
beta1,4-galacto-oligosaccharides
-
partially sulfated and non-sulfated forms, IC50 values
-
capric acid
Co2+
-
complete inhibition
Cu2+
-
complete inhibition
D-isoascorbic acid
Streptomyces hyalurolyticus
-
strong inhibition
D-saccharic-1,4-lactone
Streptomyces hyalurolyticus
-
strong inhibition
dehydroascorbic acid
Streptomyces hyalurolyticus
-
-
eicosadienoic acid
eicosanoic acid
eicosapentaenoic acid
eicosatetraenoic acid
eicosatrienoic acid
elaidic acid
guanidine hydrochloride
-
strong inhibition, unfolding within 1 h
guanidine isothiocyanate
-
strong inhibition
iodoacetate
L-arginine
-
strong inhibition
L-arginine methyl ester
-
strong inhibition
L-ascorbate
noncompetitive inhibition, inhibition kinetics, overview. Residues involved in the binding of L-ascorbate are confined to HylP135-308
L-ascorbic acid
L-ascorbic acid-6-hexadecanoate
lanostanoid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
lauric acid
linoleic acid
linolenic acid
methyl (9Z)-octadecenoate
methyl 2-sulfanylbenzo[d]oxazole-5-carboxylate
-
27% inhibition
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
-
-
Mg2+
-
slight inhibition by 30% unfolding of the enzyme by ion binding
myristic acid
myristoleic acid
N-(3-phenylpropionyl)-benzoxazole-2-thione
-
-
N-(3-phenylpropionyl)benzoxazole-2-thione
-
-
NaCl
-
slight inhibition, wild-type and mutant enzymes
nervonic acid
Ni2+
-
complete inhibition
oleic acid
palmitic acid
palmitoleic acid
partially sulfated neomycin
-
the non-sulfated neomycin is not inhibitory
-
partially sulfated planteose
-
the non-sulfated planteose is not inhibitory, IC50 is 0.015 mM
partially sulfated verbascose
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.030 mM and 0.001 mM
-
petroselinic acid
polyporenic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
ricinoleic acid
saccharic acid
Streptomyces hyalurolyticus
-
-
SDS
-
complete inhibition
stearic acid
sulfated 2-hydroxyphenyl monolactobioside
-
IC50 is 0.35 mM
-
sulfated hydroquinone galactoside
-
IC50 is 0.080 mM
Tetranitromethane
-
inactivation, tyrosine-specific reagent
Triton X-100
-
weak inhibition
Tween 80
-
weak inhibition
vaccenic acid
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CD44
intracellular hyaluronic acid degradation is predominantly mediated by Hyal-1 after incorporation of hyaluronic acid by CD44; without CD44 expression, Hyal-2 exists in a granular pattern, and does not show hyaluronidase activity
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 3.8
hyaluronan
0.08
hyaluronan hexasaccharide
-
recombinant wild-type enzyme, pH 6.0, 22°C
0.38 - 0.44
hyaluronate
0.285 - 0.71
hyaluronic acid
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.9
hyaluronan
-
recombinant enzyme, pH 6.0, 30°C
2.76 - 7.61
hyaluronic acid
additional information
chondroitin sulfate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035
(25S)-(+)-12alpha-hydroxy-3alpha-methylcarboxyacetate-24-methyllanosta-8,24(31)-diene-26-oic acid
Streptococcus agalactiae;
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0035 mM
0.16 - 0.31
(2E)-1-furan-2-yl-3-(4-nitrophenyl)prop-2-en-1-one
Streptococcus agalactiae;
Q53591
IC50 at enzyme optimum pH 5.0 is 0.31 mM, and 0.16 mM at physiological pH 7.4
0.07
(3-chlorophenyl)(2-thioxo-1H-benzo[d]imidazol-1-yl)methanone
Streptococcus agalactiae;
-
pH 7.4, 37°C
2.54
1,3-benzoxazole-2(3H)-thione
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.0001
1,3-diacetyl-1H-benzo[d]imidazol-2(3H)-one
Streptococcus agalactiae;
-
pH 7.4, temperature not specified in the publication
0.005 - 0.16
1,3-diacetyl-benzimidazole-2-thione
Streptococcus agalactiae;
Q53591
IC50 at enzyme optimum pH 5.0 is 0.16 mM, and 0.005 mM at physiological pH 7.4
0.005
1,3-diacetylbenzimidazole-2-thione
Streptococcus agalactiae;
-
pH 7.4, temperature not specified in the publication
1.86
1,3-dihydro-2H-benzimidazole-2-thione
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.029
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.02
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)butan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.017
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)ethanone
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.016
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)hexan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.026
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)propan-1one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.025
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)decan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.042
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.017
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexadecan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.029
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.048
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.012
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
Streptococcus agalactiae;
-
pH 7.4, temperature not specified in the publication
0.019
1-(3-ethyl-1,2-dihydro-2-thioxobenzo[d]imidazole-1-yl)ethanone
Streptococcus agalactiae;
-
pH 7.4, temperature not specified in the publication
0.011
1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate
Streptococcus agalactiae;
-
pH 5.0
0.9 - 0.37
2,2'-benzene-1,4-diyldiacetic acid
Streptococcus agalactiae;
Q53591
IC50 at enzyme optimum pH 5.0 is 0.37 mM, and 0.90 mM at physiological pH 7.4
0.062
2-phenoxy-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.069
2-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
Streptococcus agalactiae;
-
pH 7.4, 37°C
1.45
3-acetylbenzo[d]oxazol-2(3H)-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.02
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.024
3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.04
3alpha-acetylpolyporenic acid A
Streptococcus agalactiae;
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.040 mM
0.019
4-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)butan-1-one
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.556
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.7
L-ascorbate
Streptococcus pyogenes phage H4489A;
P15316
pH 6.0, 25°C, recombinant wild-type enzyme
6.1 - 34.8
L-ascorbic acid
0.0042 - 0.1
L-ascorbic acid-6-hexadecanoate
0.051
lanostanoid
Streptococcus agalactiae;
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
0.021
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
Streptococcus agalactiae;
-
pH 7.4, 37°C
0.015
N-(3-phenylpropionyl)-benzoxazole-2-thione
Streptococcus agalactiae;
-
pH 5.0
0.015 - 0.024
N-(3-phenylpropionyl)benzoxazole-2-thione
0.015
partially sulfated planteose
Streptococcus agalactiae;
-
the non-sulfated planteose is not inhibitory, IC50 is 0.015 mM
0.03
partially sulfated verbascose
Streptococcus agalactiae;
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.030 mM and 0.001 mM
-
0.0125
polyporenic acid
Streptococcus agalactiae;
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
0.35
sulfated 2-hydroxyphenyl monolactobioside
Streptococcus agalactiae;
-
IC50 is 0.35 mM
-
0.08
sulfated hydroquinone galactoside
Streptococcus agalactiae;
-
IC50 is 0.080 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
-
mutant W292A/F343V, in absence of NaCl
4.3
-
mutant W292A, in absence of NaCl
9.62
-
pH 5.5, 37°C, purified recombinant enzyme
68.9
-
mutant F343V, in absence of NaCl
231.4
-
wild-type enzyme, in absence of NaCl
3571
-
purified 92 kDa mature form
3680
-
purified 111 kDa pro-form
400000
stabilized by addition of 5 mg ovalbumin/mg hyaluronate lyase
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.4
-
assay at
6 - 7
Hyal-2
6.5
Streptomyces hyalurolyticus
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
-
high activity at pH 3.0-4.0, lower activity at pH 7.0
3 - 8
-
activity range, profile overview
4.6 - 7
-
pH 4.6: about 75% of maximal activity, pH 7.0: about 45% of maximal activity
5 - 8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 45% of maximal activity
5 - 9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 55% of maximal activity
5.5 - 7.5
pH 5.5: about 55% of maximal activity, pH 7.5: about 40% of maximal activity
6 - 6.8
-
pH 6.0: optimum, pH 6.8: 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 4.7
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is anchored via its carboxy-terminal part to the pneumococcal cell wall by a covalent linkage with peptidoglycan structures
Manually annotated by BRENDA team
-
enzyme is relaesed only when the pneumolysin causes lysis of the pneumococci
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
Streptococcus agalactiae serotype III (strain NEM316);
Q8CWU3
Streptococcus pneumoniae (strain ATCC BAA-255 / R6);
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4);
Streptococcus pyogenes serotype M1;
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39500
-
x * 39500, SDS-PAGE
41000
-
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE
44000
-
x * 44000 + x * 47000, HYAL3 in sperm, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
54260
x * 54260, sequence calculation
55000
-
x * 47000 + x * 55000, HYAL3 in sperm, SDS-PAGE
70000
-
gel filtration
70000 - 75000
-
gel filtration
80000
-
1 * 80000, SDS-PAGE
82000
x * 82000, amino acid sequence calculation
83027
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
83097
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
83102
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
83208
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
83218
-
x * 83218, calculation from nucleotide sequence
83273
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
83280
-
mass spectrometry experiments
85000
-
x * 100000, SDS-PAGE, x * 85000, SDS-PAGE, x * 75000-50000, trypsin digested enzyme, SDS-PAGE
85110
-
gel filtration
91000 - 107000
-
the recombinantly expressed enzyme exists in different proteolytically fragmented forms of the full-length enzyme with Mr of 107 kDa
100000
-
x * 100000, SDS-PAGE, x * 85000, SDS-PAGE, x * 75000-50000, trypsin digested enzyme, SDS-PAGE
107000
-
x * 107000, amino acid sequence calculation
110000
111000
-
pro-form, gel filtration
114000
x * 114000, amino acid sequence calculation
120000
recombinant enzyme, glutaraldehyde cross-linking
121000
x * 121000, amino acid sequence calculation
126000
-
x * 126000, SDS-PAGE
126500 - 130000
amino acid sequence calculation and native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
-
pH 7.0, aggregation at pH 5.0, gel filtration, SDS-PAGE after chemical cross-linking
monomer
-
1 * 80000, SDS-PAGE; x * 83218, calculation from nucleotide sequence
trimer
additional information