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 1801
-
-
Manually annotated by BRENDA team
strain 8325-4, gene hysA
-
-
Manually annotated by BRENDA team
AEMC 1801
-
-
Manually annotated by BRENDA team
strain M18
-
-
Manually annotated by BRENDA team
strain SHL-03
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
prophage encoded
SwissProt
Manually annotated by BRENDA team
strain SF370
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M1 SF370
strain SF370
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 1020
strain 1020
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 1055
strain 1055
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 350
strain 350
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 3779
strain 3779
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 422
strain 422
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 872
strain 872
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 94146
strain 94146
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 2397
strain 2397
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 4282
strain 4282
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 4283
strain 4283
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 445
strain 445
UniProt
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, 22C
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
Streptococcus pyogenes phage H4489A
-
recombinant enzyme, pH 6.0, 30C
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, 37C
2.54
1,3-benzoxazole-2(3H)-thione
Streptococcus agalactiae
-
pH 7.4, 37C
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, 37C
0.029
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.02
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)butan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.017
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)ethanone
Streptococcus agalactiae
-
pH 7.4, 37C
0.016
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)hexan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.026
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)propan-1one
Streptococcus agalactiae
-
pH 7.4, 37C
0.025
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)decan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.042
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
Streptococcus agalactiae
-
pH 7.4, 37C
0.017
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexadecan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.029
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.048
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
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, 37C
0.069
2-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
Streptococcus agalactiae
-
pH 7.4, 37C
1.45
3-acetylbenzo[d]oxazol-2(3H)-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.02
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
0.024
3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Streptococcus agalactiae
-
pH 7.4, 37C
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, 37C
0.556
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
Streptococcus agalactiae
-
pH 7.4, 37C
0.7
L-ascorbate
Streptococcus pyogenes phage H4489A
P15316
pH 6.0, 25C, 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, 37C
0.015
N-(3-phenylpropionyl)-benzoxazole-2-thione
0.024
N-(3-phenylpropionyl)benzoxazole-2-thione
Streptococcus agalactiae
-
pH 7.4, 37C
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, 37C, 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
6.5
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
ORGANISM
UNIPROT
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000 - 75000
-
gel filtration
70000
-
gel filtration
83280
-
mass spectrometry experiments
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
110000
111000
-
pro-form, gel filtration
120000
recombinant enzyme, glutaraldehyde cross-linking
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
side-chain modification