Any feedback?
No. of entries
Information on EC 3.2.1.35 - hyaluronoglucosaminidase
for references in articles please use BRENDA:EC3.2.1.35
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.35 hyaluronoglucosaminidase
IUBMB Comments
Also hydrolyses 1,4-β-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.
The enzyme appears in viruses and cellular organisms
- 3.2.1.35
- glycosaminoglycans
- proteoglycans
- hyaluronan
- cartilage
- collagen
- heparan
- hyaluronidases
- disaccharide
- oligosaccharide
- dermatan
- fibronectin
- chondrocytes
- heparitinase
-
articular
-
hyals
-
alcian
-
cspgs
-
acrosomal
- chabc
- aggrecan
- 4-sulfate
- tetrasaccharide
-
35ssulfate
-
cumulus
-
mucopolysaccharides
- haase
-
pericellular
- keratanase
- pellucida
-
6-sulphate
- hexasaccharide
-
transglycosylation
- diagnostics
- chlorate
- chondroitin-6-sulfate
-
rhamm
-
ha-binding
-
monosulfated
-
hexuronic
-
cetylpyridinium
-
d-glucuronic
- molecular biology
-
acrosome-reacted
-
iduronic
- biotechnology
-
glca
-
3hglucosamine
- pharmacology
-
perineuronal
- analysis
- neurocan
- disulfated
- octasaccharide
-
tgfbr3
- heparinum
- medicine
Reaction Schemes
showSynonyms
chondroitinase, testicular hyaluronidase, hyal1, hyal2, ph-20, hyal-1, rhuph20, spreading factor, hyal-2, mgea5, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BTH
BVH
chondritinase I
-
-
-
-
chondroitin sulfate hydrolase
chondroitinase
EC 3.2.1.34
-
-
formerly
-
HAase
Hyal
Hyal 1
Hyal-1
Hyal-2
HYAL1
HYAL1-v1
alternatively spliced and enzymatically inactive variant of HYAL1
Hyal2
HYAL3
HYAL4
hyaluronidase
hyaluronidase 1
hyaluronidase 2
hyaluronidase-1
hyaluronidase-2
hyaluronidase-4
hyaluronoglucosidase
HYase
HYL
hylB
Mu toxin
-
-
-
-
PH-20
SPAM1
Sperm surface protein PH-20
-
-
-
-
spreading factor
chondroitinase
-
-
-
-
hyaluronidase
-
-
-
-
hyaluronidase
-
-
hyaluronidase
-
-
hyaluronoglucosidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
-
-
-
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
hydrolase mechanism
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
enzyme is a beta-1,4-glucosidase, substrate binding groove, enzyme-substrate complex structure, catalytic groups and reaction mechanism
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
endoglycosidase with exoglycosidase activity
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
specifically hydrolyses 1,4-beta-D-glycosidic linkages, reaction mechanism, simulation of product formation process, active site
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
reaction mechanism and three-dimensional structure, catalytic residue is Glu149, substrate positioning residues, overview
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
reaction mechanism and three-dimensional structure, catalytic residue is Glu113, substrate positioning residues, overview
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
reaction mechanism and three-dimensional structure, catalytic residues of isozymes Hyal1-Hyal4 are Glu131, Glu135, Glu129, and Glu147, respectively, substrate positioning residues, active site structure of isozymes, overview
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
reaction mechanism and three-dimensional structure
-
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
the enzyme contains four hyaluronan binding sites [B(X)7B]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
hyaluronate 4-glycanohydrolase
Also hydrolyses 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37326-33-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chondroitin B sulfate + H2O
?
Substrates: very little hydrolase activity towards chondroitin sulfate B (dermatan sulfate)
Products: -
Products: -
?
hyaluronan + H2O
hexasaccharides + tetrasaccharides
-
Substrates: absolutely specific for
Products: main products, with N-acetyl-beta-D-glucosamine at the reducing end, cleavage of beta-1,4-glycosidic linkage, not beta-1,3-glycosidic linkage
Products: main products, with N-acetyl-beta-D-glucosamine at the reducing end, cleavage of beta-1,4-glycosidic linkage, not beta-1,3-glycosidic linkage
?
hyaluronan + H2O
N-acetylglucosamine + D-glucuronate + ?
-
Substrates: complete degradation, absolutely specific for
Products: -
Products: -
?
hyaluronan + H2O
oligosaccharides
-
Substrates: specific cleavage of beta-1,4-glucosidic linkages
Products: -
Products: -
?
hyaluronan decasaccharide + H2O
hyaluronan tetrasaccharide + hyaluronan hexasaccharide + hyaluronan octasaccharide +
-
Substrates: -
Products: 31.5% hyaluronan tetrasaccharide, 48.3% hyaluronan hexasaccharide, 14.7% hyaluronan octasaccharide, 5.5% hyaluronan decasaccharide
Products: 31.5% hyaluronan tetrasaccharide, 48.3% hyaluronan hexasaccharide, 14.7% hyaluronan octasaccharide, 5.5% hyaluronan decasaccharide
?
hyaluronan octasaccharide + H2O
hyaluronan tetrasaccharide + hyaluronan hexasaccharide
-
Substrates: -
Products: 46.8% hyaluronan tetrasaccharide, 32.7% hyaluronan hexasaccharide, 20.5% hyaluronan octasaccharide. Enzyme generates a disaccharide intermediate from hyaluronan oligosaccharide, the majority of which is transferred to the nonreducing ends of other oligosaccharides, only traces being released as free disaccharide. When hyaluronan octasaccharide, with an unsaturated glucuronic acid at the nonreducing end, is used as a substrate, only a tetrasaccharide product is detected by HPLC. MS shows that the product is a mixture of equal amounts of two tetrasaccharides, one with and the other without the unsaturated glucuronic acid. This suggests that, in the case of substrates with a double bond at the nonreducing end, a tetrasaccharide is cleaved off instead of a disaccharide
Products: 46.8% hyaluronan tetrasaccharide, 32.7% hyaluronan hexasaccharide, 20.5% hyaluronan octasaccharide. Enzyme generates a disaccharide intermediate from hyaluronan oligosaccharide, the majority of which is transferred to the nonreducing ends of other oligosaccharides, only traces being released as free disaccharide. When hyaluronan octasaccharide, with an unsaturated glucuronic acid at the nonreducing end, is used as a substrate, only a tetrasaccharide product is detected by HPLC. MS shows that the product is a mixture of equal amounts of two tetrasaccharides, one with and the other without the unsaturated glucuronic acid. This suggests that, in the case of substrates with a double bond at the nonreducing end, a tetrasaccharide is cleaved off instead of a disaccharide
?
hyaluronan oligosaccharides + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate
-
Substrates: specific cleavage of beta-1,4-glucosidic linkages
Products: -
Products: -
?
hyaluronate + H2O
(GlcUA-GlcNAc)2 + (GlcUA-GlcNAc)3
Substrates: -
Products: -
Products: -
?
hyaluronate + H2O
hyaluronic acid hexasaccharide + hyaluronic acid octasaccharide + hyaluronic acid decasaccharide
Substrates: -
Products: -
Products: -
?
hyaluronate + H2O
hyaluronic acid tetrasaccharide + hyaluronic acid hexasaccharide
Hirudo sp.
-
Substrates: LHase seems to possess strict substrate specificity toward HA
Products: -
Products: -
?
hyaluronate + H2O
oligosaccharides
-
Substrates: from human umbilical cord
Products: establishing of a rapid, sensitive PAGE method for analysis of hyaluronan oligosaccharides
Products: establishing of a rapid, sensitive PAGE method for analysis of hyaluronan oligosaccharides
?
hyaluronate octasaccharide + H2O
(GlcUA-GlcNAc)2 + (GlcUA-GlcNAc)3
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid tetrasaccharides + ?
-
Substrates: complete hydrolysis
Products: -
Products: -
?
hyaluronic acid + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid hexasaccharide + H2O
?
-
Substrates: not only lower oligosaccharides, but also higher oligosaccharides are produced, transglycosylation activity, multiple disaccharide units are rapidly transferred from one substrate molecule to another
Products: -
Products: -
r
hyaluronic acid hexasaccharide + H2O
hyaluronic acid octasaccharide + hyaluronic acid disaccharide + hyaluronic acid tetrasaccharide
-
Substrates: hydrolysis in disaccharide units, transglycosylation activity, smallest substrate
Products: -
Products: -
r
hyaluronic acid octasaccharosyl-pyridylaminoside + H2O
hexasaccharosyl-pyridylaminoside + hyaluronic acid disaccharide
-
Substrates: smallest substrate, hydrolysis of even-numbered oligosaccharides with glucuronic acid at the non-reducing terminal by successive removal of disaccharide units from the non-reducing terminal
Products: -
Products: -
?
4-S-chondroitin sulfate + H2O
?
Substrates: -
Products: -
Products: -
?
6-S-chondroitin sulfate + H2O
?
Substrates: the enzyme is capable of degrading chondroitin sulfate C at a rate of around 40% compared to its hyaluronidase activity
Products: -
Products: -
?
6-S-chondroitin sulfate + H2O
?
Substrates: -
Products: -
Products: -
?
6-S-chondroitin sulfate + H2O
?
EU152302
Substrates: the enzyme is capable of degrading CS-C at a rate of around 40% compared to its hyaluronidase activity
Products: -
Products: -
?
chondroitin + H2O
GlcAbeta(1-3)GalNAcbeta(1-4)GlcAbeta(1-3)GalNAc + ?
-
Substrates: -
Products: main product
Products: main product
ir
chondroitin + H2O
GlcAbeta(1-3)GalNAcbeta(1-4)GlcAbeta(1-3)GalNAc + ?
-
Substrates: -
Products: main product
Products: main product
ir
chondroitin 4-sulfate + H2O
?
-
Substrates: 28% activity compared to sodium hyaluronate
Products: -
Products: -
?
chondroitin 4-sulfate + H2O
?
Substrates: -
Products: -
Products: -
?
chondroitin 6-sulfate + H2O
?
-
Substrates: 19% activity compared to sodium hyaluronate
Products: -
Products: -
?
chondroitin 6-sulfate + H2O
?
Substrates: -
Products: -
Products: -
?
chondroitin sulfate A + H2O
oligosaccharides + ?
-
Substrates: acting at the same rate as with hyaluronic acid
Products: -
Products: -
?
chondroitin sulfate A + H2O
oligosaccharides + ?
-
Substrates: production of even-numbered oligosaccharides only produced by lysosomal hyaluronidase
Products: -
Products: -
?
chondroitin sulfate A + H2O
oligosaccharides + ?
-
Substrates: -
Products: -
Products: -
?
chondroitin sulfate B + H2O
?
Substrates: very little hydrolase activity
Products: -
Products: -
?
chondroitin sulfate B + H2O
?
EU152302
Substrates: very little hydrolase activity
Products: -
Products: -
?
chondroitin sulfate C + H2O
?
-
Substrates: acting at the same rate as with hyaluronic acid
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
chondroitin sulfate-rich proteoglycan + H2O
?
Vipera elegans
-
Substrates: from bovine nasal cartilage
Products: -
Products: -
?
dermatan + H2O
?
-
Substrates: 7% activity compared to sodium hyaluronate
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: from Streptococcus zooepidemicus, degradation
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: highly specific substrate with 10fold higher activity compared to chondroitin 4-sulfate, chondroitin 6-sulfate, or dermatan
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: absolute specificity for hyaluronan
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: from Streptococcus zooepidemicus
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: from Streptococcus zooepidemicus, degradation
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: from Streptococcus zooepidemicus, degradation
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + H2O
?
-
Substrates: a fluorescent substrate (FRET-HA) to quantitatively assess hyaluronidase activity is developed. Hyaluronan (HA)is dual labeled with fluorescein amine and rhodamine B amine. The fluorescein amine fluorescence signal is significantly quenched and the rhodamine B amine signal is significantly enhanced due to fluorescence resonance energy transfer (FRET). In the presence of bovine testes hyaluronidase, cleavage of HA disrupts FRET, resulting in a loss of the fluorescein amine quenching that is dependent on both enzyme concentration and time. Increase in the fluorescein amine signal can be conveniently monitored in both noncontinuous and continuous fashions
Products: -
Products: -
?
hyaluronan + H2O
?
-
Substrates: HPLC and MS analyses of the products reveal the existance of oligosaccharides which are not produced under hydrolysis conditions, but during transglycosylation by the enzyme, suggesting that a novel enzyme is present as a contaminant in commercial BTH, which acts as an N-deacetylase of N-acetylglucosamine at the reducing terminal of hyaluronan oligosaccharides
Products: -
Products: -
?
hyaluronan + H2O
?
-
Substrates: hyaluronan fragments are used with a molar mass ranging from 800 g/mol to 250000 g/mol and native hyaluronan to study the influence of the chain length of hyaluronan on the kinetics of its HAase-catalyzed hydrolysis. The initial hydrolysis rate strongly varies with hyaluronan chain length. The ability of HA chains to form an efficient enzyme-substrate complex is maximum for hyaluronan molar masses ranging from 3000 to 20000 g/mol. Shorter hyaluronan chains are too short to form a stable complex and longer hyaluronan chains encounter difficulties in forming a complex, due to steric hindrance. As the chain length decreases the HAase increasingly catalyses transglycosylation rather than hydrolysis. Two hyaluronan chain populations, corresponding to hyaluronan chain molar masses lower and higher than approximately 20000 g/mol are identified and related to the bi-exponential character
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: wild-type isozyme HYAL1 sequence, amino acid residues 301-330, is critical for hyaluronidase activity
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: complete degradation, absolutely specific for
Products: -
Products: -
?
hyaluronan + H2O
?
-
Substrates: hyaluronan deposition and turnover is even more abundant and more rapid in malignant tissues. The proportion of low molecular weight (LMW) fragments of HA is greater in tumors and tumor patients than in the normal
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: human platelets degrade the proinflammatory matrix hyaluronan through the activity of HYAL2 and platelet activation causes the immediate translocation of HYAL2 from a distinct population of alpha-granules to platelet surfaces where it exerts its catalytic activity
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: -
Products: catalyzes the endolytic hydrolysis of beta-1,4 glycosidic linkages in hyaluronan. Products are saturated hyaluronan-disaccharides
Products: catalyzes the endolytic hydrolysis of beta-1,4 glycosidic linkages in hyaluronan. Products are saturated hyaluronan-disaccharides
?
hyaluronan + H2O
?
Substrates: complete degradation, absolutely specific for
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: the enzyme is required for fertility facilitating the penetration of sperm through the cumulus mass in the ovum
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: the enzyme shows low activity, degradation
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: human skin sections
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: isozyme NNH2 shows endoglycosidase activity, absolute specific for in vitro, substrate from human skin
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
Substrates: human substrate
Products: -
Products: -
?
hyaluronan + H2O
tetraoligosaccharides + hexaoligosaccharides
-
Substrates: -
Products: -
Products: -
r
hyaluronan + H2O
tetraoligosaccharides + hexaoligosaccharides
-
Substrates: -
Products: after complete digestion
Products: after complete digestion
?
hyaluronan + H2O
tetrasaccharides units of hyaluronan
-
Substrates: absolutely specific for
Products: -
Products: -
?
hyaluronan + H2O
tetrasaccharides units of hyaluronan
-
Substrates: absolutely specific for, cleavage of beta-1,4-glycosidic linkages, of human skin, extracellular matrix
Products: -
Products: -
?
hyaluronate + H2O
?
KY098772
Substrates: best substrate
Products: -
Products: -
?
hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: from umbilical cord
Products: -
Products: -
?
hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: from umbilical cord
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
?
Substrates: the Asn-X-Ser/Thr sequence is essential for this activity
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: involved in inflammatory reactions, exists as inactive form activated by metal ions
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: important in hyaluronate catabolism in the vitreous
Products: -
Products: -
?
hyaluronic acid + H2O
?
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: two isoforms necessary for penetration of extracellular vestments surrounding eggs prior fertilization
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: endo-mucopolysaccharidase hydrolysing acid mucopolysaccharides from connective tissue and chondroitin-sulfate in cartilage
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
hyaluronic acid + H2O
?
Vipera elegans
-
Substrates: degradation in human skin, human muscle, chick embryo
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid + H2O
hyaluronic acid oligomers
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid from Streptococcus pyogenes (35 kDa) + H2O
?
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid from Streptococcus pyogenes (35 kDa) + H2O
?
-
Substrates: -
Products: -
Products: -
?
hyaluronic acid-rich cumulus matrix + H2O
?
-
Substrates: investment of oocyte during sperm invasion
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with chondroitin 4-sulfate, chondroitin 6-sulfate, dermatan sulfate, chondroitin sulfates D and E, and heparin, no activity with 4-nitrophenyl-beta-glucuronide or 4-nitrophenyl-N-acetyl-beta-glucoaminide
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is a major allergen of bee venom which can induce serious, occasionally fatal, systemic IgE-mediated anaphylactic reactions in humans
Products: -
Products: -
?
additional information
?
-
KY098772
Substrates: no activity with chitosan, chitin, xantham gum, pectin, alginate, and heparan sulfate
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme activity determination by the Elson-Morgan like method
Products: -
Products: -
-
additional information
?
-
-
Substrates: hyaluronan is degraded by L-ascorbic acid, D-isoascorbic acid, and dehydroascorbic acid themselves, only slightly by L-gulonic-gamma-lactone, D-saccharic-1,4-lactone, and alpha-D-glucoheptonic-gamma-lactone
Products: -
Products: -
?
additional information
?
-
-
Substrates: simulation of progress of product distribution from short oligosaccharides with the Monte Carlo method using the probalistic model
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme additionally catalyzes transglycosylation reactions of chondroitin sulfates. Barium salt of chondroitin sulfates enhances transglycosylation, the zinc salt of chondroitin sulfates inhibits transglycosylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: minimum substrate for bovine testicular hyaluronidase is the hyaluronan hexasaccharide
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme activity determination by the Turbidimetric method. Using HA octasaccharide as substrate: BTH recognizes and cleaves the first N-acetylglucosaminide bond in (GlcUA-GlcNAc)4, releasing hexasaccharide as product, while retaining the disaccharide unit in active unit
Products: -
Products: -
-
additional information
?
-
Substrates: activity detection via the turbidimetric method
Products: -
Products: -
-
additional information
?
-
Substrates: activity detection via the turbidimetric method
Products: -
Products: -
-
additional information
?
-
-
Substrates: chondroitin, chondroitin sulfate A, chondroitin sulfate B, chondroitin sulfate C, chondroitin sulfate D, heparin, and chitosan are no substrates
Products: -
Products: -
?
additional information
?
-
Hirudo sp.
-
Substrates: detection of activity via the DNS method
Products: -
Products: -
-
additional information
?
-
-
Substrates: the splice variant is enzymatically inactive
Products: -
Products: -
?
additional information
?
-
Substrates: the splice variant is enzymatically inactive
Products: -
Products: -
?
additional information
?
-
Substrates: the splice variant is enzymatically inactive
Products: -
Products: -
?
additional information
?
-
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: HPH-20 or SPAM1, sperm adhesion molecule 1, is a bifunctional enzyme, which is also an adhesion molecule with binding properties to the cumulus mass surrounding the ovum
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
Substrates: among hyaluronidases Hyal-1 to Hyal-4, only rHuHyal-4 exhibits chondroitinase activity with both 6-S-chondroitin sulfate and 4-S-chondroitin sulfate as standard substrates
Products: -
Products: -
?
additional information
?
-
Substrates: among hyaluronidases Hyal-1 to Hyal-4, only rHuHyal-4 exhibits chondroitinase activity with both 6-S-chondroitin sulfate and 4-S-chondroitin sulfate as standard substrates
Products: -
Products: -
?
additional information
?
-
Substrates: among hyaluronidases Hyal-1 to Hyal-4, only rHuHyal-4 exhibits chondroitinase activity with both 6-S-chondroitin sulfate and 4-S-chondroitin sulfate as standard substrates
Products: -
Products: -
?
additional information
?
-
Substrates: among hyaluronidases Hyal-1 to Hyal-4, only rHuHyal-4 exhibits chondroitinase activity with both 6-S-chondroitin sulfate and 4-S-chondroitin sulfate as standard substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: among hyaluronidases Hyal-1 to Hyal-4, only rHuHyal-4 exhibits chondroitinase activity with both 6-S-chondroitin sulfate and 4-S-chondroitin sulfate as standard substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme strongly prefers D-glucuronic acid-(2-O-sulfate)-GalNAc(6-O-sulfate)-containing sequences typical in chondroitin sulfate D
Products: -
Products: -
?
additional information
?
-
-
Substrates: the jaagsiekte sheep retrovirus receptor Hyal2 interacts specifically with the virus particles of the amphotropic murine leukemia virus-pseudotype vectors/JSRV-pseudotype vector envelope protein, binding kinetics, the binding inhibits virus entry into cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity detection via the turbidimetric method
Products: -
Products: -
-
additional information
?
-
-
Substrates: does not hydrolyze chondroitin sulfate B, heparin, or heparan sulfate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with dermatan sulfate and heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with dermatan sulfate and heparan sulfate
Products: -
Products: -
?
additional information
?
-
-
Substrates: CD44-mediated specific role of certain populations of testicular enzyme in the induction of angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity in serum from tumour-bearing mice, e.g. H460M or SA87 cell grafted mice, is increased, the level is corrsponding to the tumour mass, not in serum from CB193 cell grafted mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme depolymerizes various chondroitin sulfate isoforms to a similar extent, suggesting broad substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme NNH2 is nontoxic, but indirectly potentiates the hemorrhagic activity of hemorrhagic complex-I
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme indirectly potentiates the myotoxicity of VRV-PL-VIII, a phospholipolytic myotoxin, and also the hemorrhagic potency of a hemorrhagic complex-I
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with chondroitin sulfates, heparin, and different chitosans
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with chondroitin sulfates, heparin, chitosan, 4-nitrophenyl-N-acetyl-beta-D-glucosaminide, or 4-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: chondroitin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: chondroitin
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant enzyme rTsHyal-1 presents the highest substrate specificity to hyaluronan followed by chondroitin-6-sulfate, chondroitin-4-sulfate, and dermatan sulfate
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hyaluronan + H2O
tetrasaccharides units of hyaluronan
-
Substrates: absolutely specific for
Products: -
Products: -
?
hyaluronate + H2O
(GlcUA-GlcNAc)2 + (GlcUA-GlcNAc)3
Substrates: -
Products: -
Products: -
?
hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronic acid-rich cumulus matrix + H2O
?
-
Substrates: investment of oocyte during sperm invasion
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: highly specific substrate with 10fold higher activity compared to chondroitin 4-sulfate, chondroitin 6-sulfate, or dermatan
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
-
Substrates: -
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: complete degradation, absolutely specific for
Products: -
Products: -
?
hyaluronan + H2O
?
Substrates: human platelets degrade the proinflammatory matrix hyaluronan through the activity of HYAL2 and platelet activation causes the immediate translocation of HYAL2 from a distinct population of alpha-granules to platelet surfaces where it exerts its catalytic activity
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: the enzyme is required for fertility facilitating the penetration of sperm through the cumulus mass in the ovum
Products: -
Products: -
?
hyaluronan + H2O
hyaluronan oligomers
-
Substrates: human skin sections
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: involved in inflammatory reactions, exists as inactive form activated by metal ions
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: important in hyaluronate catabolism in the vitreous
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: two isoforms necessary for penetration of extracellular vestments surrounding eggs prior fertilization
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: endo-mucopolysaccharidase hydrolysing acid mucopolysaccharides from connective tissue and chondroitin-sulfate in cartilage
Products: -
Products: -
?
hyaluronic acid + H2O
?
-
Substrates: spreading factor for dermonecrosis
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is a major allergen of bee venom which can induce serious, occasionally fatal, systemic IgE-mediated anaphylactic reactions in humans
Products: -
Products: -
?
additional information
?
-
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
Substrates: alternative splicing controls the cellular expression of enzymatically active hyaluronidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
Substrates: increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
Products: -
Products: -
?
additional information
?
-
-
Substrates: HPH-20 or SPAM1, sperm adhesion molecule 1, is a bifunctional enzyme, which is also an adhesion molecule with binding properties to the cumulus mass surrounding the ovum
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 suppresses tumour growth in vivo but not in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 1 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 2 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
-
Substrates: Hyal 3 is expressed in airway epithelium and may operate in a coordinated fashion to depolymerize hyaluronan during inflammation associated with up-regulation of TNF-alpha and IL-1beta, such as allergen-induced asmatic responses
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: this gene may play an important role in the development of lung and renal malignancies, the expression of hyaluronidase-1 or hyaluronidase-2 suppresses tumour growth in vivo but not in vitro, HYAL2 inhibits experimental lung metastases in nu/nu mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: CD44-mediated specific role of certain populations of testicular enzyme in the induction of angiogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity in serum from tumour-bearing mice, e.g. H460M or SA87 cell grafted mice, is increased, the level is corrsponding to the tumour mass, not in serum from CB193 cell grafted mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme NNH2 is nontoxic, but indirectly potentiates the hemorrhagic activity of hemorrhagic complex-I
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
Mg2+
Na+
NaCl
additional information
NaCl
KY098772
the purified enzyme is halotolerant and stable at 2 M NaCl
additional information
KY098772
the enzyme activity remains unaffected by 10 mM of PMSF, DTT and reduced glutathione
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
-
-
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
-
-
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]oxy]butanedioic acid
-
-
(2R,3S)-2-hydroxy-2-(4-hydroxybenzyl)-3-[[(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
-
-
(2R,3S)-2-hydroxy-2-(4-hydroxybenzyl)-3-[[(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
-
-
(2R,3S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-2-hydroxy-2-(4-hydroxybenzyl)butanedioic acid
-
-
(2R,3S)-3-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]-2-hydroxy-2-(4-hydroxybenzyl)butanedioic acid
-
-
(2S)-2-(3,4-dimethoxy-5-oxo-2,5-dihydrofuran-2-yl)-2-hydroxyethyl hexadecaneperoxoate
-
inactive at concentrations less than 0.2 mM, at pH 5.0
(2S)-2-[3,4-bis(benzyloxy)-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl hexadecaneperoxoate
-
inactive at concentrations less than 0.2 mM, at pH 5.0
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-21-cyclohexyl-28-hydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-23,28-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-22-[[(2Z)-2-methylbut-2-enoyl]oxy]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-22-[(2-methylbutanoyl)oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic aci
-
-
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosidur
-
-
(3beta,16alpha,21beta,22alpha)-16,28-bis(acetyloxy)-22-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,28-bis(acetyloxy)-22-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic a
-
-
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-22-[[(2E)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosi
-
-
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosi
-
-
(3beta,16alpha,21beta,22alpha)-22-(acetyloxy)-16,28-dihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-22-(acetyloxy)-16,28-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-28-(acetyloxy)-16,22-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,21beta,22alpha)-28-(acetyloxy)-21-cyclohexyl-16,22-dihydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,22alpha)-22-(cyclohexyloxy)-16,23,28-trihydroxyolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(3beta,16alpha,22alpha)-22-(cyclohexyloxy)-16,28-dihydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
-
-
(5R)-3,4-bis(benzyloxy)-5-(1,2-dihydroxyethyl)furan-2(5H)-one
-
inactive at concentrations less than 13 mM, at pH 5.0
(5R)-5-(1,2-dihydroxyethyl)-3,4-dimethoxyfuran-2(5H)-one
-
inactive at concentrations less than 13 mM, at pH 5.0
(7S)-7-(1,2-dihydroxyethyl)-2,3-dihydrofuro[3,4-b][1,4]dioxin-5(7H)-one
-
inactive at concentrations less than 13 mM, at pH 5.0
2-hydroxy-2-[(5R)-7-oxo-2,3,5,7-tetrahydrofuro[3,4-b][1,4]dioxin-5-yl]ethyl hexadecaneperoxoate
-
inactive at concentrations less than 0.2 mM, at pH 5.0
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl ([1-[2-(benzyloxy)ethenylidene]but-2-yn-1-yl]oxy)ethaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 11-phenoxyundecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 11-[[1-(2-phenylethenylidene)but-2-yn-1-yl]oxy]undecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 2,2-dimethylpropaneperoxoate
-
inactive at concentrations less than 1.1 mM, at pH 5.0
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 3-(2-phenylethenylidene)hex-4-yneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 6-(benzyloxy)hexaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 6-phenoxyhexaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl benzenecarboperoxoate
-
33% inhibition at 1.43 mM
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl decaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl dodecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl hexadecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl hexaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl octadecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl octaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl tetradecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl tridecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl undecaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl [(1-prop-1-yn-1-ylpenta-1,2-dien-1-yl)oxy]ethaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl [[1-(2-phenylethenylidene)but-2-yn-1-yl]oxy]ethaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl [[2-(2-phenylethenylidene)pent-3-yn-1-yl]oxy]ethaneperoxoate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl {[1-(2-phenylethenylidene)but-2-yn-1-yl]oxy}ethaneperoxoate
-
-
3-(4-methylpiperazin-1-yl)-5-phenyl-1H-indole
-
0.05 mM, 23% inhibition in stains-all assay, pH 7.0
3-amino-6-chloro-N-(diaminomethylidene)-5-[ethyl(propan-2-yl)amino]pyrazine-2-carboxamide
-
fully O-sulfonated chondroitin sulfate
-
competitive and noncompetitive mode, 50% inhibition at 0.00135 mg/ml
-
fully O-sulfonated dermatan sulfate
-
competitive and noncompetitive mode, 50% inhibition at 0.00133 mg/ml
fully O-sulfonated heparan sulfate
-
competitive and noncompetitive mode, 50% inhibition at 0.00128 mg/ml
-
heparin O-sulfate
-
IC50 = 0.00114 mg/ml, competitive and non-competitive inhibitory effects
-
N-(4,6-dimethylpyridin-2-yl)-(1-ethylindole-3-yl)acetamide
-
inhibition at pH 7: 3%, but at pH 3.5: 134% activation
N-(4,6-dimethylpyridin-2-yl)-[5-bromo-1-(4-methyl)indole-3-yl]carboxamide
-
inhibition at pH 7: 37%, but at pH 3.5: 117% activation
N-(pyridin-4yl)-[5-bromo-1-(4-fluorobenzyl)indole-3-yl]carboxamide
-
inhibition at pH 7: 50%, but at pH 3.5: 120% activation
sorghum bran
-
the ability of ethanolic extracts of bran from six cultivated varieties of Sorghum bicolor to inhibit hyaluronidase activity in vitro is assessed. Each extract inhibits hyaluronidase activity with this order of potency: Sumac higher than Shanqui Red higher than Black higher than Mycogen higher than Fontanelle higher than White sorghum. Hyaluronidase inhibition correlate positively with total phenolic content and ferric reducing antioxidant power values for each bran extract. Inhibition is not only due to condensed tannins (proanthocyanidins) because the Black sorghum cultivar lacks condensed tannins but has abundant anthocyanins and other polyphenols
-
type I collagen
-
purified 2alpha1[I]alpha2[I] collagen and collagen peptides (about 30 kDa) derived from the skin of marlin (Istiophoridae) show inhibition of hyaluronidase activity
-
type V collagen
-
purified alpha1[V]alpha3[V]alpha2[V] collagen and collagen peptides (about 30 kDa) derived from the skin of marlin (Istiophoridae) show inhibition of hyaluronidase activity
-
beta1,4-galacto-oligosaccharides
-
partially sulfated and non-sulfated forms, especially tri-, tetra-, and pentasaccharides
-
beta1,4-galacto-oligosaccharides
-
partially sulfated and non-sulfated forms, especially tri-, tetra-, and pentasaccharides, IC50 values
-
heparin
-
inhibitory potency can be regulated by chemical modification, in form of conformational changes, with aldehyde dextran, increase in modification degree decreases the inhibition, best at 70-90% modification, overview
N-(4-chlorobenzyl)-1-(4-fluorobenzyl)-1H-indole-3-carboxamide
-
0.05 mM, 66% inhibition at pH 7.0
N-(4-chlorobenzyl)-1-(4-fluorobenzyl)-1H-indole-3-carboxamide
-
0.05 mM, 21% inhibition at pH 7.0
N-(4-fluorobenzyl)-1-benzyl-1H-indole-2-carboxamide
-
0.05 mM, 80% inhibition at pH 7.0
N-(4-fluorobenzyl)-1-benzyl-1H-indole-2-carboxamide
-
0.05 mM, 61% inhibition at pH 7.0
partially sulfated planteose
-
the non-sulfated planteose is not inhibitory, IC50 is 0.008 mM
partially sulfated planteose
-
the non-sulfated planteose is not inhibitory, IC50 is 0.005 mM
partially sulfated verbascose
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.040 mM and 0.003 mM
-
partially sulfated verbascose
-
2 forms, the non-sulfated verbascose is not inhibitory
-
serum protein
-
inhibition strongly influenced by salts, that in- or decrease the effect
-
Urea
KY098772
34% inhibition at 1 mM, 79% at 5 mM, and complete inhibition at 10 mM
additional information
KY098772
the enzyme activity remains unaffected by 10 mM of PMSF, DTT and reduced glutathione
-
additional information
-
not affected by ascorbic acid, phenylmethylsulfonyl fluoride, dithiothreitol, glutathione (reduced), or L-cysteine
-
additional information
-
enzyme stably covalently linked to activated glycosaminoglycans, such as heparin, dextran and dermatan sulfate, is reduced in its activity and the inhibitory effect of free heparin is increased, while chondroitin sulfate stabilizes the enzyme against heparin inhibition, effect of glycosaminoglycan fragments with different residues, at different pH values, overview
-
additional information
-
iridoids from leaves and stem of malaysian medical plants Rothmannia macrophylla and Saprosma scortechinii are poor inhibitors, e.g. sapromoside A, D, E, G, asperulosidic acid, paederosidic acid, 6-epi-paederosidic acid, methylpaederosidate, 6alpha-hydroxygeniposide, asperuloside, paederoside, macrophylloside, and gardenogenin A and B, overview
-
additional information
-
no inhibition by saccharic acid, poor inhibitors are alpha-D-glucoheptonic-gamma-lactone, D-saccharic-1,4-lactone, L-gulonic-gamma-lactone, D-ribonic-gamma-lactone, and D-gluconic-gamma-lactone
-
additional information
-
not inhibited by gallic acid, methyl gallate, ethyl gallate, propyl gallate, butyl galate, dodecyl gallate, octyl 3-hydroxybenzoate, and octyl 4-hydroxybenzoate
-
additional information
-
at pH 4 bovine serum albumin (BSA) is able to compete with HAase to form electrostatic complexes with hyaluronan, liberating HAase which recovers its catalytic activity, the BSA concentration necessary to prevent the HAase binding is 25times higher at pH 5.25 than at pH 4.0
-
additional information
-
inhibition data for human and bovine enzyme differ, bovine enzyme is not applicable as an alternative to human PH-20
-
additional information
-
aminomethyl indole derivatives with phenyl substitution at position 5 have higher activity. More lipophilic compounds have better inhibition against the hyaluronidase enzyme
-
additional information
the effect of modified di- and trisaccharides on hyaluronidase activity is assessed by capillary electrophoresis-based enzymatic assay. Hyaluronidase is mostly inhibited in a concentration-dependent fashion by a deoxy modification and activated by a methoxy modification. Trisaccharides are more effective on hyaluronidase activity than disaccharides. Position 4 is more favorable for hyaluronidase activity than position 6 and the activity in position 2 is negligible
-
additional information
-
the ethanol extract of of the stem bark of Butea monosperma dose-dependently inhibits enzyme with IC50 of 0.1254 mg/ml
-
additional information
-
the residual activities normalized to 100% at 0 concentrations of Terminalia chebula extract are reduced to 84% at 0.1 mg/ml, 68% at 0.5 mg/ml, 57% at 1 mg/ml, 26% at 1.5 mg/ml, 20% at 3 mg/ml, and 7% at 30 mg/ml
-
additional information
-
blocking of CD44-receptors inhibits the enzyme-induced tubular structure formation of endothelial cells
-
additional information
-
the ethanol extract of of the stem bark of Butea monosperma dose-dependently inhibits enzyme with IC50 of 0.0494 mg/ml
-
additional information
-
ascorbic acid is a poor inhibitor, the plant-derived inhibitors inhibit isozyme NNH1, reduce the local tissue damage, and retard the easy diffusion of systemic toxins and increase survival time, inhibitory potencies, overview
-
additional information
-
the ethanol extract of of the stem bark of Butea monosperma dose-dependently inhibits enzyme with IC50 of 0.012 mg/ml
-
additional information
-
the residual activities normalized to 100% at 0 concentrations of Terminalia chebula extract are reduced to 88% at 0.1 mg/ml, 78% at 0.5 mg/ml, 58 at 1 mg/ml, 49% at 1.5 mg/ml, 29% at 3 mg/ml, and 15% at 30 mg/ml
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
interleukin 1-beta
acts synergistically with TNF-alpha to increase gene expression and activity
-
lysozyme
-
lysozyme can enhance HAase activity over a wide pH range from 3 to 9. Lysozyme can compete with HAase to form complexes with yaluronan, HAase is catalytically active over this whole pH domain when LYS limits its complexation with HA, and either the pI of bovine testicular HAase is high or positive patches on the surface of HAase allow the formation of electrostatic HA-HAase complexes at high pH values
-
N-(4,6-dimethylpyridin-2-yl)-(1-ethylindole-3-yl)acetamide
-
acts as an inhibitor at pH 7 and at pH 3.5 activity is increased to 134%
N-(4,6-dimethylpyridin-2-yl)-[5-bromo-1-(4-methyl)indole-3-yl]carboxamide
-
acts as an inhibitor at pH 7 and at pH 3.5 activity is increased to 117%
N-(pyridin-4yl)-[5-bromo-1-(4-fluorobenzyl)indole-3-yl]carboxamide
-
acts as an inhibitor at pH 7 and at pH 3.5 activity is increased to 120%
TNF-alpha
acts synergistically with interleukin 1-beta to increase gene expression and activity
-
bovine serum albumin
-
at pH 3.0 to 5.3, at low bovine serum albumin concentrations, HAase activity increases as bovine serum albumin concentration increases, and at high bovine serum albumin concentrations, HAase activity decreases as bovine serum albumin concentration increases
-
NaCl
0.1-0.4 M NaCl increases the enzyme's activity by 20-30%
additional information
the effect of modified di- and trisaccharides on hyaluronidase activity is assessed by capillary electrophoresis-based enzymatic assay. Hyaluronidase is mostly inhibited in a concentration-dependent fashion by a deoxy modification and activated by a methoxy modification. Trisaccharides are more effective on hyaluronidase activity than disaccharides. Position 4 is more favorable for hyaluronidase activity than position 6 and the activity in position 2 is negligible
-
additional information
addition of MgCl2, CaCl2, and EDTA shows no significant effect
-
additional information
-
addition of MgCl2, CaCl2, and EDTA shows no significant effect
-
additional information
activity is optimal at physiological salt concentrations
-
additional information
-
activity is optimal at physiological salt concentrations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.48
chondroitin sulfate
-
apparent KM, substrate calculated as disaccharide
49.3
hyaluronic acid from Streptococcus pyogenes (35 kDa)
-
apparent KM, substrate calculated as disaccharide
-
additional information
hyaluronan
kinetic measurement on hyaluronan substrates with sizes ranging from 90 to 752 kDa. Km-values: 0.87-0.91 mg/ml. A simple and sensitive method is developed for kinetic measurement of recombinant human hyaluronidase PH20 (rHuPH20) on hyaluronan substrates with sizes ranging from 90 to 752 kDa. The method is based on 2-aminobenzamide labeling of hydrolyzed hyaluronan products combined with separation by size exclusion-ultra performance liquid chromatography coupled with fluorescence detection
additional information
hyaluronan
-
kinetic measurement on hyaluronan substrates with sizes ranging from 90 to 752 kDa. Km-values: 0.87-0.91 mg/ml. A simple and sensitive method is developed for kinetic measurement of recombinant human hyaluronidase PH20 (rHuPH20) on hyaluronan substrates with sizes ranging from 90 to 752 kDa. The method is based on 2-aminobenzamide labeling of hydrolyzed hyaluronan products combined with separation by size exclusion-ultra performance liquid chromatography coupled with fluorescence detection
additional information
hyaluronic acid
-
Km: 0.00848 mg/ml, at 37°C, pH 8.0
additional information
additional information
-
Km (hyaluronan) (microgram/ml): 4.91, Vmax (hyaluronan): 2.02 U/min
-
additional information
additional information
-
Km strongly decreases with increasing HA chain sizes
-
additional information
additional information
KY098772
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
hyaluronan
kinetic measurement on hyaluronan substrates with sizes ranging from 90 to 752 kDa. kcat: 40.5-42.4/s. A simple and sensitive method is developed for kinetic measurement of recombinant human hyaluronidase PH20 (rHuPH20) on hyaluronan substrates with sizes ranging from 90 to 752 kDa. The method is based on 2-aminobenzamide labeling of hydrolyzed hyaluronan products combined with separation by size exclusion-ultra performance liquid chromatography coupled with fluorescence detection
additional information
hyaluronan
-
kinetic measurement on hyaluronan substrates with sizes ranging from 90 to 752 kDa. kcat: 40.5-42.4/s. A simple and sensitive method is developed for kinetic measurement of recombinant human hyaluronidase PH20 (rHuPH20) on hyaluronan substrates with sizes ranging from 90 to 752 kDa. The method is based on 2-aminobenzamide labeling of hydrolyzed hyaluronan products combined with separation by size exclusion-ultra performance liquid chromatography coupled with fluorescence detection
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.082
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.112
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.251
(2R,3S)-2-(3,4-dihydroxybenzyl)-2-hydroxy-3-[[(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]oxy]butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.092
(2R,3S)-2-hydroxy-2-(4-hydroxybenzyl)-3-[[(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.12
(2R,3S)-2-hydroxy-2-(4-hydroxybenzyl)-3-[[(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy]butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.153
(2R,3S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-2-hydroxy-2-(4-hydroxybenzyl)butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.138
(2R,3S)-3-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]oxy]-2-hydroxy-2-(4-hydroxybenzyl)butanedioic acid
Bos taurus
-
in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.0285
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-21-cyclohexyl-28-hydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0264
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-23,28-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0193
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0364
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0556
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.052
(3beta,16alpha,21beta,22alpha)-16,22-bis(acetyloxy)-28-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0302
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-22-[[(2Z)-2-methylbut-2-enoyl]oxy]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0242
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-22-[(2-methylbutanoyl)oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic aci
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.02
(3beta,16alpha,21beta,22alpha)-16,23,28-trihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosidur
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0552
(3beta,16alpha,21beta,22alpha)-16,28-bis(acetyloxy)-22-hydroxy-21-[(2Z)-2-methylbut-2-enoyl]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0515
(3beta,16alpha,21beta,22alpha)-16,28-bis(acetyloxy)-22-hydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0449
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic a
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0405
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-22-[[(2E)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosi
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0368
(3beta,16alpha,21beta,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosi
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0297
(3beta,16alpha,21beta,22alpha)-22-(acetyloxy)-16,28-dihydroxy-21-[(2Z)-2-methylbut-2-enoyl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0387
(3beta,16alpha,21beta,22alpha)-22-(acetyloxy)-16,28-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0549
(3beta,16alpha,21beta,22alpha)-28-(acetyloxy)-16,22-dihydroxy-21-[(3Z)-3-methyl-2-oxopent-3-en-1-yl]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0487
(3beta,16alpha,21beta,22alpha)-28-(acetyloxy)-21-cyclohexyl-16,22-dihydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0241
(3beta,16alpha,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-glucopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0249
(3beta,16alpha,22alpha)-16,28-dihydroxy-22-[[(2Z)-2-methylbut-2-enoyl]oxy]olean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0266
(3beta,16alpha,22alpha)-22-(cyclohexyloxy)-16,23,28-trihydroxyolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.0288
(3beta,16alpha,22alpha)-22-(cyclohexyloxy)-16,28-dihydroxy-23-oxoolean-12-en-3-yl beta-D-glucopyranosyl-(1->2)-[beta-D-xylopyranosyl-(1->2)-alpha-L-arabinopyranosyl-(1->3)]-beta-D-glucopyranosiduronic acid
Bos taurus
-
in 0.1 M acetate buffer (pH 4.0), at 37°C
0.21
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl ([1-[2-(benzyloxy)ethenylidene]but-2-yn-1-yl]oxy)ethaneperoxoate
Bos taurus
-
at pH 5.0
0.105
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 11-phenoxyundecaneperoxoate
Bos taurus
-
at pH 5.0
0.037
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 11-[[1-(2-phenylethenylidene)but-2-yn-1-yl]oxy]undecaneperoxoate
Bos taurus
-
at pH 5.0
2.006
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl 3-(2-phenylethenylidene)hex-4-yneperoxoate
Bos taurus
-
at pH 5.0
1.38
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl decaneperoxoate
Bos taurus
-
at pH 5.0
0.208
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl dodecaneperoxoate
Bos taurus
-
at pH 5.0
0.057
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl hexadecaneperoxoate
Bos taurus
-
at pH 5.0
0.039
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl octadecaneperoxoate
Bos taurus
-
at pH 5.0
0.071
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl tetradecaneperoxoate
Bos taurus
-
at pH 5.0
0.096
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl tridecaneperoxoate
Bos taurus
-
at pH 5.0
0.58
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl undecaneperoxoate
Bos taurus
-
at pH 5.0
0.188
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl [[1-(2-phenylethenylidene)but-2-yn-1-yl]oxy]ethaneperoxoate
Bos taurus
-
at pH 5.0
0.543
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl [[2-(2-phenylethenylidene)pent-3-yn-1-yl]oxy]ethaneperoxoate
Bos taurus
-
at pH 5.0
0.22
lansiumamide B
Deinagkistrodon acutus
-
pH and temperature not specified in the publication
0.56
myricetin 3-O-beta-D-glucopyranoside
Naja atra
-
pH and temperature not specified in the publication
0.078
N-(4,6-dimethylpyridin-2-yl)-[5-bromo-1-(4-methyl)indole-3-yl]carboxamide
Bos taurus
-
pH: 7.0
0.046
N-(pyridin-4yl)-[5-bromo-1-(4-fluorobenzyl)indole-3-yl]carboxamide
Bos taurus
-
pH: 7.0
4
N-acetyl-L-cysteine
Bos taurus
-
in 0.2 M sodium acetate buffer pH 5.5 containing 0.15 M NaCl at 37°C
0.902
octyl 3,4-dihydroxybenzoate
Bos taurus
-
in 0.1 M sodium acetate buffer, pH 4.0, at 37°C
0.113
octyl 3,5-dihydroxybenzoate
Bos taurus
-
in 0.1 M sodium acetate buffer, pH 4.0, at 37°C
0.04
partially sulfated verbascose
Apis mellifera
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.040 mM and 0.003 mM
-
0.658
shomaside D
Bos taurus
-
IC50 above 0.658 mM, in 0.1 mM acetate buffer (pH 3.5), at 37°C
0.18
aristolochic acid
Deinagkistrodon acutus
-
pH and temperature not specified in the publication
0.005
partially sulfated planteose
Bos taurus
-
the non-sulfated planteose is not inhibitory, IC50 is 0.005 mM
0.008
partially sulfated planteose
Apis mellifera
-
the non-sulfated planteose is not inhibitory, IC50 is 0.008 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000245
recombinant enzyme from crude extract, in 100 mM sodium phosphate, pH 5.0, at 37°C
0.000239
recombiannt enzyme after 9.6fold purification, in 100 mM sodium phosphate, pH 5.0, at 37°C
0.49
1.72
fresh nerve tissue, hyaluronidase activity, pH not specified in the publication, 37°C
4.64
transection tissue, hyaluronidase activity, pH not specified in the publication, 37°C
4.77
437.5
purified enzyme, pH and temperature not specified in the publication
additional information
additional information
KY098772
highest activity of 289 U/ml at pH 7.0, 37°C, and optimized consitions in cell culture of Brevibacterium halotolerans strain DC1
additional information
-
development of a highly sensitive fluorometric assay method using a chromogenic reaction with the N-acetylglucosamine residues at the reducing ends produced by the enzymic cleavage, mechanism, overview
additional information
the partially purified tagged recombinant enzyme shows 1-6 U/ml activity
additional information
-
activity measured as turbidicity reducing units
additional information
-
enzyme shows low enzymatic activity. Hyaluronan is the preferred substrate
additional information
-
activity in serum samples, development of a highly sensitive fluorometric assay method using a chromogenic reaction with the N-acetylglucosamine residues at the reducing ends produced by the enzymic cleavage, mechanism, overview
additional information
-
development of a flow injection assay method using commercial bovine enzyme and fluorometric detection, comparison of fluorogenic reagents, enzyme activity in human urine samples
additional information
the purified recombinant enzyme shows 150 mU/ml activity
additional information
the purified recombinant enzyme shows 150 mU/ml activity
additional information
the purified recombinant enzyme PH-20 shows 2-258 mU/ml activity
additional information
the purified recombinant enzyme PH-20 shows 2-258 mU/ml activity
additional information
-
activity in serum samples, development of a highly sensitive fluorometric assay method using a chromogenic reaction with the N-acetylglucosamine residues at the reducing ends produced by the enzymic cleavage, mechanism, overview
additional information
comparative analysis of the hyaluronidase activities of H3S1, H3S2, deglycosylated H3S1, and deglycosylated H3S2 using the turbidimetric method, overview
additional information
comparative analysis of the hyaluronidase activities of H3S1, H3S2, deglycosylated H3S1, and deglycosylated H3S2 using the turbidimetric method, overview
additional information
the recombinant enzyme shows 233.5 U/ml activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.6
3.8
3.9
4.2
4.5
5 - 6
5.4
5.5
6 - 7
6.5
5.4
-
broad optimum below, pH-activity curve depends on hyaluronate-enzyme and enzyme-inhibitor interactions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 9
-
the optimum activity at pH 3.8 decreases by half at pH 2.5 and 6.0 and is virtually abolished at pH 9.0
3 - 8
4 - 7
6 - 8
additional information
3 - 8
native and the recombinant enzyme are active at extreme conditions
3 - 8
EU152302
native and the recombinant enzyme are active at extreme conditions
4 - 7
pH 4.0: about 90% of maximal activity, pH 7.0: about 75% of maximal activity
4 - 7
about 40% activity at pH 4.0, more than 90% activity at pH 5.0-6.0, about 50% activity at pH 6.5, about 10% activity at pH 7.0
additional information
narrow activity range in the slightly acidic and neutral pH, inactive below pH 5.4
additional information
-
narrow activity range in the slightly acidic and neutral pH, inactive below pH 5.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
45
50
62
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20°C: about 40% of maximal activity, 50°C: about 40% of maximal activity
20 - 55
-
more than 50% activity between 20 and 55°C. Activity is abolished at 60°C
4 - 90
4 - 90
34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum
4 - 90
EU152302
34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
WormBase accession T22C8.2, cDNA: WBGene 00011923 (WormBase)
-
-
brenda
from northernmost state of Brazil, named Roraima, and southern region of Guyana, collected in the region of Boa Vista
-
-
brenda
using the information of preferred Pichia pastoris codons as provided by Genscript, Inc., the native sequence is de novo synthesized to create a fully codon-optimized cDNA (Hya delta c) and the synthetic gene is expressed in Pichia
EU152302
Genbank
brenda
expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein
UniProt
brenda
-
664596, 666687, 677943, 678640, 679226, 680397, 681742, 681743, 695542, 698133, 699233, 699474, 699963, 700874, 701690, 702753, 703188, 703288, 705245, 705485, 714053, 714911, 714954, 716094, 717012, 729118, 729585, 729842, 730951, 730998
-
-
brenda
WormBase accession T22C8.2, cDNA: WBGene 00011923 (WormBase)
-
-
brenda
expression in human bronchial epithelial cell (HBE)
SwissProt
brenda
gene mgea5, bifunctional enzyme possessing hyaluronidase and beta-N-acetylglucoaminidase activities
SwissProt
brenda
2 isoforms, intraspecific variability in isoforms with different geographical distribution in the indian subcontinent
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Hyal-like activity is present in the apical and basolateral secretions from HBE cells where Hyals 1, 2, and 3 are expressed
brenda
increased expression and activity is observed in tracheal sections and in bronchoalveolar lavage (BAL) obtained from subjects with asthma when compared with normal lung donors and healthy volunteers
brenda
-
cell line derived from newborn H-2kb tsA58 transgenic mice
brenda
-
cells form tubular structures after stimulation by angiogenic factors, e.g. the enzyme and the basic fibroblast growth factor bFGF, treatment leads to cell survival and prevents from apoptosis, respectively
brenda
additional information
G2 and G3 tumour tissues, and invasive tumour cells
brenda
the enzyme translocates to the surface upon activation to function in extracellular matrix degradation
brenda
-
Hyal3 is expressed in epididymal tissue/fluid, from where it is acquired by caudal mouse sperm in vitro
brenda
isoform HYAL 4 has little expression in the renal papilla
brenda
isoforms HYAL 1 is highly expressed in the renal papilla
brenda
isoforms HYAL 2 is highly expressed in the renal papilla
brenda
isoforms HYAL 3 is highly expressed in the renal papilla
brenda
-
from mice grafted with human-tumour-derived, enzyme secreting H460M or SA87 cells, and mice grafted with enzyme non-secreting CB 193 cells
brenda
-
Hyal3 is expressed in epididymal tissue/fluid, from where it is acquired by caudal mouse sperm in vitro
brenda
-
-
brenda
-
-
700874, 695542, 699233, 699474, 698133, 699963, 703288, 705245, 705485, 701690, 702753, 703188, 716094, 717012, 714053, 714911, 714954, 729842, 730951, 730998, 729118, 729585
brenda
two highly purified isoforms of sheep testicular hyaluronidase
brenda
high expression in adult male testis, low expression in young male testis
brenda
additional information
KY098772
higher growth and hyase production are observed in nutrient broth fortified with hyaluronic acid at pH 7.0, temperature 37°C, 120 rpm upon 48 h of incubation
brenda
additional information
-
higher growth and hyase production are observed in nutrient broth fortified with hyaluronic acid at pH 7.0, temperature 37°C, 120 rpm upon 48 h of incubation
-
brenda
additional information
both splice variants of gene mgea5 are ubiquitously expressed in various tissues
brenda
additional information
-
both splice variants of gene mgea5 are ubiquitously expressed in various tissues
brenda
additional information
-
during virus maturation in the host cell, the enzyme is located at the cell surface by a GPI-anchor
brenda
additional information
differential cellular localization of enzymes, with hyaluronidase 1 in astrocytes and hyaluronan synthase 2 in astrocytes and neurons, and poststroke upregulation of both of them in astrocytes. No association between Hyal-1 expression and Iba1- or NeuN-positive cells is visible. Isozymes Hyal-1 and Hyal-2 expression in astrocytic and neuronal cultures in ischaemic post-stroke and control mice, overview
brenda
additional information
differential cellular localization of enzymes, with hyaluronidase 1 in astrocytes and hyaluronan synthase 2 in astrocytes and neurons, and poststroke upregulation of both of them in astrocytes. No association between Hyal-1 expression and Iba1- or NeuN-positive cells is visible. Isozymes Hyal-1 and Hyal-2 expression in astrocytic and neuronal cultures in ischaemic post-stroke and control mice, overview
brenda
additional information
differential cellular localization of enzymes, with hyaluronidase 1 in astrocytes and hyaluronan synthase 2 in astrocytes and neurons, and poststroke upregulation of both of them in astrocytes. Hyal-2 immunoreactivity is sparse and low. In sham cortex, dotted staining is observed that localizes to apical part of putative neuronal bodies mostly located in layer V and astrocytic cell bodies and processes. Neuronal staining does not change, but astrocytic Hyal-2 immunoreactivity is increased 7 days post-stroke in the perilesional area and ipsilateral hippocampus. Isozymes Hyal-1 and Hyal-2 expression in astrocytic and neuronal cultures in ischaemic post-stroke and control mice, overview
brenda
additional information
differential cellular localization of enzymes, with hyaluronidase 1 in astrocytes and hyaluronan synthase 2 in astrocytes and neurons, and poststroke upregulation of both of them in astrocytes. Hyal-2 immunoreactivity is sparse and low. In sham cortex, dotted staining is observed that localizes to apical part of putative neuronal bodies mostly located in layer V and astrocytic cell bodies and processes. Neuronal staining does not change, but astrocytic Hyal-2 immunoreactivity is increased 7 days post-stroke in the perilesional area and ipsilateral hippocampus. Isozymes Hyal-1 and Hyal-2 expression in astrocytic and neuronal cultures in ischaemic post-stroke and control mice, overview
brenda
additional information
level and pattern of Hyal1 expression in different tissues
brenda
additional information
level and pattern of Hyal1 expression in different tissues
brenda
additional information
level and pattern of Hyal1 expression in different tissues
brenda
additional information
level and pattern of Hyal2 expression in different tissues
brenda
additional information
level and pattern of Hyal2 expression in different tissues
brenda
additional information
level and pattern of Hyal2 expression in different tissues
brenda
additional information
level and pattern of Hyal3 expression in different tissues
brenda
additional information
level and pattern of Hyal3 expression in different tissues
brenda
additional information
level and pattern of Hyal3 expression in different tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mouse isoforms are differentially distributed in the soluble, membrane, and acrosome-related fraction, where they are most abundant
-
brenda
-
mouse isoforms are differentially distributed in the soluble, membrane, and acrosome-related fraction, where they are most abundant
-
brenda
Hyal2 is partly expressed at the cell surface
brenda
Hyal2 is strongly associated with cell membrane fractions from which it can be extracted using a Triton X-114 treatment, but not an osmotic shock or an alkaline carbonate solution. Treatment of membrane preparations with phosphatidylinositol-specific phospholipase C releases immunoreactive Hyal2 into the aqueous phase. The protein is attached to the membrane through a functional GPI anchor. Hyal2 transfected in COS-7 cells is associated with detergent-resistant, cholesterol-rich membranes known as lipid rafts
brenda
also expressed at the apical pole associated with the plasma membrane in bronchial epithelial cells
brenda
-
protein resides in the membrane over the sperm head and midpiece
brenda
-
mouse isoforms are differentially distributed in the soluble, membrane, and acrosome-related fraction, where they are most abundant. Protein resides in the membrane over the sperm head and midpiece
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
isoform Vesp v 2A only exists in the genera Vespa and Vespula, not in Polistes species
evolution
the most abundant isoform Vesp v 2B exhibits 93% sequence identity with the Ves v 2 isoform of Vespula vulgaris
evolution
the enzyme belongs to the glycosyl hydrolase family 56, GH56
evolution
Hirudo sp.
-
leech hyaluronidase (LHase) is a member of hyaluronate 3-glycanohydrolases
malfunction
-
HYAL5-deficient epididymal sperm is functionally normal, the loss of SPAM1 results in a remarkably increased accumulation of sperm on the surface or outer edge of the cumulus
malfunction
-
enzyme deficiency reduces survival in macrophages compared to the wild type and stimulates a significantly higher release of proinflammatory cytokines, such as interleukin (IL)-1beta, IL-6, and tumor necrosis factor alpha than the wild type in macrophages as well as in mice
malfunction
patients with inflammatory bowel disease have lower platelet HYAL2 levels and activity than healthy controls
malfunction
perineuronal nets (PNNs) are presumed to limit plasticity in adult animals. Ischaemic stroke results in the massive breakdown of PNNs resulting in rejuvenating states of neuronal plasticity. As hyaluronic acid (HA) is the structural backbone of PNNs, these changes might be a consequence of the altered expression of HA metabolism enzymes. Early hyaluronidase inhibition could interfer with post-stroke PNN reduction and behavioural recovery. After stroke, a substantial reorganization of polysaccharide content occurs. Hyaluronidase inhibition accelerates functional recovery from stroke in the mouse brain
malfunction
-
enzyme deficiency reduces survival in macrophages compared to the wild type and stimulates a significantly higher release of proinflammatory cytokines, such as interleukin (IL)-1beta, IL-6, and tumor necrosis factor alpha than the wild type in macrophages as well as in mice
-
metabolism
gene expression of two hyaluronidase isozymes, HYAL1 and HYAL2, and HA-binding receptor CD44 are studied in two injury models: rat sciatic nerve crush and critical gap transection. HYAL2 and CD44 are shown to be upregulated 3 days after crush injury, whereas HYAL1 is upregulated at 3 weeks, which collectively demonstrate temporal patterning of HA breakdown. Additionally, differences are observed between HYAL and HA expression at 3 weeks when compared for both nerve injury models
metabolism
-
gene expression of two hyaluronidase isozymes, HYAL1 and HYAL2, and HA-binding receptor CD44 are studied in two injury models: rat sciatic nerve crush and critical gap transection. HYAL2 and CD44 are shown to be upregulated 3 days after crush injury, whereas HYAL1 is upregulated at 3 weeks, which collectively demonstrate temporal patterning of HA breakdown. Additionally, differences are observed between HYAL and HA expression at 3 weeks when compared for both nerve injury models
-
physiological function
Hyal2, through direct interactions with CD44 and possibly some pericellular hyaluronidase activity requiring acidic foci, suppresses the formation or the stability of the glycocalyx, modulates ezrin-radixin-moesin-related cytoskeletal interactions, and diminishes cell motility
physiological function
-
SPAM1 is involved in sperm penetration through the cumulus matrix
physiological function
the Synanceia verrucosa hyaluronidase enhances the capillary permeability-increasing activity of the Synanceia verrucosa toxin, neoverrucotoxin
physiological function
-
generation of a deletion mutant in the Caenorhabditis elegans orthologue of mammalian hyaluronidase, Hya-1. Mutant animals are viable and grossly normal, but exhibit defects in vulval morphogenesis and egg-laying and show increased staining with alcian blue, consistent with an accumulation of glycosaminoglycan. A hya-1::GFP reporter is expressed in a restricted pattern in somatic tissues of the animal with strongest expression in the intestine, the PLM sensory neurons and the vulva. Total protein extracts from wild-type animals exhibit chondroitin-degrading but not hyaluronan-degrading activity. Chondroitinase activities are observed at both neutral and acidic pH conditions while both neutral and acidic activities are absent in extracts from Hya-1 mutant strains
physiological function
-
although fully fertile, Hyal3 null sperm shows delayed cumulus penetration and reduced acrosomal exocytosis. Spam1 null mutants lacking sperm adhesion molecule 1 have significantly diminished Hyal3 activity
physiological function
-
the enzyme play a special role in the testes of adult mice being involved in the maturation of sperm or during fertilization
physiological function
-
hyaluronidase has a strong influence on the intracellular survival of Streptococcus agalactiae and proinflammatory cytokine expression, suggesting that it plays a key role in pathogenicity
physiological function
the enzyme potentiates the hemorrhagic and hemolytic activity of whole venom, but decreases subplantar edema caused by an L-amino acid oxidase
physiological function
human platelets degrade the proinflammatory matrix hyaluronan through the activity of HYAL2 and platelet activation causes the immediate translocation of HYAL2 from a distinct population of alpha-granules to platelet surfaces where it exerts its catalytic activity
physiological function
-
hyaluronic acid (HA), a polysaccharide present in the extracellular matrix, is a linear, non-sulfated glycosaminoglycan consisting of a repeating group of units of N-acetylglucosamine and glucuronic acid. When canceration, inflammation, and oxidative stress occur, the dynamic balance of the extracellular matrix is disrupted. The rapid degradation of endogenous high molecular weight HA by hyaluronidase (HAase) and reactive oxygen species leads to an increase in low molecular weight HA (about 250 kDa), which stimulates the production of proinflammatory cytokines, subsequently raising the risk of disease development
physiological function
hyaluronic acid (HA) is ubiquitously found in biological tissues and mediates wound healing mechanisms after injury by promoting cell migration and proliferation. Hyaluronidases (HYALs) are the complementary enzymes that are responsible for HA turnover and endogenous degradation. Hyaluronidase isozymes act in a spatiotemporal manner dictated by their roles in hyaluronate (HA) catabolism, temporal patterning of HA breakdown, overview. Isozyme HYAL2 is the main mediator of extracellular high molecular weight HA breakdown, whereas isozyme HYAL1 is responsible for intracellular breakdown of HA oligomers smaller than 20 kDa. These roles define their temporal action, where HYAL2 is expressed as a precursor to HYAL1. HA content and hyaluronidase expression do not significantly change after nerve crush injury out to 6 weeks, however there may be differences in HA turnover between transection and crush injury models
physiological function
PH20 is a hyaluronidase enzyme that can hydrolyze the glycosidic bond in hyaluronic acid as the major proteoglycan found in extracellular matrices
physiological function
hyaluronidases from animal venoms cleave hyaluronan present in the extracellular matrix, acting as spreading factors of toxins into the tissues of the victim
physiological function
Hirudo sp.
-
leech hyaluronidase (LHase) degrades hyaluronate(HA) into (GlcNAc- GlcUA)2 and (GlcNAc-GlcUA)3 by cleaving the beta-1,3-glucuronide bonds, and efficiently produce oligomers with glucuronic acid on the reducing end
physiological function
by cleaving the beta-1,4 N-acethylhexosaminide bonds, BTH degrades hyaluronate into (GlcUA-GlcNAc)2 and (GlcUA-GlcNAc)3
physiological function
-
the venom of the brasilian scorpion Rhopalurus crassicauda contains the scorpion neurotoxin (Rc1), and a spreading factor, the hyaluronidase. Hyaluronidases facilitate the spreading of toxins into the tissues of the prey/victims, since these enzymes hydrolyze hyaluronan of the interstitial matrix. Brazilian scorpion (ScA) antivenom recognizes the hyaluronidase, although not the toxin
physiological function
-
hyaluronic acid (HA) is ubiquitously found in biological tissues and mediates wound healing mechanisms after injury by promoting cell migration and proliferation. Hyaluronidases (HYALs) are the complementary enzymes that are responsible for HA turnover and endogenous degradation. Hyaluronidase isozymes act in a spatiotemporal manner dictated by their roles in hyaluronate (HA) catabolism, temporal patterning of HA breakdown, overview. Isozyme HYAL2 is the main mediator of extracellular high molecular weight HA breakdown, whereas isozyme HYAL1 is responsible for intracellular breakdown of HA oligomers smaller than 20 kDa. These roles define their temporal action, where HYAL2 is expressed as a precursor to HYAL1. HA content and hyaluronidase expression do not significantly change after nerve crush injury out to 6 weeks, however there may be differences in HA turnover between transection and crush injury models
-
physiological function
-
hyaluronidase has a strong influence on the intracellular survival of Streptococcus agalactiae and proinflammatory cytokine expression, suggesting that it plays a key role in pathogenicity
-
additional information
development of a comprehensive kinetic model describing the enzymatic cleavage of hyaluronan (HA) by bovine testicular hyaluronidase (BTH) specifically on the late stage of the hydrolysis, where the concentrations of a limited number of oligomers may be determined experimentally with accuracy as functions of time. The model is applied to fit different experimental sets of kinetic data collected by capillary electrophoresis at two HA concentrations and three concentrations of PEG crowder. The reaction mechanism in the late degradation stage essentially reduces to the cleavage or transfer of active dimers. While the recombination of dimers is the fastest reaction, the rate-limiting step turns out to be invariably the hydrolysis of hexamers. Crowding, hyaluronan itself or other inert, volume-excluding agents, clearly boosts recombination events and concomitantly slows down all fragmentation pathways. Kinetic fragmentation mechanism, overview
additional information
Hirudo sp.
-
the crystal structure of LHase reveals a (beta/alpha)8-barrel domain and a beta-sandwich domain, corresponds to other GH79 family proteins for the wild-type enzyme. Two glutamine residues E176 and E290 are considered as the catalytic residues, and a distinguishable exo-pocket loop is proved to associate with the HA binding, HA specificity and the endolytic way of action of LHase
additional information
enzyme residue Glu113 is the proton donor, and the N-acetyl carbonyl group of hyaluronate acts as the nucleophilic base. The BVH enzyme contains a second hyaluronate binding site which works in coordination with a bulky loop formation, for the release of hydrolysis product
Show AA Sequence and Transmembrane Helices (9425 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
x * 130000, enzyme form 1, SDS-PAGE, x * 75000, enzyme form 2, SDS-PAGE
180000
40000
45000
47000
50000
52000
54000
55000
59000
64500
65000
-
SDS-PAGE, the 65000 Da enzyme form found in seminal vesicle fluids is active only at acidic pH and does not interact with heparin
69000
70000
75000
x * 130000, enzyme form 1, SDS-PAGE, x * 75000, enzyme form 2, SDS-PAGE
80000
additional information
52000
-
SDS-PAGE under non-reducing conditions, three enzyme bands are detected the most prominent one at 52000 Da
54000
-
recombinant enzyme from Drosophila melanogaster Schneider-2 cells, SDS-PAGE
55000
-
SDS-PAGE, the 55000 Da enzyme form is active both at the acidic (pH 3.7) and the neutral pH (pH 7.4) and is able to bind to heparin
80000
-
SDS-PAGE, presumably glycosylated (53000 Da, expected molecular mass)
additional information
presence of multiple forms of Hyal3 ranging from about 45000 to 56000 Da in expression lysates
additional information
-
presence of multiple forms of Hyal3 ranging from about 45000 to 56000 Da in expression lysates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 130000, enzyme form 1, SDS-PAGE, x * 75000, enzyme form 2, SDS-PAGE
monomer
-
1 x 45000, non-reduced enzyme SDS-PAGE, 1 * 54000, reduced enzyme, SDS-PAGE
additional information
the recombinant enzyme has an unusual (beta/alpha)7 TIM barrel structure, different from classical eight-stranded structures in other glycosyl hydrolases
additional information
-
2 isoforms of approximately 55 kDa and 75 kDa
additional information
-
2 isoforms of approximately 55 kDa and 75 kDa
additional information
-
three-dimensional structure analysis and modeling of isozymes, structure-reaction mechanism relationship, overview
additional information
-
2 isoforms of approximately 55 kDa and 75 kDa
additional information
-
2 isoforms of approximately 55 kDa and 75 kDa, a high molecular weight isoform in venom
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
mannosylation at Trp130 negatively regulate enzyme secretion and attenuates enzymatic activity
glycoprotein
-
N-glycosylation is absolutely necessary for activity, deglycosylation leads to complete loss of activity, enzyme binds to lectins Con A, LEL, STL, PHA-e, Jacalin, and PSA, mannose is the major sugar within and at the terminal sequence of the glycans
glycoprotein
the enzyme has two glycosylation sites. The activity of deglycosylated H3S1 diminishes by 29.2 % compared to glycosylated H3S1. Deglycosylation by PNGase F treatment. N-glycan FM4A1 (Fuc1HexNAc3Hex4) is attached to the NVHSVNVCMAEDICIEGPVK peptide of H3S1. The structure comprises one N-glycoform [HexNAc2Hex9] attached to the IINVTLAAK peptide (Asn333), whereas five N-glycoforms [Fuc1HexNAc2Hex3], [Fuc1HexNAc3Hex3], [Fuc1HexNAc3Hex4], [Fuc1HexNAc4Hex3], and [Fuc1HexNAc3Hex5] are attached to the NVHSVNVCMAEDICIEGPVK peptide (Asn422)
glycoprotein
the enzyme has two glycosylation sites. The activity of deglycosylated H3S2 diminishes by 28.9% compared to glycosylated H3S2. Deglycosylation by PNGase F treatment. N-glycan FM4A1 (Fuc1HexNAc3Hex4) is attached to the NVHSVNVCMAEDICIEGPVK peptide of H3S2. The structure comprises one N-glycoform [HexNAc2Hex9] attached to the IINVTLAAK peptide (Asn333), whereas five N-glycoforms [Fuc1HexNAc2Hex3], [Fuc1HexNAc3Hex3], [Fuc1HexNAc3Hex4], [Fuc1HexNAc4Hex3], and [Fuc1HexNAc3Hex5] are attached to the NVHSVNVCMAEDICIEGPVK peptide (Asn422)
glycoprotein
the enzyme contains three potential N-glycosylation sites
glycoprotein
sequence is predicted to have potential N-glycosylation sites at the positions 78, 169 and 364
glycoprotein
recombinant enzyme treatment with PNGase F and analysis by mass spectrometry (MALDI-TOF) indicate a potential N-glycosylation of 4.5 kDa
proteolytic modification
posttranslational modification of a larger protein of 130 kDa to a 75 kDa form
proteolytic modification
the precursor enzyme contains a signal sequence for targeting into endoplasmic reticulum
proteolytic modification
sequence contains a N-terminal signal pepitde of 28 amino acids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
8-10 mg/ml purified recombinant enzyme, with or wihtout hexameric hyaluronic acid, in 5 mM sodium acetate, pH 5.4, hanging drop vapour diffusion method, 20°C, for triclinic crystals, equal volume of protein solution with reservoir solution containing 30% PEG 8000, 0.1 M sodium cacodylate, pH 6.5, 0.2 M ammonium sulfate, equilibration against the reservoir solution, 6-8 months, for monoclinic crystal growth within several days, 10% PEG 6000, 1.0 M NaCl, 20 mM acetic acid, pH 4.2 is used for mixing and equilibration, X-ray diffraction structure determination and analysis at 1.6-2.7 A resolution
three-dimensional structure analysis
hanging drop vapour diffusion method with mother liquor containing 1.5 M NaCl, 10% (v/v) ethanol, and 1/10 volume of 30% (w/v) galactose, at pH 4.6
structure analysis of the enzyme HYAL-1 with the EGF-like domain, PDB ID 2PE4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D129N
D146N
-
site-directed mutagenesis of HPH-20, the mutant shows highly reduced activity
DELTA351-end
putative structural mutant with a deleted EGF-like domain, significant decreased enzymatic activity
DELTA356-end
putative structural mutant with a deleted EGF-like domain, significant decreased enzymatic activity
E131Q
N216A
N350A
R265L
S245A
Y202F
Y247F
additional information
D129N
catalytic mutant, Km higher compared to wild-type, Vmax lower than wild-type
N216A
putative structural mutant, Km higher compared to wild-type, Vmax unaltered compared to wild-type, ca. 44% of wild-type activity
N350A
putative structural mutant, significant decreased enzymatic activity
R265L
putative structural mutant, significant decreased enzymatic activity
S245A
substrate binding mutant, Km higher compared to wild-type, Vmax unaltered compared to wild-type, ca. 41% of wild-type activity
Y202F
substrate binding mutant, Km higher compared to wild-type, Vmax lower than wild-type
additional information
after expression of a fusion protein by linking hyaluronidase and human serum albumin together with the recognition sequence for the protease, factorXa, fragmented protein products are obtained in the culture supernatant, only after replacement of the hinge region with a serine-glycine-rich linker, stable full-length fusion protein could be generated
additional information
when changing the codons of the original transcript to triplet sequences preferred by Pichia pastoris, no further increase of protein product can be achieved
additional information
-
the effect of hyaluronidase coinoculation on the outcome of Leishmania major infection in BALB/c mice: Hyaluronidase exacerbates skin lesions caused by Leishmania major, more severe lesions developed in mice where Leishmania major promastigotes are coinjected with hyaluronidase
additional information
mutagenesis analysis reveales that among the five potential N-linked glycosylation sites, three contributed to significant inhibition of hyaluronidase activity
additional information
-
mutagenesis analysis reveales that among the five potential N-linked glycosylation sites, three contributed to significant inhibition of hyaluronidase activity
additional information
Hirudo sp.
-
by the destruction of the HA layer by recombinantly expressing leech hyaluronidase and optimization of synthetic pathway, a highest-to-date LMM-HA production of 74.1 g/l has been achieved by engineered Corynebacterium glutamicum. A temperature-controlled HA synthesis system is constructed in Bacillus subtilis by introducing a temperature-sensitive plasmid with a leech hyaluronidase gene insertion. HA in different wanted molecular mass is produced by simply adjusting the incubation temperature of recombinant strain
additional information
-
expression as PH-20-autotransporter fusion protein for cell surface display in Escherichia coli F470, a strain missing the O-polysaccharide of LPS, yields cells with sufficient hyaluronidase activity
additional information
construction of two donor plasmids, one of them with one and the second with two PH20 expression cassettes. The expression vectors are site specifically integrated into the genome of HEK293T cells using PhiC31 integrase system to develop HEK293T stable cell lines secreting His-tagged recombinant human PH20 (rhPH20) in the culture supernatant. The secreted rhPH20 in the culture supernatant has the specific activity of 16660 IU/mg and the recombinant enzyme is able to remove the cumulus cells from oocytes. PhiC31 enzyme inserts the PH20-expressing donor vectors into the specific pseudo attP sites including 10q21.2 and 20q11.22 in the genome of the target cells with different copy numbers. RT-PCR enzyme expression analysis. PhiC31 integrase system is able to be applied as a robust tool for efficient production and secretion of soluble and active rhPH20 by HEK293T cells as a semi-adherent human cell line
additional information
the expression of CD44v6 is reduced when MDA-MB-231 cancer cells are treated with BmHYA1 for 48 h
additional information
EU152302
after expression of a fusion protein by linking hyaluronidase and human serum albumin together with the recognition sequence for the protease, factorXa, fragmented protein products are obtained in the culture supernatant, only after replacement of the hinge region with a serine-glycine-rich linker, stable full-length fusion protein could be generated
additional information
EU152302
when changing the codons of the original transcript to triplet sequences preferred by Pichia pastoris, no further increase of protein product can be achieved
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
5.1 - 5.9
human serum hyaluronidase 1 is inactive above pH 5.1, while human serum hyaluronidase 1 variant HYAL1DELTAL exhibits activity up to pH 5.9
5
stable at pH 5.0 for 40 h, with a slight decrease after 160 h incubation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
enzyme is stable for at least 30 min when incubated at 20°C and 30°C
4 - 90
40
50
4 - 90
34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum
4 - 90
EU152302
34% activity at temperatures as low as 4°C still exhibits hydrolase activity at 90°C to an extent of 19% in comparison to the optimum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
adding bovine serum albumin (1.0 mg/ml) to the enzyme sample prior to freezing results in complete retention of enzyme activity
-
at room temperature activity rapidly lost, addition of a peptide derived from gelatin increases stability
-
enzyme activity lost by freezing, addition of bovine serum albumin or 1% dimethylsulfoxide, v/v, prevents inactivation
-
extremely labile, addition of 1% bovine serum albumin prevents inactivation for more than 1 month at -70°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22°C, 100 mM sodium acetate buffer (pH 3.8) containing 150 mM NaCl, 4 weeks, 58% activity retained
-
4°C, 100 mM sodium acetate buffer (pH 3.8) containing 150 mM NaCl, 4 weeks, 92% activity retained
-
4°C, purified native enzyme, pH 7.0, stable for 30 days without loss of activity
KY098772
room temperature, purified native enzyme, pH 7.0, loss of 40% activity within 30 days
KY098772
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
25.6fold to homogeneity from venom by gel filtration and ion exchange chromatography
Palamneus gravimanus
-
according to their inhibition activity for hyaluronidases, 6-chloromethyluracil and 2-aminobenzimidazole are coupled with sepharose beads for the affinity adsorption of bovine hyaluronidase-1. In good accordance with structural simulation, the ligands designed from 2-aminobenzimidazole show much higher specificity for the target enzyme, because they had more H bonds and pi-pi interactions with target sites. After optimization, through one step of affinity adsorption with sorbent L-4, bovine hyaluronidase can be isolated from the supernatant of bovine testes extract, with purity and recovery up to 96.4% and 89.4%, respectively. Based on the less steps of purification, short time consuming, higher purity, and higher activity recoveries, industrial application of this method is of great potential
by gel filtration
by ion exchange chromatography and gel filtration
by ion exchange chromatography at pH 5.0
Chelating Sepharose Fast Flow column chromatography and Sephacryl S200 gel filtration
CM-cellulose-52 column chromatography, phenyl-Sepharose column chromatography, and Sephacryl S-100 gel filtration
from sperm surface by treatment with phosphatidylinositol-specific phospholipase C
-
Hyal2 is strongly associated with cell membrane fractions from which it can be extracted using a Triton X-114 treatment, but not an osmotic shock or an alkaline carbonate solution. Treatment of membrane preparations with phosphatidylinositol-specific phospholipase C releases immunoreactive Hyal2 into the aqueous phase. The protein is attached to the membrane through a functional GPI anchor. Hyal2 transfected in COS-7 cells is associated with detergent-resistant, cholesterol-rich membranes known as lipid rafts
isozymes NNH1 and NNH2 33fold and 26fold, respectively, from venom by gel filtration and ion exchange chromatography
-
native enzyme 13fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration, to near homogeneity
KY098772
native isozyme NNH1 33fold to homogeneity from venom by successive gel filtration and ion exchange chromatography
-
native isozyme NNH2 26fold to homogeneity from venom by successive gel filtration and ion exchange chromatography
-
partial
purified by gel filtration on Sephacryl S-100 and ion-exchange chromatography on SP-Sepharose. Procedure provides 376.4fold purification with a 2.94% yield
-
recombinant enzyme 1.31fold from Pichia pastoris by cation exchange chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
-
recombinant enzyme from Spodoptera frugiperda Sf9 cells by metal affinity chromatography and gel filtration
recombinant enzyme Hyal-1 from DS-2 cells by metal affinity chromatography
recombinant enzyme PH-20 from Pichia pastoris strain GS115 by Phenylboronic acid resin adsorption and metal affinity chromatography
recombinant His6-tagged viral enzyme from insect cells by metal affinity chromatography, ultrafiltration, and gel filtration
-
recombinant tagged enzyme BTH from Spodoptera frugeiperda Sf9 cells or from Pichia pastoris strain GS115 by metal affinity chromatography
Sephadex G-100 column chromatography and CM-Sephadex C-25 column chromatography
-
the commercial preparation is further purified by heparin affinity chromatography and gel filtration. Two STH isozymes, H3S1 and H3S2, are obtained to a purity of over 98% with a yield of 3.4% and 5.1%, respectively. Isozyme H3S2 is purified by 8fold
the commercial preparation is futher purified by heparin affinity chromatography and gel filtration. Two STH isozymes, H3S1 and H3S2, are obtained to a purity of over 98% with a yield of 3.4% and 5.1%, respectively. Isozyme H3S1 is purified by 5.8fold
the two hyaluronidase isozymes Vesp v 2A and Vesp v 2B cannot be separated from each other, but they are partially purified
to homogeneity, 2step chromatography
using successive chromatography: gel filtration, anion exchange chromatography, cation exchange chromatography, reversed-phase HPLC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of core nucleotide sequence in two fused fragments, PH-20 gene DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
DNA and amino acid sequence analysis, expression as active C-terminally His-tagged enzyme in insect cells via baculovirus infection
DNA and amino acid sequence determination and analysis, cloning of a codon optimized gene and recombinant functional expression in Escherichia coli strain BL21(DE3) in inclusion bodies, method evaluation and process optimization for production of a high specific titer of active soluble enzyme, overview
DNA and amino acid sequence determination and analysis, expressed by injection of mRNA in frog oocytes on the outer surface of the cell membrane
DNA and amino acid sequence determination and analysis, in vitro translation
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
KY098772
expressed in 22Rv1 human prostate adenomacarcinoma cells and in HEK-293 human embryonic kidney cells as a N-terminal FLAG fusion protein. Abundant soluble FLAG-tagged Hyal1 is secreted to the conditioned cell culture media of transfectants
expressed in COS-7 cells
expressed in Escherichia coli BL21(DE3)RIL cells and Drosophila melanogaster Schneider-2 cells
-
expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein
expression of His6-tagged viral enzyme via baculovirus transfection in Spodoptera frugiperda Sf9 insect cells, the His-tag replaces the GPI anchor of the enzyme to make it soluble
-
gene Hyal-1, recombinant expression of tagged enzyme BTH in Spodoptera frugeiperda Sf9 cells and in Pichia pastoris strain GS115, recombinant expression in HEK-293 cells
gene mgea5, DNA sequence determination and analysis, genomic organization on chromosome 10, 2 splice variants, one missing a putative acetyltransferase domain of the enzyme
gene SPAM1, recombinant expression of enzyme PH-20 in Pichia pastoris strain GS115
genes HYAL1, HYAL2, and HYAL3 are clustered on chromosome SSC13q21, DNA and amino acid sequence determination and analysis
genes HYAL1, HYAL2, and HYAL3 clustered on chromosome SSC13q21, DNA and amino acid sequence determination and analysis
isozymes Hyal1-Hyal4, sequence comparison, the genes encoding isozymes Hyal1-Hyal3 are tightly clustered on chromosome 3q21.3, Hyal4 and HPH-20 are clustered on 7q31.3, expression profiles
-
precursor from venom gland, DNA and amino acid sequence determination and analysis, phylogenetic analysis and sequence comparisons, functional expression of His-tagged enzyme in insect cells, but not in Escherichia coli, and secretion of the recombinant enzyme, overview
recombinant enzyme expression in Spodoptera frugiperda Sf9 cells
recombinant exxpression of hyaluronidase from scorpion venom in Pichia pastoris from the pPICZalphaA vector
the bovine SPAM1 open reading frame is cloned into the mammalian expression vector pCXN2 and then transfected to the HEK293 cell line
using the information of preferred Pichia pastoris codons as provided by Genscript, Inc., the native sequence is de novo synthesized to create a fully codon-optimized cDNA (Hya delta c) and the synthetic gene is expressed in Pichia
EU152302
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant effect of stroke on Hyal-1 expression is observed in the perilesional area. Transcriptional upregulation is observable 24 hr post-stroke, peaks 7 days post-stroke, and is no longer observed 1 month after photothrombosis
an effect of stroke on Hyal-1 expression is observed in the perilesional area. A transient increase in Hyal-2 expression is observed 24 hr post-stroke. In the contralateral areas, or in the remote area, no significant changes in Hyal-1 and Hyal-2 expression are found
basic fibroblast growth factor decreases hyaluronidase-2 expression in HT-1080 cells
estrogen receptor(-) breast cancer cells secrete significantly more hyaluronidase than estrogen receptor(+) breast cancer cells
-
gene expression of two hyaluronidase isozymes, HYAL1 and HYAL2, and HA-binding receptor CD44 are studied in two injury models: rat sciatic nerve crush and critical gap transection. HYAL2 and CD44 are shown to be upregulated 3 days after crush injury, whereas HYAL1 is upregulated at 3 weeks, which collectively demonstrate temporal patterning of HA breakdown. Additionally, differences are observed between HYAL and HA expression at 3 weeks when compared for both nerve injury models
hyaluronidase activity is elevated in dehydrated rats
hyaluronidase-1 activity is increased in the lungs of monocrotaline-challenged rats
the median of isoform HYAL1 mRNA level is 69% lower in grade 3 serous ovarian cancers compared to normal ovaries
gene expression of two hyaluronidase isozymes, HYAL1 and HYAL2, and HA-binding receptor CD44 are studied in two injury models: rat sciatic nerve crush and critical gap transection. HYAL2 and CD44 are shown to be upregulated 3 days after crush injury, whereas HYAL1 is upregulated at 3 weeks, which collectively demonstrate temporal patterning of HA breakdown. Additionally, differences are observed between HYAL and HA expression at 3 weeks when compared for both nerve injury models
gene expression of two hyaluronidase isozymes, HYAL1 and HYAL2, and HA-binding receptor CD44 are studied in two injury models: rat sciatic nerve crush and critical gap transection. HYAL2 and CD44 are shown to be upregulated 3 days after crush injury, whereas HYAL1 is upregulated at 3 weeks, which collectively demonstrate temporal patterning of HA breakdown. Additionally, differences are observed between HYAL and HA expression at 3 weeks when compared for both nerve injury models
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in inclusion bodies in Escherichia coli strain BL21(DE3) is solubilized using solubilization buffer containing 7.5 M guanidine hydrochloride and 62 mM Tris, at pH 8.0
using 100 mM Tris-HCl pH 10.0, 3 mM reduced glutathione, 0.3 mM oxidized glutathione, 0.4 M L-arginine, 0.2 mg bovine serum albumin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
cancer cell lines often secrete hyaluronidase, the enzyme might therefore be a marker for growing tumours
biotechnology
diagnostics
increased concentration of HYAL1-type enzyme correlates with tumour progression and is a marker for grade (G) 2 or 3 bladder cancer
medicine
molecular biology
-
the influence of hyaluronidase digestion modulates CD44 expression in various cancer cell lines
pharmacology
-
isozyme NNH1 is a target for first aid agents from plants in snakebit therapy
biotechnology
-
a fluorescent substrate (FRET-HA) to quantitatively assess hyaluronidase activity is developed
biotechnology
-
novel products in hyaluronan digested by commercially available bovine testicular hyaluronidase are found which originate from a novel enzyme contaminat in the BTH
medicine
-
increasing absorption of fluids in dermal clysis, increasing diffusion of injected substances
medicine
EU152302
this recombinant hyaluronidase can be applied for biochemical or medical purposes
medicine
this recombinant hyaluronidase can be applied for biochemical or medical purposes
medicine
as major hyaluronidases in human cells, HYAL1 and HYAL2 may control intercellular interactions and microenvironment of tumour cells providing excellent targets for cancer treatment
medicine
-
hyaluronidases are added to anticancer regimens, particularly in Europe. Tumors previously resistant to chemotherapy become sensitive when hyaluronidase is added. The enzyme may decrease intratumoral pressure, permitting drugs to penetrate the malignancy. Studies are available suggesting that hyaluronidase has intrinsic anti-tumor activity
medicine
-
human cancers grown in SCID mice regress dramatically following administration of purified testicular hyaluronidase. Hyaluronidase treatment also prevents lymph node invasion in a murine model for T-cell lymphoma
medicine
-
hyaluronidase correlates with tumor progression which is documented in tumors of the male genito-urinary tract, in prostate and urinary bladder cancers. Aggressiveness of other human cancers also correlates with hyaluronidase, including breast and laryngeal cancer
medicine
-
the codelivery of hyaluronidase enzyme with oncolytic adenoviruses is analysed to determine whether it improves the spread of the virus throughout tumors, thereby leading to a greater overall antitumor efficacy in tumor models: In mice injected with the adenovirus Ad5/35GFP and hyaluronidase (50 U), a significant increase in the number of GFP-expressing cells is observed when compared with animals injected with virus only. When the oncolytic adenoviruses Ad5OV or Ad5/35 OV are codelivered with 50 U of hyaluronidase, a significant delay in tumor progression is observed, which translates into a significant increase in the mean survival time of tumor-bearing mice compared with either of the monotherapy-treated groups. Furthermore, the mice that receive the combination of Ad5/35 OV and hyaluronidase show the best antitumor efficacy
medicine
it is assessed whether hyaluronic acid and HYAL-1 can predict progression to muscle invasion and recurrence among patients with non-muscle-invasive bladder carcinoma. In a cohort of 178 bladder carcinoma specimens HA and HYAL-1 expression is evaluated by immunohistochemistry and graded for intensity and area of staining. Association of HA and HYAL-1 staining with bladder carcinoma recurrence and muscle invasion is evaluated by univariate and multivariate models. HYAL-1 is a potential prognostic marker for predicting progression to muscle invasion and recurrence
medicine
the effect of anticoagulants on plasma HAase activity is evaluated and compared with the serum HAase activity that is devoid of anticoagulants. The plasma HAase activity in the presence of the recommended concentration of EDTA is highly comparable to that of the serum HAase activity. In contrast, citrated or heparinized plasma record a significantly reduced level of activity than that of the serum HAase activity. EDTA-treated plasma samples are a better choice compared with heparin and citrated samples to assess the HAase activity
medicine
-
intravitreous injection of ovine hyaluronidase to patients with persistent vitreous hemorrhage is efficacious and has a favorable safety profile
medicine
hyaluronidase 1 is a prognostic indicator for both local recurrence and progression of non-muscle-invasive bladder cancer after transurethral resection
medicine
-
isoforms of hyaluronidase are predictors of a prostate cancer of good prognosis
medicine
-
hyaluronidase improves pharmacokinetic profiles of HI-6 dichloride and HI-6 dimethansulfonate. Hyaluronidase is supposed to increase tissue permeability and diminishes discomfort caused by the intramuscular injection
medicine
-
bovine hyaluronidase is an adjuvant for infiltration anesthesia. By degrading hyaluronan in the extracellular matrix, hyaluronidase increases membrane permeability, thereby rendering tissues more permeable to injected fluids. As a consequence, hyaluronidase reduces viscosity of hyaluronan which improves tissue diffusion and the resorption rate of excess fluids. Co-administration of hyaluronidase is a potential option to enhance the effectiveness of local anesthesia, increasing the analgesic efficacy with respect to the anesthetized area per time (e.g., subcutaneous and intramuscular injections). Hyaluronidase is used in ophthalmic surgery in combination with local anesthetics for peritubular, retrotubular or sub-Tenon's anesthesia and is established in other surgical disciplines, including dermatosurgery. Injection of hyaluronidase-based fillers in aesthetic dermatology
medicine
hyaluronidase is an important enzyme for oncological care. The enzyme itself is known for rendering tissues more permeable for drug absorption (spreading effect). It is further used for defined production of hyaluronan oligosaccharides, which play crucial roles in different cellular responses. One of the main applications is tumor suppression and angiogenesis-formation of new blood vessels in tissues
EXTERNAL LINKS (specific for EC-Number 3.2.1.35)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
