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EC Tree
IUBMB Comments 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.
The taxonomic range for the selected organisms is: Apis mellifera The enzyme appears in selected viruses and cellular organisms
Synonyms
chondroitinase, testicular hyaluronidase, hyal1, hyal2, ph-20, hyal-1, rhuph20, spreading factor, hyal-2, mgea5,
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hyaluronoglucosidase
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Sperm surface protein PH-20
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hyaluronidase
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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
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
reaction mechanism and three-dimensional structure, catalytic residue is Glu113, substrate positioning residues, overview
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hydrolysis of O-glycosyl bond
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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.
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4-S-chondroitin sulfate + H2O
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6-S-chondroitin sulfate + H2O
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the enzyme is capable of degrading chondroitin sulfate C at a rate of around 40% compared to its hyaluronidase activity
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chondroitin B sulfate + H2O
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very little hydrolase activity towards chondroitin sulfate B (dermatan sulfate)
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chondroitin sulfate A + H2O
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chondroitin sulfate B + H2O
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very little hydrolase activity
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chondroitin sulfate C + H2O
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hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
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hyaluronan + H2O
hyaluronan oligomers
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hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
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hyaluronic acid + H2O
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additional information
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the enzyme is a major allergen of bee venom which can induce serious, occasionally fatal, systemic IgE-mediated anaphylactic reactions in humans
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hyaluronic acid + H2O
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hyaluronic acid + H2O
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from rooster comb
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hyaluronan + H2O
hyaluronan oligomers
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hyaluronate + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
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hyaluronic acid + H2O
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additional information
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the enzyme is a major allergen of bee venom which can induce serious, occasionally fatal, systemic IgE-mediated anaphylactic reactions in humans
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glutathione
non-competitive
N-acetyl-L-cysteine
non-competitive
beta1,4-galacto-oligosaccharides
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partially sulfated and non-sulfated forms, especially tri-, tetra-, and pentasaccharides
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partially sulfated neomycin
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the non-sulfated neomycin is not inhibitory
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partially sulfated planteose
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the non-sulfated planteose is not inhibitory, IC50 is 0.008 mM
partially sulfated verbascose
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2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.040 mM and 0.003 mM
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sulfated hydroquinone galactoside
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IC50 is 0.006 mM
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0.008
partially sulfated planteose
Apis mellifera
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the non-sulfated planteose is not inhibitory, IC50 is 0.008 mM
0.04
partially sulfated verbascose
Apis mellifera
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2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.040 mM and 0.003 mM
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0.006
sulfated hydroquinone galactoside
Apis mellifera
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IC50 is 0.006 mM
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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
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3 - 8
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3 - 8
native and the recombinant enzyme are active at extreme conditions
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4 - 90
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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
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UniProt
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bee
UniProt
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expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein
UniProt
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hyaluronoglucosaminidase precursor
UniProt
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venom
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venom
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HUGA_APIME
382
1
44260
Swiss-Prot
Secretory Pathway (Reliability: 1 )
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additional information
three-dimensional structure analysis
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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
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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
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3 - 8
native and recombinant enzyme exhibit activity
682687
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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
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by ion exchange chromatography at pH 5.0
HiTrap HP SP column chromatography
recombinant His-tagged enzyme
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DNA and amino acid sequence analysis, expression as active C-terminally His-tagged enzyme in insect cells via baculovirus infection
expressed in Pichia pastoris strain GS115
expression in Pichia pastoris GS115, expression vector pPIC9, together with human serum albumin, expression in Escherichia coli BL21 DE3, vector pMW172, fusion protein
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medicine
enzyme is the target for immunotherapy of allergen reaction
medicine
this recombinant hyaluronidase can be applied for biochemical or medical purposes
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Markovic-Housley, Z.; Miglierini, G.; Soldatova, L.; Rizkallah, P.J.; Muller, U.; Schirmer, T.
Crystal structure of hyaluronidase, a major allergen of bee venom
Structure
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1025-1035
2000
Apis mellifera (Q08169)
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Stern, R.; Jedrzejas, M.J.
Hyaluronidases: their genomics, structures, and mechanisms of action
Chem. Rev.
106
818-839
2006
Bos taurus, Homo sapiens, Mus musculus, Apis mellifera (Q08169)
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Salmen, S.; Hoechstetter, J.; Kaesbauer, C.; Paper, D.H.; Bernhardt, G.; Buschauer, A.
Sulphated oligosaccharides as inhibitors of hyaluronidases from bovine testis, bee venom and Streptococcus agalactiae
Planta Med.
71
727-732
2005
Apis mellifera, Bos taurus
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Reitinger, S.; Boroviak, T.; Laschober, G.T.; Fehrer, C.; Muellegger, J.; Lindner, H.; Lepperdinger, G.
High-yield recombinant expression of the extremophile enzyme, bee hyaluronidase in Pichia pastoris
Protein Expr. Purif.
57
226-233
2008
synthetic construct (EU152302), Apis mellifera (Q08169)
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Sunitha, K.; Suresh, P.; Santhosh, M.S.; Hemshekhar, M.; Thushara, R.M.; Marathe, G.K.; Thirunavukkarasu, C.; Kemparaju, K.; Kumar, M.S.; Girish, K.S.
Inhibition of hyaluronidase by N-acetyl cysteine and glutathione: role of thiol group in hyaluronan protection
Int. J. Biol. Macromol.
55
39-46
2013
Bos taurus, Echis carinatus, Homo sapiens, Apis mellifera (Q08169)
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