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Information on EC 4.2.2.1 - hyaluronate lyase and Organism(s) Homo sapiens and UniProt Accession Q12891
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4.2.2.1 hyaluronate lyaseIUBMB Comments
The enzyme catalyses the degradation of hyaluronan by a beta-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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Word Map
- 4.2.2.1
- streptococcus
- chondroitin
- disaccharide
- glycosaminoglycans
- agalactiae
- chondroitinase
-
enteroaggregative
- hyaluronidases
- medicine
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hyals
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hyalurolyticus
- pharmacology
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autotransporter
- degradation
- synthesis
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
hyaluronate lyase, mucinase, hylp2, hyaluronan lyase, bacterial hyaluronidase, hyaluronidase sd, ha lyase, spnhl, hylb4755, spnhyal, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucuronoglycosaminoglycan lyase
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-
-
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hyaluronidase
HYase
lyase, glucuronoglycosaminoglycan
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lyase, hyaluronate
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-
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mucinase
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spreading factor
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hyaluronidase
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HYase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
hyaluronate lyase
The enzyme catalyses the degradation of hyaluronan by a beta-elimination reaction. Also acts on chondroitin. The product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
CAS REGISTRY NUMBER
COMMENTARY
37259-53-3
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CD44
without CD44 expression, Hyal-2 exists in a granular pattern, and does not show hyaluronidase activity
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CD44
intracellular hyaluronic acid degradation is predominantly mediated by Hyal-1 after incorporation of hyaluronic acid by CD44
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
pH 5.5: about 55% of maximal activity, pH 7.5: about 40% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
acidic, somatic hyaluronidase 3 exists in two isoforms, and resides on the plasma membrane over the head and midpiece
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Hyal-2 activityis detected in the membrane fraction of cells co-expressing Hyal-2 and CD44
additional information
additional information
although Hyal-1 is active only in intracellular space in vivo, a certain amount of the enzyme is secreted to extracellular space. This extracellular Hyal-1 is incorporated by cells and such uptake of Hyal-1 is, in part, involved in the intracellular degradation of hyaluronic acid
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additional information
although Hyal-1 is active only in intracellular space in vivo, a certain amount of the enzyme is secreted to extracellular space. This extracellular Hyal-1 is incorporated by cells and such uptake of Hyal-1 is, in part, involved in the intracellular degradation of hyaluronic acid
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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in general, neutral-active or reproductive hyaluronidases, i.e. hyases, exemplified by sperm adhesion molecule 1, SPAM1, are responsible for hyaluronan digestion in the egg vestments and for sperm-zona binding. Presence of HYAL3 in human sperm where it contributes to hyase activity at pH 3, 4 and 7 as well as to cumulus penetration and the induction of the acrosome reaction
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Hyal-1/293 and Hyal-1/CD44/293 are stably overexpressing Hyal-1. The expressed Hyal-1 is not only accumulated intracellularly, but is also secreted to the outside of the cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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as compared to bovine-derived enzyme cumulase is safe and effective in an intracytoplasmic sperm injection treatment program and can provide comparable if not improved parameters, including fertilization and embryo developmental rates
medicine
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antitumor activity and overall survival of mice bearing highly aggessive tumors are significantly improved by codelivery of oncolytic adenovirus and hyaluronidase when compared with either of the monotherapy-treated groups, and it may prove to be a potent and novel approach to treating patients with cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, T.H.; Elliott, T.; Colturato, L.F.; Straub, R.J.; Mitchell-Leef, D.; Nagy, Z.P.
Comparison of bovine- and recombinant human-derived hyaluronidase with regard to fertilization rates and embryo morphology in a sibling oocyte model: a prospective, blinded, randomized study
Fertil. Steril.
85
1544-1546
2006
Bos taurus, Homo sapiens
Harada, H.; Takahashi, M.
CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2
J. Biol. Chem.
282
5597-5607
2007
Homo sapiens (Q12794), Homo sapiens (Q12891)
Ganesh, S.; Gonzalez-Edick, M.; Gibbons, D.; Van Roey, M.; Jooss, K.
Intratumoral coadministration of hyaluronidase enzyme and oncolytic adenoviruses enhances virus potency in metastatic tumor models
Clin. Cancer Res.
14
3933-3941
2008
Homo sapiens
Reese, K.L.; Aravindan, R.G.; Griffiths, G.S.; Shao, M.; Wang, Y.; Galileo, D.S.; Atmuri, V.; Triggs-Raine, B.L.; Martin-Deleon, P.A.
Acidic hyaluronidase activity is present in mouse sperm and is reduced in the absence of SPAM1: evidence for a role for hyaluronidase 3 in mouse and human sperm
Mol. Reprod. Dev.
77
759-772
2010
Homo sapiens, Mus musculus
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