4.2.2.1: hyaluronate lyase
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For detailed information about hyaluronate lyase, go to the full flat file.
Word Map on EC 4.2.2.1
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4.2.2.1
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streptococcus
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chondroitin
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disaccharide
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glycosaminoglycans
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agalactiae
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chondroitinase
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enteroaggregative
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hyaluronidases
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medicine
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hyals
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hyalurolyticus
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pharmacology
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autotransporter
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degradation
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synthesis
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analysis
- 4.2.2.1
- streptococcus
- chondroitin
- disaccharide
- glycosaminoglycans
- agalactiae
- chondroitinase
-
enteroaggregative
- hyaluronidases
- medicine
-
hyals
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hyalurolyticus
- pharmacology
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autotransporter
- degradation
- synthesis
- analysis
Reaction
Synonyms
acidic hyase, bacterial HAse, bacterial hyaluronidase, bacterial spreading factor, bacteriophage-associated hyaluronate lyase, Cumulase, EC 4.2.99.1, GBS HA lyase, GBS hyase, glucuronoglycosaminoglycan lyase, h-SD, h-SH, HA lyase, HL, Hyal, Hyal-1, Hyal-2, HYAL1, Hyal2, HYAL3, hyaluronan lyase, hyaluronate lyase, hyaluronate lyase HylA, hyaluronate lyase HylP2, hyaluronidase, hyaluronidase 3, hyaluronidase SD, hyaluronidase SH, hyaluronidase-1, hyaluronidase-2, hyaluronoglucosaminidase-1, hyaluronoglucosaminidase-2, HYase, HylA7, hylB, hylB4755, HylP, Hylp2, LUCA-1, LUCA-2, lyase, glucuronoglycosaminoglycan, lyase, hyaluronate, More, mucinase, protein SEQ2045, rHuPH20, SagHL, SagHyal, spnHL, SpnHyal, spreading factor, SP_0314
ECTree
4.2.2.1 hyaluronate lyaseAdvanced search results
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Application on EC 4.2.2.1 - hyaluronate lyase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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application for the specific determination of hyaluronan concentration
degradation
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use of biocompatible magnetic macroporous bead cellulose functionalised with hyaluronan lyase for controlled fragmetation of hyaluronan. Immobilisation of enzyme on macroporous bead cellulose via reductive amination or macroporous bead cellulose with fixed iminodiacetic acid via a His8-tag has minimal impact on its catalytic activity. The carrier with with fixed iminodiacetic acid shows excellent operational and storage stability, and both carriers enable reproducible time-controlled fragmentation of highly viscous high moleculare weight hyaluronan solutions, yielding hyaluronan fragments of appropriate molecular weight
medicine
pharmacology
synthesis
Streptomyces hyalurolyticus
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enzymatic production of fully O-sulfated oligosaccharides by large scale depolymerization of hyaluronan polymer
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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safe and effective in an intracytoplasmic sperm injection treatment program
medicine
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transient perfusion induces acute hypoxia and may limit the radiotherapy response and induce drug resistance. Hyaluronidase improves perfusion in human osteosarcoma xenografts grown orthotopically and in dorsal skinfold chambers
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
medicine
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distribution of hyaluronate lyase-producing Streptococcus pneumoniae among invasive, noninvasive and carriage isolates from patients and carriers. A total of 100 isolates from various clinical samples all possessed the Hyl gene. Ninety-six isolates including 34 carriage isolates were positive for production of hyaluronate lyase. Four hyaluronate lyase-negative isolates are from blood (2 isolates) and sputum (2 isolates). No significant association is detected among hyaluronate lyase production and bacterial characteristics except for colonial morphology
medicine
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Streptococcus suis hyaluronate lyase does not represent a critical virulence factor in its active form. Exogenous hyaluronic acid appears to modulate several virulence determinants of the bacterium, in addition to promote inflammation
pharmacology
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enzyme can be used for production of pharmaceuticals as an alternative to bovine testicular hyaluronidase, BTH, because the production of BTH is stopped due to risk of BSE
pharmacology
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enzyme is a target for development of antimicrobial agents
pharmacology
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the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy
pharmacology
the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy
pharmacology
in vitro microbial hyaluronate lyase is able to split the hyaluronic acid in atherosclerotic plaques under release of calcium deposits and reduces in vivo the development of atherosclerotic lesions in hyperlipidaemic rabbits
