4.2.2.1: hyaluronate lyase
This is an abbreviated version!
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
results (
results (Inhibitors
Inhibitors on EC 4.2.2.1 - hyaluronate lyase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(25S)-(+)-12alpha-hydroxy-3alpha-methylcarboxyacetate-24-methyllanosta-8,24(31)-diene-26-oic acid
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from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0035 mM
(2E)-1-furan-2-yl-3-(4-nitrophenyl)prop-2-en-1-one
IC50 at enzyme optimum pH 5.0 is 0.31 mM, and 0.16 mM at physiological pH 7.4
(E)-3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)prop-2-en-1-one
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36% inhibition
1,3-diacetyl-benzimidazole-2-thione
IC50 at enzyme optimum pH 5.0 is 0.16 mM, and 0.005 mM at physiological pH 7.4
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
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1-decyl-2-(4-sulfamoyloxyphenyl)-1H-indol-6-yl sulfamate
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inhibitor fits in the enzymatic active site via interactions resembling the binding mode of the natural hyaluronan substrate
2,2'-benzene-1,4-diyldiacetic acid
IC50 at enzyme optimum pH 5.0 is 0.37 mM, and 0.90 mM at physiological pH 7.4
3alpha-acetylpolyporenic acid A
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from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.040 mM
beta1,4-galacto-oligosaccharides
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partially sulfated and non-sulfated forms, IC50 values
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guanidine hydrochloride
strong inhibition, unfolding within 1 h
L-ascorbate
noncompetitive inhibition, inhibition kinetics, overview. Residues involved in the binding of L-ascorbate are confined to HylP135-308
lanostanoid
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from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
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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 0.015 mM
partially sulfated verbascose
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2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.030 mM and 0.001 mM
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polyporenic acid
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from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
Ca2+
slight inhibition by 30% unfolding of the enzyme by ion binding
Ca2+
interacts with the collagenous Gly-X-Y motif of the enzyme, activates up to 20 mM, but inhibits at higher concentrations, inactivation above 50 mM
L-ascorbic acid
i.e. vitamin C, reversible, competitive, one molecule binds to the active site of all 3 catalytic positions, interacts with enzyme residues R243, N290, W292, Y408, R462, R466, and N580, inhibits the invasion and spreading of the bacterium in tissues in vivo
Mg2+
slight inhibition by 30% unfolding of the enzyme by ion binding
additional information
structure-based design of bacterial hyaluronan lyase inhibitors, combinatorial chemistry database and crystal structure, method, overview
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additional information
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development of structure-based 1-acylated benzimidazole-2-thiones and benzoxazole-2-thiones inhibitors, using the crystal structure of Streptococcus pneumoniae Hyal, overview. Except for N-(3-phenylpropionyl)benzoxazole-2-thione, other N-acylated benzimidazoles and benzoxazoles are just as active at pH 7.4, but not at pH 5.0. The compounds show a binding mode characterized by interactions with residues in the catalytic site and with a hydrophobic patch, overview. No inhibition by 3-hexanoylbenzo[d]oxazol-2(3H)-one. Inhibition at pH 5.0, structure-activity relationships, overview
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additional information
not inhibited by ascorbic acid at concentration up to 20 mM
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additional information
no inhibition and conformational change induced by NaCl
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additional information
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no inhibition and conformational change induced by NaCl
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additional information
IC50 for 1,3-diacetylbenzimidazole-2-thione is above 0.1 mM
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additional information
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IC50 for 1,3-diacetylbenzimidazole-2-thione is above 0.1 mM
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additional information
Streptomyces hyalurolyticus
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poor inhibitors are alpha-D-glucoheptonic-gamma-lactone, L-gulonic-gamma-lactone, D-ribonic-gamma-lactone, and D-gluconic-gamma-lactone
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