4.2.2.5: chondroitin AC lyase
This is an abbreviated version!
For detailed information about chondroitin AC lyase, go to the full flat file.
Word Map on EC 4.2.2.5
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4.2.2.5
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glycosaminoglycans
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proteoglycans
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dermatan
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heparan
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hyaluronic
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hyaluronidase
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glucuronic
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heparinum
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flavobacterium
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heparitinase
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6-sulfate
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lyases
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iduronic
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4-sulphate
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glca
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cetylpyridinium
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hexasaccharide
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monosulfated
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cuprolinic
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3hglucosamine
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galactosaminoglycans
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aurescens
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undersulfated
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oversulfated
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keratanase
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35ssulfate
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analysis
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medicine
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synthesis
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trisulfated
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blue-positive
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chondroitin-4-sulfate
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food industry
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cupromeronic
- 4.2.2.5
- glycosaminoglycans
- proteoglycans
- dermatan
- heparan
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hyaluronic
- hyaluronidase
-
glucuronic
- heparinum
- flavobacterium
- heparitinase
- 6-sulfate
- lyases
-
iduronic
-
4-sulphate
-
glca
-
cetylpyridinium
- hexasaccharide
-
monosulfated
-
cuprolinic
-
3hglucosamine
- galactosaminoglycans
- aurescens
-
undersulfated
-
oversulfated
- keratanase
-
35ssulfate
- analysis
- medicine
- synthesis
-
trisulfated
-
blue-positive
- chondroitin-4-sulfate
- food industry
-
cupromeronic
Reaction
= n-1 4-deoxy-beta-D-gluc-4-enuronosyl-1,4-beta-D-hexosylamine +
Synonyms
A-Chase, AC I lyase, c-ACI, c-ACII, ChnAC, chon-AC-lyase, ChonAC, chondroitin AC eliminase, chondroitin AC I lyase, Chondroitin AC lyase, chondroitin ACII lyase, chondroitin lyase AC, chondroitin sulfate lyase, chondroitinase, chondroitinase AC, chondroitinase ACI, chondroitinase ACII, ChSase-AC, EC 4.2.99.6, F-Chase, lyase, chondroitin AC, Pedsa_3808, PL8A
ECTree
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Crystallization
Crystallization on EC 4.2.2.5 - chondroitin AC lyase
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native enzyme alone and in complex with substrates chondroitin 4-sulfate tetrasaccharide, and hyaluronan tetrasaccharide, hanging drop vapour diffusion method, 0.002 ml protein solution: 10 mg/ml protein, + 0.002 ml reservoir solution: 23% w/v PEG 8000, 0.1 M sodium phosphate, pH 6.4, 0.4 M ammonium acetate, 10% v/v glycerol, suspended over 1 ml reservoir solution, a few days, larger crystals by macroseeding, X-ray diffraction structure determination and analysis of the enzyme-substrate complexes at 1.25-1.9 A high resolution
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complexes of the wild-type enzyme with dermatan sulfate hexasaccharide, tetrasaccharide, and hyaluronic acid tetrasaccharide, and mutant Y234F enzyme in complex with chondroitin sulfate tetrasaccharide, hanging drop vapour diffusion method, equal volumes, 0.005 ml, of protein and reservoir solution are suspended over 1 ml reservoir solution containing 15% w/v PEG 3350, 0.4 M sodium acetate, 0.1 M HEPES, pH 7.5, at room temperature of about 20°C, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
modeling of structure. Residues N153, W105, H203, Y208, Y212, R266 and E349 are involved in catalysis