5.1.3.19: chondroitin-glucuronate 5-epimerase
This is an abbreviated version!
For detailed information about chondroitin-glucuronate 5-epimerase, go to the full flat file.
Word Map on EC 5.1.3.19
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5.1.3.19
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iduronic
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glycosaminoglycans
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proteoglycans
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epimerization
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decorin
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d-glucuronic
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ehlers-danlos
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musculocontractural
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chst14
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4-o-sulfotransferase
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mceds
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idoa
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4-o-sulfated
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analysis
- 5.1.3.19
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iduronic
- glycosaminoglycans
- proteoglycans
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epimerization
- decorin
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d-glucuronic
- ehlers-danlos
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musculocontractural
- chst14
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4-o-sulfotransferase
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mceds
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idoa
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4-o-sulfated
- analysis
Reaction
Synonyms
Chondroitin D-glucuronosyl 5-epimerase, chondroitin-glucuronate C5-epimerase, dermatan sulfate epimerase, dermatan sulfate epimerase 1, dermatan sulfate epimerase 2, dermatan sulfate epimerase like, dermatan sulfate epimerase-2, dermatan sulfate epimerase-like a, dermatan sulfate epimerase-like b, Dermatan-sulfate 5-epimerase, DS epimerase 1, DS epimerase 2, DS-epi1, DS-epi2, DS-epimerase 1, DSE, DSEL, dsela, dselb, Epimerase, chondroitin glucuronate 5-, Polyglucuronate 5-epimerase, SART2
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Substrates Products
Substrates Products on EC 5.1.3.19 - chondroitin-glucuronate 5-epimerase
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REACTION DIAGRAM
Chondroitin D-glucuronate
Dermatan L-iduronate
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capsular polysaccharide from Escherichia coli K4 consists of a chondroitin backbone to which beta-fructofuranose units are linked to C-3 of the D-glucuronic acid residues. Removal of the fructose units by mild acid hydrolysis provides a substrate for the chondroitin-glucuronate 5-epimerase
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Chondroitin D-glucuronate
Dermatan L-iduronate
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C5-inversion of D-glucuronic acid to L-iduronic acid occurs on the polymer level. This transformation is greatly promoted by 4-sulfation of neighboring N-acetylgalactosamine moieties
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Chondroitin L-iduronosyl residues
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D-glucuronate
L-iduronate
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in dermatan sulfate, iduronic acid residues are either clustered together in blocks or alternating with glucuronic acid, forming hybrid structures
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D-glucuronate
L-iduronate
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DS-epi2 has epimerase activity, which involves conversion of D-glucuronic acid to L-iduronic acid, EC 5.1.3.19, but no O-sulfotransferase activity, ovcerview
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most of the L-iduronic acid residues generated by the enzyme occur singly, although some formation of two or three consecutive L-iduronic acid residue containing disaccharide units is observed
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additional information
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dermatan sulfate and chondroitin sulfate are inactive as substrates, which indicates that epimerization takes place before sulfation
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additional information
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epimerization of D-glucuronosyl residues to L-iduronosyl during biosynthesis of dermatan sulfate
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additional information
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epimerization of D-glucuronosyl residues to L-iduronosyl during biosynthesis of dermatan sulfate
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additional information
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identification of the catalytic site, and of three putative catalytic residues in DS-epimerase 1, His205, Tyr261, and His450, by tertiary structure modeling and amino acid conservation to heparinase II
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additional information
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tandem mass spectrometry analysis, based on fragment analysis of reducing-end labeled GAG oligosaccharides, of heterogeneous epimerase products, DS-epi1-catalyzed incorporation of deuterium into the oligosaccharide substrates causes a discernible shift of the isotopic pattern in the mass spectra, and generation of site-specific modification information by acid-catalyzed glycan sequencing (PRAGS). Optimal substrate binding requires an octasaccharide or longer
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