Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.
Identifieur interne : 002A01 ( Main/Exploration ); précédent : 002A00; suivant : 002A02Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.
Auteurs : Nicola Volpi [Italie]Source :
- Glycoconjugate journal [ 0282-0080 ] ; 2008.
Descripteurs français
- KwdFr :
- Chondroitine lyases (métabolisme), Chromatographie d'échange d'ions, Chromatographie en phase liquide à haute performance, Diholoside (), Diholoside (analyse), Données de séquences moléculaires, Escherichia coli (métabolisme), Fructose (métabolisme), Polymères (métabolisme), Spectrométrie de masse ESI, Séquence glucidique.
- MESH :
English descriptors
- KwdEn :
- Carbohydrate Sequence, Chondroitin Lyases (metabolism), Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Disaccharides (analysis), Disaccharides (chemistry), Escherichia coli (metabolism), Fructose (metabolism), Molecular Sequence Data, Polymers (metabolism), Spectrometry, Mass, Electrospray Ionization.
- MESH :
- chemical , analysis : Disaccharides.
- chemical , chemistry : Disaccharides.
- chemical , metabolism : Chondroitin Lyases, Fructose, Polymers.
- metabolism : Escherichia coli.
- Carbohydrate Sequence, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Molecular Sequence Data, Spectrometry, Mass, Electrospray Ionization.
Abstract
Chondroitin C lyase was demonstrated to be unable to act on fructosylated sequences inside a partially fructosylated polysaccharide having the chondroitin backbone structure, the Escherichia coli K4 polymer, using different analytical approaches. Chondroitin C lyase produced various unsaturated oligosaccharides by acting on an approximately 27%-fructosylated K4 polymer. The online HPLC-ESI-MS approach showed the disaccharide nature of the main species produced by chondroitinase C as DeltaHexA-GalNAc. Furthermore, the non-digested sequences inside the K4 polymer were demonstrated to be oligosaccharides bearing a fructose for each glucuronic acid unit. In fact, unsaturated fully fructosylated oligomers, from tetrasaccharide to decasaccharide (DeltaHexA(Fru)-GalNAc-[GlcA(Fru)-GalNAc](n) with n between 1 and 4), at decreasing percentages, were produced by the enzyme. These results clearly indicate that chondroitinase C cleaved the innermost glucuronic acid-N-acetylgalactosamine linkage without affecting the 1,4 glycosidic linkage between fructosylated glucuronic acid and N-acetylgalactosamine residues, confirming that the 3-O-fructosylation of the GlcA residue renders the polysaccharide resistant to the enzyme action. This novel specific activity of chondroitinase C was also useful for the production of discrete microgram amounts of fully fructosylated oligomers, from 4- to 10-mers, from E. coli K4 for possible further studies and applications.
DOI: 10.1007/s10719-007-9074-8
PubMed: 17902054
Affiliations:
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Le document en format XML
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sortKey="Volpi, Nicola" sort="Volpi, Nicola" uniqKey="Volpi N" first="Nicola" last="Volpi">Nicola Volpi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biologia Animale, University of Modena and Reggio Emilia, Modena, Italy. volpi@unimo.it</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biologia Animale, University of Modena and Reggio Emilia, Modena</wicri:regionArea><wicri:noRegion>Modena</wicri:noRegion></affiliation></author></analytic><series><title level="j">Glycoconjugate journal</title><idno type="ISSN">0282-0080</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carbohydrate Sequence</term><term>Chondroitin Lyases (metabolism)</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Ion Exchange</term><term>Disaccharides (analysis)</term><term>Disaccharides (chemistry)</term><term>Escherichia coli (metabolism)</term><term>Fructose (metabolism)</term><term>Molecular Sequence Data</term><term>Polymers (metabolism)</term><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chondroitine lyases (métabolisme)</term><term>Chromatographie d'échange d'ions</term><term>Chromatographie en phase liquide à haute performance</term><term>Diholoside ()</term><term>Diholoside (analyse)</term><term>Données de séquences moléculaires</term><term>Escherichia coli (métabolisme)</term><term>Fructose (métabolisme)</term><term>Polymères (métabolisme)</term><term>Spectrométrie de masse ESI</term><term>Séquence glucidique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Disaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disaccharides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chondroitin Lyases</term><term>Fructose</term><term>Polymers</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Diholoside</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chondroitine lyases</term><term>Escherichia coli</term><term>Fructose</term><term>Polymères</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Ion Exchange</term><term>Molecular Sequence Data</term><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term><term>Chromatographie en phase liquide à haute performance</term><term>Diholoside</term><term>Données de séquences moléculaires</term><term>Spectrométrie de masse ESI</term><term>Séquence glucidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chondroitin C lyase was demonstrated to be unable to act on fructosylated sequences inside a partially fructosylated polysaccharide having the chondroitin backbone structure, the Escherichia coli K4 polymer, using different analytical approaches. Chondroitin C lyase produced various unsaturated oligosaccharides by acting on an approximately 27%-fructosylated K4 polymer. The online HPLC-ESI-MS approach showed the disaccharide nature of the main species produced by chondroitinase C as DeltaHexA-GalNAc. Furthermore, the non-digested sequences inside the K4 polymer were demonstrated to be oligosaccharides bearing a fructose for each glucuronic acid unit. In fact, unsaturated fully fructosylated oligomers, from tetrasaccharide to decasaccharide (DeltaHexA(Fru)-GalNAc-[GlcA(Fru)-GalNAc](n) with n between 1 and 4), at decreasing percentages, were produced by the enzyme. These results clearly indicate that chondroitinase C cleaved the innermost glucuronic acid-N-acetylgalactosamine linkage without affecting the 1,4 glycosidic linkage between fructosylated glucuronic acid and N-acetylgalactosamine residues, confirming that the 3-O-fructosylation of the GlcA residue renders the polysaccharide resistant to the enzyme action. This novel specific activity of chondroitinase C was also useful for the production of discrete microgram amounts of fully fructosylated oligomers, from 4- to 10-mers, from E. coli K4 for possible further studies and applications.</div></front></TEI><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Volpi, Nicola" sort="Volpi, Nicola" uniqKey="Volpi N" first="Nicola" last="Volpi">Nicola Volpi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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