MersV1, PubMed, Curation, bibRecord, 002159

Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.

Identifieur interne : 002159 ( PubMed/Curation ); précédent : 002158; suivant : 002160

Chondroitin 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.

RBID : pubmed:17902054

Descripteurs français

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

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<author><name 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>
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<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>
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<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>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Disaccharides</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chondroitin Lyases</term>
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<term>Polymers</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chondroitine lyases</term>
<term>Escherichia coli</term>
<term>Fructose</term>
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<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>
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<term>Chromatographie en phase liquide à haute performance</term>
<term>Diholoside</term>
<term>Données de séquences moléculaires</term>
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<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>
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<Abstract><AbstractText>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.</AbstractText>
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Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.

Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.

Source :

Descripteurs français

English descriptors

Abstract

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