Document Detail


Chondroitin C lyase [4.2.2.] is unable to cleave fructosylated sequences inside the partially fructosylated Escherichia coli K4 polymer.
MedLine Citation:
PMID:  17902054     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Nicola Volpi
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Publication Detail:
Type:  Journal Article     Date:  2007-09-28
Journal Detail:
Title:  Glycoconjugate journal     Volume:  25     ISSN:  0282-0080     ISO Abbreviation:  Glycoconj. J.     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-05-28     Completed Date:  2009-01-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8603310     Medline TA:  Glycoconj J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  451-7     Citation Subset:  IM    
Affiliation:
Department of Biologia Animale, University of Modena and Reggio Emilia, Modena, Italy. volpi@unimo.it
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MeSH Terms
Descriptor/Qualifier:
Carbohydrate Sequence
Chondroitin Lyases / metabolism*
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Disaccharides / analysis,  chemistry
Escherichia coli / metabolism*
Fructose / metabolism*
Molecular Sequence Data
Polymers / metabolism*
Spectrometry, Mass, Electrospray Ionization
Chemical
Reg. No./Substance:
0/Disaccharides; 0/Polymers; 30237-26-4/Fructose; EC 4.2.2.-/Chondroitin Lyases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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