{"refrec":{"BRefID":67411,"RR":"<b>Barbeyron, T.; Flament, D.; Michel, G.; Potin, Ph.; Kloareg, B.</b> (2001). The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution. <i>Cah. Biol. Mar. 42(1-2)</i>: 169-183","BEntID":328852,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Cah. Biol. Mar. 42(1-2)</i>: 169-183","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Barbeyron, T.; Flament, D.; Michel, G.; Potin, Ph.; Kloareg, B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Barbeyron, T. <i>et al.</i>","Englishabstract":"The carrageenans and agars are major cell-wall polysaccharides from red algae. These sulphated galactans are degraded by enzymes, called carrageenases and agarases that display strict substrate specifities and recognize the pattern of galactan sulphation. From a set of various marine bacteria enzymes, we have investigated the influence of ester-sulphate groups, of D/L isomery and of linkage anomery on the structure-function relationships of the specific galactan hydrolases that degrade sulphated polysaccharides. With this aim, we have cloned a representative set of sulphated-galactan hydrolase genes. The sequence analysis methods indicate that the beta-agarases and kappa- carrageenases display secondary structure similarities with members of family 16 of glycoside hydrolases. In contrast, the L-carrageenases have no structural relationships with the family-16 beta-agarases and kappa-carrageenases and they constitute a novel structural family of glycan hydrolases. As a preliminary step towards the functional analysis of these two structural families, we have overexpressed the L- and kappa-carrageenase genes in <i>Escherichia coli</i> and crystals from these enzymes have been obtained. Finally, an alpha-agarase, the only one galactanase known to cleave the alpha-1,3 linkage in agarose has no similarity with other glycoside hydrolases or proteins and display some interesting characteristics. To date, this enzyme is an unclassified glycoside hydrolase.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"The sulphated-galactan hydrolases, agarases and carrageenases: structural biology and molecular evolution","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2001,"MonPub":null,"DateUpdate":"2021-02-16","DateCreate":"2004-10-21","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000168120500016","VABBcode":null,"OpenAcc":1},"refs":null,"anarec":{"AnaID":67411,"PubliDate":2001,"Pagination":"169-183","XtraPublOfAnaID":null,"ISBN":null,"Volume":"42","Issue":"1-2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42348,"SerRR":"Cahiers de Biologie Marine. Station Biologique de Roscoff: Paris.  ISSN 0007-9723; e-ISSN 2262-3094","StandardTitleSer":"Cahiers de Biologie Marine","ISSN":"0007-9723","AbbrevSer":"Cah. Biol. Mar.","StandardTitleMon":null,"StartPage":169,"Pages":15,"ToPubliDate":null,"BRefBibLvlCode":"S","SerNotes":"Open access for all articles older than 2 years."},"monrec":null,"serrec":null,"relations":[{"YBRefID":67326,"RefStrFull":"(2001). Proceedings of the International Workshop \"Current approaches in basic and applied phycology\". <i>Cahiers de Biologie Marine</i>, 42(1-2). 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