{"refrec":{"BRefID":221272,"RR":"<b>Loumaye, E.; Andersen, A.C.; Clippe, A.; Degand, H.; Dubuisson, M.; Zal, F.; Morsomme, P.; Rees, J.F.; Knoops, B.</b> (2008). Cloning and characterization of <i>Arenicola marina</i> peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins. <i>Free Radic. Biol. Med. 45(4)</i>: 482-493. <a href=\"http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033\" target=\"_blank\">http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033</a>","BEntID":213002,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Free Radic. Biol. Med. 45(4)</i>: 482-493. <a href=\"http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033\" target=\"_blank\">http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Loumaye, E.; Andersen, A.C.; Clippe, A.; Degand, H.; Dubuisson, M.; Zal, F.; Morsomme, P.; Rees, J.F.; Knoops, B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Loumaye, E. <i>et al.</i>","Englishabstract":"Peroxiredoxins (PRDXs) are a superfamily of thiol-dependent peroxidases found in all phyla. PRDXs are mechanistically divided into three subfamilies, namely typical 2-Cys, atypical 2-Cys, and 1-Cys PRDXs. To reduce peroxides, the N-terminal peroxidatic Cys of PRDXs is first oxidized into sulfenic acid. This intermediate is reduced by forming a disulfide bond either with a resolving Cys of another monomeric entity (typical 2-Cys) or of the same molecule (atypical 2-Cys). In 1-Cys PRDXs, the resolving Cys is missing and the sulfenic acid of the peroxidatic Cys is reduced by a heterologous thiol-containing reductant. In search of a homolog of human 1-Cys PRDX6 in <em>Arenicola marina</em>, an annelid worm living in intertidal sediments, we have cloned and characterized a PRDX exhibiting high sequence homology with its mammalian counterpart. However, <em>A. marina</em> PRDX6 possesses five Cys among which two Cys function as peroxidatic and resolving Cys of typical 2-Cys PRDXs. Thus, <em>A. marina</em> PRDX6 belongs to a transient group exhibiting sequence homologies with mammalian 1-Cys PRDX6 but must be mechanistically classified into typical 2-Cys PRDXs. Moreover, PRDX6 is highly expressed in tissues directly exposed to the external environment, suggesting that this PRDX may be of particular importance for protection against exogenous oxidative attacks.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Cloning and characterization of <i>Arenicola marina</i> peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-21 01:31:59.139688","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"    Annelid;     Arenicola marina;     Peroxidase;     Peroxiredoxin;     Antioxidant","OtherDescriptors":null,"Notes":null,"AnaPub":2008,"MonPub":null,"DateUpdate":"2015-11-04","DateCreate":"2012-12-13","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000258614700014","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.freeradbiomed.2008.04.033"},"refs":null,"anarec":{"AnaID":221272,"PubliDate":2008,"Pagination":"482-493","XtraPublOfAnaID":null,"ISBN":null,"Volume":"45","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":220679,"SerRR":"Free Radical Biology and Medicine. 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