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dc.contributor.authorMalandrinos, G.en
dc.contributor.authorLouloudi, M.en
dc.contributor.authorHadjiliadis, N.en
dc.date.accessioned2015-11-24T16:51:34Z-
dc.date.available2015-11-24T16:51:34Z-
dc.identifier.issn0306-0012-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9752-
dc.rightsDefault Licence-
dc.subject2-(alpha-hydroxyethyl)thiamin pyrophosphate hetppen
dc.subjectyeast pyruvate decarboxylaseen
dc.subjectsite-directed mutagenesisen
dc.subjectacid-base groupsen
dc.subjectasn-lys-ileen
dc.subjectcrystal-structureen
dc.subjectsaccharomyces-cerevisiaeen
dc.subjectangstrom resolutionen
dc.subjectmetal-complexesen
dc.subjectbenzoylformate decarboxylaseen
dc.titleThiamine models and perspectives on the mechanism of action of thiamine-dependent enzymesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1039/B514511m-
heal.identifier.secondary<Go to ISI>://000239211500002-
heal.identifier.secondaryhttp://pubs.rsc.org/en/content/articlepdf/2006/cs/b514511m-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2006-
heal.abstractThiamine dependent enzymes catalyze ligase and lyase reactions near a carbonyl moiety. Chemical models for these reactions serve as useful tools to substantiate a detailed mechanism of action. This tutorial review covers all such studies performed thus far, emphasizing the role of each part around the active site and the conformation of the cofactor during catalysis.en
heal.publisherRoyal Society of Chemistryen
heal.journalNameChemical Society Reviewsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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