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dc.contributor.advisorKelly, Vincent
dc.contributor.authorHayes, Patti
dc.date.accessioned2019-11-06T14:58:03Z
dc.date.available2019-11-06T14:58:03Z
dc.date.issued2011
dc.identifier.citationPatti Hayes, 'Identification of the components of the eukaryotic queuine transglycosylase complex and the effect of its substrate queuine on metabolism', [thesis], Trinity College (Dublin, Ireland). School of Biochemistry and Immunology, 2011, pp 169
dc.identifier.otherTHESIS 9083
dc.description.abstractQueuine is a 7-deazaguanine derivative of guanine, which replaces guanine in position 34 of the anticodon loop of the transfer RNA for the amino acids, asparagine, aspartic acid, histidine and tyrosine. This base or related analogues are found within eukaryotes, eubacteria and archaebacteria. The physiological relevance of queuine has yet to be determined. The enzyme responsible for the base-exchange reaction is called tRNA guanine transglycosylase (TGT). While the eubacterial and archael forms of TGT have been well characterized, very little is known about the eukaryotic enzyme.
dc.format1 volume
dc.language.isoen
dc.publisherTrinity College (Dublin, Ireland). School of Biochemistry and Immunology
dc.relation.isversionofhttp://stella.catalogue.tcd.ie/iii/encore/record/C__Rb14628654
dc.subjectBiochemistry, Ph.D.
dc.subjectPh.D. Trinity College Dublin.
dc.titleIdentification of the components of the eukaryotic queuine transglycosylase complex and the effect of its substrate queuine on metabolism
dc.typethesis
dc.type.supercollectionthesis_dissertations
dc.type.supercollectionrefereed_publications
dc.type.qualificationlevelDoctoral
dc.type.qualificationnameDoctor of Philosophy (Ph.D.)
dc.rights.ecaccessrightsopenAccess
dc.format.extentpaginationpp 169
dc.description.noteTARA (Trinity’s Access to Research Archive) has a robust takedown policy. Please contact us if you have any concerns: rssadmin@tcd.ie
dc.identifier.urihttp://hdl.handle.net/2262/90213


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