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dc.contributor.authorSternicki, Louise M
dc.contributor.authorWegener, Kate L
dc.contributor.authorBruning, John B
dc.contributor.authorBooker, Grant W
dc.contributor.authorPolyak, Steven W
dc.date.accessioned2021-04-22T04:09:15Z
dc.date.available2021-04-22T04:09:15Z
dc.date.issued2017
dc.identifier.issn0968-0004
dc.identifier.doi10.1016/j.tibs.2017.02.001
dc.identifier.urihttp://hdl.handle.net/10072/403894
dc.description.abstractProtein biotinylation is a key post-translational modification found throughout the living world. The covalent attachment of a biotin cofactor onto specific metabolic enzymes is essential for their activity. This modification is distinctive, in that it is carried out by a single enzyme: biotin protein ligase (BPL), an enzyme that is able to biotinylate multiple target substrates without aberrant-off target biotinylation. BPL achieves this target selectivity by recognizing a sequence motif in the context of a highly conserved tertiary structure. One structural class of BPLs has developed an additional ‘substrate verification’ mechanism to further enable appropriate protein selection. This is crucial for the precise and selective biotinylation required for efficient biotin management, especially in organisms that are auxotrophic for biotin.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofpagefrom383
dc.relation.ispartofpageto394
dc.relation.ispartofissue5
dc.relation.ispartofjournalTrends in Biochemical Sciences
dc.relation.ispartofvolume42
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode32
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsBiochemistry & Molecular Biology
dc.subject.keywordsHOLOCARBOXYLASE SYNTHETASE DEFICIENCY
dc.subject.keywordsACETYL-COA CARBOXYLASE
dc.titleMechanisms Governing Precise Protein Biotinylation
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationSternicki, LM; Wegener, KL; Bruning, JB; Booker, GW; Polyak, SW, Mechanisms Governing Precise Protein Biotinylation, Trends in Biochemical Sciences, 2017, 42 (5), pp. 383-394
dcterms.dateAccepted2017-02-03
dc.date.updated2021-04-22T04:07:41Z
gro.hasfulltextNo Full Text
gro.griffith.authorSternicki, Louise


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