dc.contributor.author | Sternicki, Louise M | |
dc.contributor.author | Wegener, Kate L | |
dc.contributor.author | Bruning, John B | |
dc.contributor.author | Booker, Grant W | |
dc.contributor.author | Polyak, Steven W | |
dc.date.accessioned | 2021-04-22T04:09:15Z | |
dc.date.available | 2021-04-22T04:09:15Z | |
dc.date.issued | 2017 | |
dc.identifier.issn | 0968-0004 | |
dc.identifier.doi | 10.1016/j.tibs.2017.02.001 | |
dc.identifier.uri | http://hdl.handle.net/10072/403894 | |
dc.description.abstract | Protein 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.peerreviewed | Yes | |
dc.language | English | |
dc.publisher | Elsevier | |
dc.relation.ispartofpagefrom | 383 | |
dc.relation.ispartofpageto | 394 | |
dc.relation.ispartofissue | 5 | |
dc.relation.ispartofjournal | Trends in Biochemical Sciences | |
dc.relation.ispartofvolume | 42 | |
dc.subject.fieldofresearch | Chemical sciences | |
dc.subject.fieldofresearch | Biological sciences | |
dc.subject.fieldofresearch | Biomedical and clinical sciences | |
dc.subject.fieldofresearchcode | 34 | |
dc.subject.fieldofresearchcode | 31 | |
dc.subject.fieldofresearchcode | 32 | |
dc.subject.keywords | Science & Technology | |
dc.subject.keywords | Life Sciences & Biomedicine | |
dc.subject.keywords | Biochemistry & Molecular Biology | |
dc.subject.keywords | HOLOCARBOXYLASE SYNTHETASE DEFICIENCY | |
dc.subject.keywords | ACETYL-COA CARBOXYLASE | |
dc.title | Mechanisms Governing Precise Protein Biotinylation | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dcterms.bibliographicCitation | Sternicki, 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.dateAccepted | 2017-02-03 | |
dc.date.updated | 2021-04-22T04:07:41Z | |
gro.hasfulltext | No Full Text | |
gro.griffith.author | Sternicki, Louise | |