Biotin, which serves as a carboxyl group carrier in reactions catalyzed by biotin-dependent carboxylases, is essential for life in most organisms. To function in carboxylate transfer, the vitamin must be post-translationally linked to a specific lysine residue on the biotin carboxyl carrier (BCC) of a carboxylase in a reaction catalyzed by biotin protein ligases. Although biotin addition is highly selective for any single carboxylase substrate, observations of interspecies biotinylation suggested little discrimination among the BCCs derived from the carboxylases of a broad range of organisms. Application of single turnover kinetic techniques to measurements of post-translational biotin addition reveals previously unappreciated selectivity that may be of physiological significance.
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December 2018
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Dysfunctional cytoskeleton and neurodegeneration: novel pathways in Parkinson's disease? This image represents the degeneration of the neuronal tree during the aging process. In this issue Civiero et al. discuss the consequence of impaired cytoskeletal dynamics on neurite morphology and neuronal physiology in Parkinson's disease. For further details see pages 1653–1663.
Review Article|
October 31 2018
Specificity and selectivity in post-translational biotin addition
Dorothy Beckett
1Department of Chemistry & Biochemistry, University of Maryland, College Park, MD 20742, U.S.A.
Correspondence: Dorothy Beckett (dbeckett@umd.edu)
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Publisher: Portland Press Ltd
Received:
August 01 2018
Revision Received:
September 13 2018
Accepted:
September 14 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (6): 1577–1591.
Article history
Received:
August 01 2018
Revision Received:
September 13 2018
Accepted:
September 14 2018
Citation
Dorothy Beckett; Specificity and selectivity in post-translational biotin addition. Biochem Soc Trans 17 December 2018; 46 (6): 1577–1591. doi: https://doi.org/10.1042/BST20180425
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