Webb, ME, Yorke, BA, Kershaw, T et al. (7 more authors) (2014) Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase. Acta Crystallographica Section D: Biological Crystallography, 70 (Pt 4). 1166 - 1172. ISSN 0907-4449
Abstract
Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formed via the intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014 Webb et al. This is an open access article under the terms of the Creative Commons Attribution License CC-BY. |
Keywords: | amino-acid-derived cofactors; aspartate decarboxylase; post-translational modification; pyruvoyl-dependent; Enzyme Activation; Escherichia coli; Glutamate Decarboxylase; Models, Molecular; Mutation; Protein Structure, Tertiary; Threonine |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 24 Aug 2015 10:09 |
Last Modified: | 24 Aug 2015 10:09 |
Published Version: | http://dx.doi.org/10.1107/S1399004713034275 |
Status: | Published |
Publisher: | International Union of Crystallography |
Identification Number: | 10.1107/S1399004713034275 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:85556 |