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Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase.

Published version
Peer-reviewed

Type

Article

Change log

Authors

Webb, Michael E 
Yorke, Briony A 
Kershaw, Tom 
Lovelock, Sarah 
Lobley, Carina MC 

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.

Description

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

Journal Title

Acta Crystallogr D Biol Crystallogr

Conference Name

Journal ISSN

0907-4449
1399-0047

Volume Title

70

Publisher

International Union of Crystallography (IUCr)
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/D005817/1)