Threonine 57 is required for the post-translational activation of Escherichia coli aspartate α-decarboxylase.
Acta Crystallogr D Biol Crystallogr
; 70(Pt 4): 1166-72, 2014 Apr.
Article
em En
| MEDLINE
| ID: mdl-24699660
ABSTRACT
Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of ß-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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Escherichia coli
/
Glutamato Descarboxilase
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article