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

ABSTRACT: Aspartate ?-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of ?-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.

SUBMITTER: Webb ME 

PROVIDER: S-EPMC3975893 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature