Structural highlights
Function[PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.[1] Publication Abstract from PubMedAspartate alpha-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of beta-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. Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase.,Webb ME, Yorke BA, Kershaw T, Lovelock S, Lobley CM, Kilkenny ML, Smith AG, Blundell TL, Pearson AR, Abell C Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1166-72. doi:, 10.1107/S1399004713034275. Epub 2014 Mar 21. PMID:24699660[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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