PMID:1765143

Citation	Brookfield, DE, Green, J, Ali, ST, Machado, RS and Guest, JR (1991) Evidence for two protein-lipoylation activities in Escherichia coli. FEBS Lett. 295:13-6
Abstract	The lipoate acyltransferase subunits of the 2-oxo acid dehydrogenase complexes are post-translationally modified with one or more covalently-bound lipoyl cofactors. Two distinct lipoate-protein ligase activities, LPL-A and LPL-B, have been detected in E. coli by their ability to modify purified lipoyl apo-domains of the bacterial pyruvate dehydrogenase complex. Both enzymes require ATP and Mg2+, use L-lipoate, 8-methyllipoate, lipoyl adenylate and octanoyl adenylate as substrates, and both activate lipoyl-deficient pyruvate dehydrogenase complexes. In contrast, only LPL-B uses D-lipoate and octanoate and there are differences in the metal-ion and phosphate requirements. It is suggested that LPL-B may be responsible for the octanoylation of lipoyl domains observed previously under lipoate-deficient conditions.
Links	PubMed
Keywords	Chromatography, Affinity; Enzyme Activation; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Peptide Synthases/genetics; Peptide Synthases/isolation & purification; Peptide Synthases/metabolism; Protein Processing, Post-Translational; Pyruvate Dehydrogenase Complex/metabolism; Substrate Specificity; Thioctic Acid/metabolism
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