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. 1991 Dec 16;295(1-3):13-6.
doi: 10.1016/0014-5793(91)81373-g.

Evidence for two protein-lipoylation activities in Escherichia coli

D E Brookfield  1 , J Green, S T Ali, R S Machado, J R Guest
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Free article

Evidence for two protein-lipoylation activities in Escherichia coli

D E Brookfield et al. FEBS Lett. .
Free article

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.

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