Evidence for two protein‐lipoylation activities in Escherichia coli

FEBS Letters

Machado, Rosane S.¹  Brookfield, Dawn E.¹  Green, Jeffrey¹  Ali, Sohail T.¹  Guest, John R.¹ 

[1] The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2UH, UK

关键词: Lipoate-protein ligase;    Protein acylation;    Lipoyl domain;    Pyruvate dehydrogenase complex;    Post-translational modification;    Escherichia coli;    LPL;    lipoate-protein ligase;    E2p;    lipoate acetyltransferase;    E2o;    lipoate succinyltransferase;    EDTA;    diaminoethane tetraacetate;    IPTG;    isopropyl β-thiogalactoside;    ODH;    2-oxoglutarate dehydrogenase;    PAGE;    polyacrylamide gel electrophoresis;    PDH;    pyruvate dehydrogenase;    PMSF;    phenylmethylsulphonyl fluoride;   

DOI  :  10.1016/0014-5793(91)81373-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown