FEBS Letters | |
Evidence for two protein‐lipoylation activities in Escherichia coli | |
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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020295729ZK.pdf | 398KB | download |