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Evidence for two protein‐lipoylation activities in Escherichia coli
Author(s) -
Brookfield Dawn E.,
Green Jeffrey,
Ali Sohail T.,
Machado Rosane S.,
Guest John R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81373-g
Subject(s) - escherichia coli , computer science , escherichia coli proteins , chemistry , computational biology , microbiology and biotechnology , biology , biochemistry , gene
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 Mg 2+ , 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.