title: Function, attachment and synthesis of lipoic acid in Escherichia coli.
abstract: A series of genetic, biochemical, and physiological studies in Escherichia coli have elucidated the unusual pathway whereby lipoic acid is synthesized. Here we describe the results of these investigations as well as the functions of enzyme proteins that are modified by covalent attachment of lipoic acid and the enzymes that catalyze the modification reactions. Some aspects of the synthesis and attachment mechanisms have strong parallels in the pathways used in synthesis and attachment of biotin and these are compared and contrasted. Homologues of the lipoic acid metabolism proteins are found in all branches of life, save the Archea, and thus these findings seem to have wide biological relevance.
authors.affiliation: Department of Microbiology, University of Illinois, Urbana, IL 61801, USA.
authors.forename: John E
authors.initials: JE
authors.lastname: Cronan
authors.forename: Xin
authors.initials: X
authors.lastname: Zhao
authors.forename: Yanfang
authors.initials: Y
authors.lastname: Jiang
mesh_terms: D000217:Acyltransferases / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D008074:Lipoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D008063:Thioctic Acid / Q000378:metabolism* / Q000502:physiology
chemical_list: D029968:Escherichia coli Proteins; D008074:Lipoproteins; C490345:lplA protein, E coli; D008063:Thioctic Acid; D000217:Acyltransferases; C421483:LipB protein, E coli; D008025:Ligases