title: Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide.
abstract: Lipoyl synthase catalyzes the final step in the de novo biosynthesis of the lipoyl cofactor, which is the insertion of two sulfur atoms into an octanoyl chain that is bound in an amide linkage to a conserved lysine on a lipoyl-accepting protein. We show herein that the sulfur atoms in the lipoyl cofactor are derived from lipoyl synthase itself, and that each lipoyl synthase polypeptide contributes both of the sulfur atoms to the intact cofactor.
authors.affiliation: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
authors.forename: Robert M
authors.initials: RM
authors.lastname: Cicchillo
authors.forename: Squire J
authors.initials: SJ
authors.lastname: Booker
mesh_terms: D001426:Bacterial Proteins; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D008401:Gas Chromatography-Mass Spectrometry; D012436:S-Adenosylmethionine / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism*; D013466:Sulfurtransferases / Q000378:metabolism*; D008063:Thioctic Acid / Q000096:biosynthesis*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C079999:LipA protein, Bacteria; D013455:Sulfur; D008063:Thioctic Acid; D012436:S-Adenosylmethionine; D013466:Sulfurtransferases; C116435:lipoic acid synthase