title: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex.
abstract: Deoxynucleotide sequencing of a cDNA for the dihydrolipoamide acetyltransferase (PDC-E2) component of human pyruvate dehydrogenase complex (PDC) revealed an open reading frame of 1848 base pairs corresponding to a leader sequence of 54 amino acids and a mature protein of 561 amino acids (59,551 Da). Both an amino-terminal lipoyl-bearing domain and a carboxy-terminal catalytic domain are present in the deduced amino acid sequence. The lipoyl-bearing domain contains two repeating units of 127 amino acids, each harboring one lipoic acid-binding lysine. Thus, mammalian PDC-E2 differs as to the number of lipoic acid-binding sites from other dihydrolipoamide acyltransferases in both prokaryotic and eukaryotic organisms.
authors.affiliation: Department of Biochemistry, Case Western Reserve, University School of Medicine, Cleveland, OH 44106.
authors.forename: T J
authors.initials: TJ
authors.lastname: Thekkumkara
authors.forename: L
authors.initials: L
authors.lastname: Ho
authors.forename: I D
authors.initials: ID
authors.lastname: Wexler
authors.forename: G
authors.initials: G
authors.lastname: Pons
authors.forename: T C
authors.initials: TC
authors.lastname: Liu
authors.forename: M S
authors.initials: MS
authors.lastname: Patel
mesh_terms: D000123:Acetyltransferases / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D006801:Humans; D008969:Molecular Sequence Data; D011768:Pyruvate Dehydrogenase Complex / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
chemical_list: D011768:Pyruvate Dehydrogenase Complex; D012333:RNA, Messenger; D004247:DNA; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase