Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex.
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.
Thekkumkara
T J
TJ
Department of Biochemistry, Case Western Reserve, University School of Medicine, Cleveland, OH 44106.
Ho
L
L
Wexler
I D
ID
Pons
G
G
Liu
T C
TC
Patel
M S
MS
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
D011768:Pyruvate Dehydrogenase Complex; D012333:RNA, Messenger; D004247:DNA; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase