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    FEBS Lett. 1988 Nov 21;240(1-2):45-8.

    Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex.

    Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS.

    Department of Biochemistry, Case Western Reserve, University School of Medicine, Cleveland, OH 44106.

    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.

    PMID: 3191998 [PubMed - indexed for MEDLINE]

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