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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.

Author information

  • 1Department of Biochemistry, Case Western Reserve, University School of Medicine, Cleveland, OH 44106.

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.

PMID:
3191998
[PubMed - indexed for MEDLINE]
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