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Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex
Author(s) -
Thekkumkara Thomas J.,
Ho Lap,
Wexler Isaiah D.,
Pons Gabriel,
Te-Chung Liu,
Patel Mulchand S.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80337-5
Subject(s) - dihydrolipoamide dehydrogenase , pyruvate dehydrogenase complex , biochemistry , amino acid , peptide sequence , biology , open reading frame , complementary dna , nucleic acid sequence , dihydrolipoyl transacetylase , lipoic acid , acetyltransferase , microbiology and biotechnology , pyruvate dehydrogenase phosphatase , enzyme , gene , acetylation , antioxidant
Deoxynucleotide sequencing of a cDNA for the dihydrolipoamide acetyltransferase (PDC‐E 2 ) 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‐E 2 differs as to the number of lipoic acid‐binding sites from other dihydrolipoamide acyltransferases in both prokaryotic and eukaryotic organisms.