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

FEBS Letters

Patel, Mulchand S.¹  Pons, Gabriel¹  Thekkumkara, Thomas J.¹  Te-Chung, Liu¹  Ho, Lap¹  Wexler, Isaiah D.¹ 

[1] Departments of Biochemistry and Pediatrics, Case Western Reserve, University School of Medicine, Cleveland, OH 44106, USA

关键词: cDNA;    Dihydrolipoamide acetyltransferase;    Nucleotide sequence;    Amino acid sequence;    (Human liver);   

DOI  :  10.1016/0014-5793(88)80337-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown