Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure

• Published in: The Journal of biological chemistry Vol. 263; no. 13; pp. 6165 - 6168
• Main Authors: Hummel, K B, Litwer, S, Bradford, A P, Aitken, A, Danner, D J, Yeaman, S J
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 05.05.1988; American Society for Biochemistry and Molecular Biology
• Subjects: 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); Acyltransferases - genetics; Amino Acid Sequence; Base Sequence; Biological and medical sciences; Biotechnology; DNA - analysis; Fundamental and applied biological sciences. Psychology; Genes. Genome; Genetic engineering; Genetic technics; Ketone Oxidoreductases - genetics; Methods. Procedures. Technologies; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes - genetics; Synthetic digonucleotides and genes. Sequencing; Human; Translation; Multienzyme complex; Complementary DNA; Nucleotide sequence; Enzyme; Polyadenylation; Restriction map; Binding site; 2-Oxoisovalerate dehydrogenase (lipoamide)
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)68766-6

Nucleotide sequence was determined for a 1.6-kilobase human cDNA putative for the branched chain acyltransferase protein of the branched chain alpha-ketoacid dehydrogenase complex. Translation of the sequence reveals an open reading frame encoding a 315-amino acid protein of molecular weight 35,759 followed by 560 bases of 3'-untranslated sequence. Three repeats of the polyadenylation signal hexamer ATTAAA are present prior to the polyadenylate tail. Within the open reading frame is a 10-amino acid fragment which matches exactly the amino acid sequence around the lipoate-lysine residue in bovine kidney branched chain acyltransferase, thus confirming the identity of the cDNA. Analysis of the deduced protein structure for the human branched chain acyltransferase revealed an organization into domains similar to that reported for the acyltransferase proteins of the pyruvate and alpha-ketoglutarate dehydrogenase complexes. This similarity in organization suggests that a more detailed analysis of the proteins will be required to explain the individual substrate and multienzyme complex specificity shown by these acyltransferases.