Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence

T. Takai, C. Yokoyama, K. Wada, T. Tanabe

Research output: Contribution to journalArticlepeer-review

80 Citations (Scopus)

Abstract

The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by Edman degradation of peptide fragments obtained by digestion of the enzyme polypeptide with Achromobacter proteinase I or staphylococcal serine proteinase. Chicken liver acetyl-CoA carboxylase is predicted to be composed of 2,324 amino acid residues, having a calculated molecular weight of 262,706. The biotin carboxyl carrier protein domain is located in the middle region of the enzyme polypeptide. The amino-terminal portion of the acetyl-CoA carboxylase has been found to exhibit a homologous primary structure to that of carbamyl phosphate synthetase. Localization of possible functional domains including biotin carboxylase subsite in the acetyl-CoA carboxylase polypeptide is discussed.

Original languageEnglish
Pages (from-to)2651-2657
Number of pages7
JournalJournal of Biological Chemistry
Volume263
Issue number6
Publication statusPublished - 1988 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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