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J. Biol. Chem., Vol. 263, Issue 6, 2651-2657, 02, 1988
T Takai, C Yokoyama, K Wada and T Tanabe
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.
Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence
Laboratory of Cell Biology, National Cardiovascular Center Research Institute, Osaka, Japan.
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