Molecular cloning and domain structure of chicken pyruvate carboxylase

Biochem Biophys Res Commun. 2002 Jul 12;295(2):387-93. doi: 10.1016/s0006-291x(02)00651-4.

Abstract

Pyruvate carboxylase (PC) [EC 6.4.1.1] is a biotin-dependent carboxylase that catalyses the conversion of pyruvate to oxaloacetate. Here we have determined the complete nucleotide sequence encoding chicken PC (cPC) by screening a liver cDNA library, by RT-PCR of poly(A)(+) RNA, and by PCR of genomic DNA. The full-length transcript contains an open reading frame of 3537 nucleotides, including the stop codon, encoding a polypeptide of 1178 amino acids with M(r) of 127,262. The amino acid sequence of cPC shows approximately 77% identity to mammalian PC. Limited proteolysis of pure cPC with chymotrypsin yields a major stable 75 kDa C-terminal peptide, including the biotinyl domain and a minor, unstable 39 kDa N-terminal peptide. Northern analysis of poly(A)(+) RNA isolated from chicken liver has shown that cPC's mRNA is approximately 5 kb in length, including a very long 3'-untranslated region.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Chickens
  • Cloning, Molecular
  • DNA, Complementary
  • Molecular Sequence Data
  • Pyruvate Carboxylase / chemistry
  • Pyruvate Carboxylase / genetics*

Substances

  • DNA, Complementary
  • Pyruvate Carboxylase

Associated data

  • GENBANK/AF509529