Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex

J Biochem. 1987 Dec;102(6):1333-6. doi: 10.1093/oxfordjournals.jbchem.a122178.

Abstract

cDNA clones for bovine adrenodoxin reductase were isolated, and the primary structure of the enzyme precursor was deduced from their nucleotide sequences. The precursor consists of 492 amino acids including an extrapeptide of 32 amino acids at the amino terminus. The extrapeptide is hydrophilic [corrected] and rich in arginine. The amino terminal sequence of the precursor is homologous with that of the adrenodoxin precursor. A possible FAD- or NADPH-binding site is present near the amino terminus of the mature enzyme.

MeSH terms

  • Adrenal Cortex / enzymology*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cattle
  • DNA / genetics*
  • DNA, Recombinant
  • Enzyme Precursors / genetics*
  • Ferredoxin-NADP Reductase / genetics*
  • Ferredoxin-NADP Reductase / metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases / genetics*
  • NADP / metabolism
  • Peptide Fragments / genetics
  • RNA, Messenger / genetics

Substances

  • DNA, Recombinant
  • Enzyme Precursors
  • Peptide Fragments
  • RNA, Messenger
  • Flavin-Adenine Dinucleotide
  • NADP
  • DNA
  • Ferredoxin-NADP Reductase
  • NADH, NADPH Oxidoreductases

Associated data

  • GENBANK/D00211