NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein

Biochemistry. 1990 Oct 23;29(42):9814-8. doi: 10.1021/bi00494a009.


cDNA clones to rat liver NADPH-cytochrome P-450 oxidoreductase were used to isolate genomic clones from a Wistar-Furth inbred rat genomic DNA library. Fifteen exons containing the coding region and 3'-nontranslated segment of the P-450 reductase gene were identified, spanning 20 kilobases of DNA contained in 3 lambda-Charon 35 clones. The organization of this single copy gene reveals a general correspondence between exons and structural domains of the protein, with the segment responsible for anchoring the reductase to the microsomal membrane and several segments involved in FMN, FAD, and NADPH binding encoded by discrete exons.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cytochrome P-450 Enzyme System / metabolism
  • DNA / genetics
  • Endoplasmic Reticulum / enzymology
  • Exons
  • Flavin Mononucleotide / metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Genes
  • Molecular Sequence Data
  • NADP / metabolism*
  • NADPH-Ferrihemoprotein Reductase / genetics*
  • Protein Binding
  • Rats
  • Rats, Inbred WF


  • Flavin-Adenine Dinucleotide
  • NADP
  • Flavin Mononucleotide
  • DNA
  • Cytochrome P-450 Enzyme System
  • NADPH-Ferrihemoprotein Reductase

Associated data

  • GENBANK/J05291
  • GENBANK/M58932
  • GENBANK/M58933
  • GENBANK/M58934
  • GENBANK/M58935
  • GENBANK/M58936
  • GENBANK/M58937