MOUSE NADPH-CYTOCHROME P-450 OXIDOREDUCTASE - MOLECULAR-CLONING AND FUNCTIONAL EXPRESSION IN YEAST

We published isolation of a mouse NADPH-cytochrome P-450 oxidoreductas e cDNA and afterward ascribed the cDNA to the guinea-pig instead of th e mouse (Ohgiya, S. et al. (1992) Biochim. Biophys. Acta 1171, 103-105 and Corrigendum (1993) Biochim. Biophys. Acta 1174, 313). We report h ere nucleotide and deduced amino acid sequences of an NADPH-cytochrome P-450 oxidoreductase cDNA isolated from the ddY mouse. The mouse cyto chrome P-450 oxidoreductase shares 98.4% identity with its rat counter part. In particular, clusters of acidic residues that presumably parti cipate in interaction with cytochrome P-450 are highly conserved in pr imary structures of mammalian cytochrome P-450 oxidoreductases. The mo use cytochrome P-450 oxidoreductase was functionally expressed in yeas t using a modified cDNA clone lacking whole noncoding regions.