J. Biochem, 1988, Vol. 103, No. 6 1004-1010
© 1988 Japanese Biochemical Society
research-article |
Primary Structure of Saccharomyces cerevisiae NADPH-Cytochrome P450 Reductase Deduced from Nucleotide Sequence of Its Cloned Gene1
Biotechnology Laboratory, Takarazuka Research Center, Sumitomo Chemical Co., Ltd. Takarazuka, Hyogo 665
We isolated cDNA (pgCYR, about 2.1 kb) and genomic DNA (pgGYR, about 4 kb) clones coding for NADPH-cytochrome P450 reductase by immunoscreening of yeast Saccharomyces cerevisiae cDNA and genomic DNA libraries in phage 
gt11. The clones were sequenced and found to encode a protein of 691 amino acid residues with a calculated molecular weight of 76,737 daltons. The amino-terminal sequence (excluding the initial methionine residue) deduced therefrom was in agreement with the protein sequence of the yeast reductase. In addition, the deduced sequence included the partial amino acid sequence determined with the papain-solubilized reductase. The total amino acid sequence of the yeast reductase showed 33–34% similarity with those of the rat, rabbit, pig, and trout reductases. In spite of low similarity in the total amino acid sequences, the possible functional domains related to binding of FAD, FMN, and NADPH were well conserved among all five species compared.
1This work was supported by the Research and Development Projects of Basic Technologies for Future Industries, Ministry of International Trade and Industry of Japan.
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