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Nucleic Acids Research, 1984, Vol. 12, No. 6 2917-2928
© 1984

MOLECULAR BIOLOGY

Mouse cytochrome P3-450: complete cDNA and amino acid sequence

Shioko Kimura, Frank J. Gonzalez and Daniel W. Nebert

Laboratory of Developmental Pharmacology, National Institute of Child Health and Human Development, National Institutes of Health Bethesda, MD 20205, USA

Received January 3, 1984. Revised February 22, 1984. Accepted February 22, 1984.

A full-length cDNA clone. (1,894 nucleotides) of mouse cytochrome P3-450 was isolated with the Okayama-Berg vector and sequenced. An open reading frame spanned positions 61 to 1602. The first 25, and three of the last five, amino acids of P3-450 are identical to those found in the amino- and carboxy-terminus, respectively, of the rat P-450d protein. Mouse P3-450 protein has 513 residues, and a molecular weight of 58,223 with six cysteine residues. P3-45O nucleotides 305 to 352 exhibit 74% homology, and nucleotides 1068 to 1260, 69% homology, with portions of rat P-450b exons 2 and 7, respectively. P3-450 shows 62% homology in the so-called "highly conserved region" of 39 nucleotides in the rat P-450b and P-450e and the mouse P-450b. These results indicate that P3-450, P-450b and P-450e arose from a common ancestral gene. Cysteinyl peptide-coding regions were examined: P3-450 nucleotides 1405 to 1464 exhibit 61% homology, and nucleotides 502 to 552 exhibit 37% homology, when compared with their corresponding regions in the rat P-450b gene. These data support the likelihood that cysteine 456 is the thiolate ligand to the heme iron in the P3-45O enzyme active-site.


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