| First Author | Kimura S | Year | 1984 |
| Journal | Nucleic Acids Res | Volume | 12 |
| Issue | 6 | Pages | 2917-28 |
| PubMed ID | 6324134 | Mgi Jnum | J:32401 |
| Mgi Id | MGI:79897 | Doi | 10.1093/nar/12.6.2917 |
| Citation | Kimura S, et al. (1984) Mouse cytochrome P3-450: complete cDNA and amino acid sequence. Nucleic Acids Res 12(6):2917-28 |
| abstractText | 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. P3-450 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 P3-450 enzyme active-site. |
