Coding Nucleotide Sequence of 3-methylcholanthrene-Inducible Cytochrome P-450d cDNA from Rat Liver

We determined the coding nucleotide sequence of the mRNA for a 3-methylcholanthrene-inducible cytochrome P-450, P-450d, of rat liver by sequence analysis of cloned cDNAs. The predicted amino acid sequence of the cytochrome is composed of 513 amino acids, and its NH2-terminal sequence of 30 amino aci...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1984-03, Vol.81 (6), p.1649-1653
Main Authors: Kawajiri, Kaname, Gotoh, Osamu, Sogawa, Kazuhiro, Tagashira, Yusaku, Muramatsu, Masami, Fujii-Kuriyama, Yoshiaki
Format: Article
Language:English
Subjects:
3-methylcholanthrene
Amino Acid Sequence
Amino acids
Animals
Base Sequence
Biochemistry
Biological Evolution
cDNA
Complementary DNA
cytochrome P-450
Cytochrome P-450 Enzyme System - genetics
cytochrome P450
Cytochromes
DNA
DNA - genetics
Enzyme Induction - drug effects
Genes
Gin
Liver
Liver - physiology
Messenger RNA
Methylcholanthrene - pharmacology
nucleotide sequence
Nucleotide sequences
Rats
RNA, Messenger - genetics
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Summary:We determined the coding nucleotide sequence of the mRNA for a 3-methylcholanthrene-inducible cytochrome P-450, P-450d, of rat liver by sequence analysis of cloned cDNAs. The predicted amino acid sequence of the cytochrome is composed of 513 amino acids, and its NH2-terminal sequence of 30 amino acids completely coincides with that reported from analysis of the purified cytochrome P-450d. The amino acid composition of the deduced sequence also agrees well with that determined from the purified protein. Computer-aided analysis was carried out to compare the complete primary structures of five species of cytochrome P-450, two molecular species of phenobarbital-inducible rat liver cytochrome P-450 (P-450b and P-450e), phenobarbital-inducible rabbit liver cytochrome P-450LM2, 3-methylcholanthrene-inducible rat liver cytochrome P-450d, and camphor-hydroxylating P-450 of Pseudomonas putida (P-450CAM). It is concluded therefrom that the time of divergence between cytochrome P-450b (P-450e) and P-450d is much earlier than that of branching between phenobarbital-inducible cytochromes P-450 of rat and rabbit. One highly conserved cysteine-containing region that is close to the COOH terminus is found in all of these cytochrome P-450 sequences, indicating that the heme-binding site is the cysteine residue in this region.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.81.6.1649