RRC ID |
50329
|
著者 |
Kawajiri K, Gotoh O, Sogawa K, Tagashira Y, Muramatsu M, Fujii-Kuriyama Y.
|
タイトル |
Coding nucleotide sequence of 3-methylcholanthrene-inducible cytochrome P-450d cDNA from rat liver.
|
ジャーナル |
Proc Natl Acad Sci U S A
|
Abstract |
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.
|
巻・号 |
81(6)
|
ページ |
1649-53
|
公開日 |
1984-3-1
|
DOI |
10.1073/pnas.81.6.1649
|
PMID |
6584898
|
PMC |
PMC344975
|
MeSH |
Amino Acid Sequence
Animals
Base Sequence
Biological Evolution
Cytochrome P-450 Enzyme System / genetics*
DNA / genetics
Enzyme Induction / drug effects
Genes
Liver / physiology*
Methylcholanthrene / pharmacology
RNA, Messenger / genetics
Rats
|
IF |
9.412
|
引用数 |
170
|
リソース情報 |
遺伝子材料 |
P450 1A2 (CYP1A2) cDNA (RDB01244) |