Omata Y, Sakamoto H, Robinson R C, Pincus M R, Friedman F K
Laboratory of Molecular Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Biochem Biophys Res Commun. 1994 Jun 30;201(3):1090-5. doi: 10.1006/bbrc.1994.1817.
Binding of cytochrome b5 to rat cytochrome P450 2B1 was inhibited (by 75%) by a synthetic peptide corresponding to P450 residues 116-134. The role of Lys-122 and Arg-125 were evaluated using peptides in which one or both of these basic residues were replaced with Glu. The Lys-122 substitution nearly abolished while the Arg-125 replacement decreased (by 20%) the inhibitory potential of the peptide. Substitution of both residues resulted in a peptide with no inhibitory activity. These results thus indicate a role for a specific P450 region as well as two basic residues within this region in the cytochrome P450-cytochrome b5 interaction.
与大鼠细胞色素P450 2B1结合的细胞色素b5被对应于P450第116 - 134位残基的合成肽抑制（75%）。使用将这些碱性残基中的一个或两个替换为Glu的肽来评估Lys-122和Arg-125的作用。Lys-122的替换几乎消除了肽的抑制潜力，而Arg-125的替换使肽的抑制潜力降低了20%。两个残基都被替换后产生了一种没有抑制活性的肽。因此，这些结果表明细胞色素P450特定区域以及该区域内的两个碱性残基在细胞色素P450 - 细胞色素b5相互作用中发挥作用。
