部位特異的変異体を用いたシトクロムP450反応機構の解析

抄録

Recent advances in genetic engineering techniques have enabled the determination of complete amino acid sequences of cytochrome P450's. Alignment of the known sequences revealed the presence of several homologous regions in the sequence. These data together with results for the crystallographic structure suggested that highly conserved residues in the oxygen binding pocket, Asp and Thr residues play a key role in the oxygen activation of this enzyme. In this paper, we summarized the function of these residues in the oxygen activation, based on findings obtained by site-directed mutagenesis.