Schwarze W, Jaeger J, Jänig G R, Ruckpaul K
Central Institute of Molecular Biology, Academy of Sciences of GDR, Berlin.
Biochem Biophys Res Commun. 1988 Feb 15;150(3):996-1005. doi: 10.1016/0006-291x(88)90727-9.
Based on (i) a detailed analysis of the physicochemical properties of selected benzphetamine derived substrates and (ii) the identification of Tyr-380 as active site residue trans to thiolate theoretical studies (computer aided molecular design) revealed a model of the substrate binding site of cytochrome P-450 LM2. The results indicate that substrates with a butterfly-like bulky conformation exhibit the highest intrinsic activity. Those substrates which preferably exist in an extended conformation are sterically hindered to intensively interact with the binding site which is demonstrated by computer graphics.
基于（i）对选定的苄非他明衍生底物的物理化学性质的详细分析以及（ii）将Tyr-380鉴定为与硫醇盐反位的活性位点残基，理论研究（计算机辅助分子设计）揭示了细胞色素P-450 LM2底物结合位点的模型。结果表明，具有蝴蝶状庞大构象的底物表现出最高的内在活性。那些优选以伸展构象存在的底物在空间上受到阻碍，无法与结合位点进行强烈相互作用，这一点通过计算机图形学得到了证明。
