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通过洋刀豆脲酶抑制剂的筛选实验得到具有较好抑制活性的化合物2-乙酰基-γ-丁内酯(COM),其半数抑制浓度在微摩尔浓度级别(IC50=375μmol·L-l).在此基础上,使用分子对接和分子动力学(MD)模拟的方法研究洋刀豆脲酶与抑制剂乙酰氧肟酸(AHA)及活性化合物COM之间的相互作用.用Gold3.0程序将两个小分子与洋刀豆脲酶的晶体结构进行对接,对接得到的复合物模型使用Amber程序进行MD模拟研究.模拟过程中,脲酶结构中的双核镍离子活性中心选用non-bonded模型.研究结果显示:AHA与洋刀豆脲酶结合时,Ni(1)和Ni(2)均为五配位;COM与洋刀豆脲酶结合时Ni(1)为五配位,Ni(2)为六配位的结合模型更加合理.这些研究为了解洋刀豆脲酶与抑制剂之间的相互作用提供了重要的参考信息.
The compound 2-acetyl-γ-butyrolactone (COM) with good inhibitory activity was obtained at a concentration of micromolar (IC50 = 375μmol·L -1) Based on this, molecular interactions and molecular dynamics (MD) simulations were used to study the interaction between yam beanase and acetohydroxamic acid (AHA) and its active compound COM.According to the Gold3.0 program, two Small molecules and the crystal structure of mandarin urease docking, docking the resulting composite model using Amber program for MD simulation study.Under the simulation of the binuclear nickel ion active center of urease structure selected non-bonded model.The results show that: Ni (1) and Ni (2) were all five-coordinated when AHA was combined with oceanflower urease; while for CO combined with oceanic bean urease, Ni (1) The binding model is more reasonable.These studies provide important reference information for understanding the interaction between the calachoine urease and the inhibitor.