钴型腈水合酶降解腈的分子模拟研究  

Molecular simulation of nitrile degradation by Co-type nitrile hydratase

作　　者：张娱 刘智峰[2] 陈明[2] 刘世军 许洪波 唐志书 ZHANG Yu, LIU Zhi-feng, CHEN Ming, LIU Shi-jun, XU Hong-bo, TANG Zhi-shu(1. Shaanxi University of Chinese Medicine/Shaanxi Collaborative Innovation Center of Chinese Medicinal Resource Industrialization, Xianyang 712083； 2. College of Environment Science and Engineering, Hunan University, Changsha 41008)

机构地区：[1]陕西中医药大学/陕西省中药资源产业化协同创新中心,咸阳712083 [2]湖南大学环境科学与工程学院,长沙410082

出　　处：《中国食品添加剂》2018年第4期59-65,共7页China Food Additives

基　　金：国家自然科学基金项目(51679085);陕西中医药大学校内基金项目(2015PY10)

摘　　要：为探索钴型腈水合酶降解腈的微观降解机制,用分子对接的方法模拟了钴型腈水合酶与腈的相互作用,得到他们复合物结构的理论模型,根据打分函数最低原则筛选出的PtNHase与烟腈之间最佳构象打分函数为-63.9557,二次打分函数为-56.056。应用LPC/CSU server研究最佳构象的相互作用情况,结果表明,PtNHase与烟腈之间以疏水作用数量最多,钴型腈水合酶的氨基酸残基αLeu88、βAla122、βLeu127、βPhe37、βPhe41和βPhe118在催化过程中起到了关键作用。In order to explore Co-type nitrile degradation enzymes microscopic degradation mechanism,molecular docking method was used to investigate the binding modes of nitrile to Co-type nitrile hydratase. The theoretical models of their structures were obtained. According to the lowest score function principle,the results showed that the best conformation scoring function between PtNHase and 3-Cyanopyridine were -63.9557,re-rank scores were -56.056. And LPC/CSU server was used in searching the interactions between PtNHase and 3-Cyanopyridine. Our results showed that hydrophobic interaction was the strongest contacts in the complex.The amino acid residues αLeu88、βAla122、βLeu127、βPhe37、βPhe41 and βPhe118 played significant roles in catalytic processes.

关 键 词：酰胺 酰胺酶 生物降解 

分 类 号：Q556[生物学—生物化学]