Theoretical Investigation on Binding Process of Allophanate to AUophanate Hydrolase

t Several molecular simulation methods were integrated to investigate the detailed binding process of allo- phanate to allophanate hydrolase and predict their stable complex structure. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also on...

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Published in:高等学校化学研究：英文版 2015 (6), p.1023-1028
Main Author: ZHANG Zidong ZHANG Jilong ZHENG Qingchuan KONG Chuipeng LI Zhengqiang ZHANG Hongxing MA Jianzhang
Format: Article
Language:English
Subjects:
复合物
模拟方法
水解酶
状态
稳定
结合过程
脲基甲酸酯
计算表
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Summary:t Several molecular simulation methods were integrated to investigate the detailed binding process of allo- phanate to allophanate hydrolase and predict their stable complex structure. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also one of the key anchor residues in the stable complex. The energetic calculation suggests the existence of an intermediate state in the enzyme-substrate binding process. The further atomic-level investigation illuminates that Tyr299, Arg307 and Ser172 can stabilize the substrate in the intermediate state. By this token, the residues Arg307 and Tyr299 function in both binding process and getting stable state.
ISSN:1005-9040
2210-3171