QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase
文献类型：期刊论文
| 作者 | Wang, Jinhu ; Hou, Qianqian ; Dong, Lihua ; Liu, Yongjun ; Liu, Chengbu |
| 刊名 | JOURNAL OF MOLECULAR GRAPHICS & MODELLING
 ; 王金虎;侯倩倩;董丽花;刘永军;刘成卜.QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase,Journal of Molecular Graphics and Modelling,2011,30(14):148-152
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| 出版日期 | 2011-09-01 |
| 英文摘要 | The quantum-mechanical/molecular-mechanical (QM/MM)method was used to study the glycosylation mechanismof rice BGlu1_-glucosidase in complexwith laminaribiose. The calculation results reveal that the glycosylation step experiences a concerted process fromthe reactant to the glycosyl-enzyme complex with an activation barrier of 15.7 kcal/mol, in which an oxocarbenium cation-like transition state (TS) is formed. At the TS, the terminal saccharide residue planarizes toward the half-chair conformation, and the glycosidic bond cleavage is promoted by the attacks of proton donor (E176) on glycosidic oxygen and nucleophilic residue (E386) on the anomeric carbon of laminaribiose. Both the nucleophilic glutamate (E386) and acid/base catalyst (E176) establish shorter hydrogen bridges with the C2-hydroxyl groups of sugar ring, which play an important role in the catalytic reaction of rice BGlu1 beta-glucosidase.; The quantum-mechanical/molecular-mechanical (QM/MM) method was used to study the glycosylation mechanism of rice BGlu1 beta-glucosidase in complex with laminaribiose. The calculation results reveal that the glycosylation step experiences a concerted process from the reactant to the glycosyl-enzyme complex with an activation barrier of 15.7 kcal/mol, in which an oxocarbenium cation-like transition state (TS) is formed. At the TS, the terminal saccharide residue planarizes toward the half-chair conformation, and the glycosidic bond cleavage is promoted by the attacks of proton donor (El 76) on glycosidic oxygen and nucleophilic residue (E386) on the anomeric carbon of laminaribiose. Both the nucleophilic glutamate (E386) and acid/base catalyst (E176) establish shorter hydrogen bridges with the C(2)-hydroxyl groups of sugar ring, which play an important role in the catalytic reaction of rice BGlu1 beta-glucosidase. (C) 2011 Elsevier Inc. All rights reserved. |
| 源URL | [http://ir.nwipb.ac.cn//handle/363003/2176]  |
| 专题 | 西北高原生物研究所_中国科学院西北高原生物研究所 |
| 推荐引用方式 GB/T 7714 | Wang, Jinhu,Hou, Qianqian,Dong, Lihua,et al. QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase[J]. JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 王金虎;侯倩倩;董丽花;刘永军;刘成卜.QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase,Journal of Molecular Graphics and Modelling,2011,30(14):148-152,2011. |
| APA | Wang, Jinhu,Hou, Qianqian,Dong, Lihua,Liu, Yongjun,&Liu, Chengbu.(2011).QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase.JOURNAL OF MOLECULAR GRAPHICS & MODELLING. |
| MLA | Wang, Jinhu,et al."QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase".JOURNAL OF MOLECULAR GRAPHICS & MODELLING (2011). |
入库方式： OAI收割
来源：西北高原生物研究所
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