QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase

NWIPB OpenIR

	QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase
	Wang, Jinhu ; Hou, Qianqian ; Dong, Lihua ; Liu, Yongjun ; Liu, Chengbu
	2011-09-01
发表期刊	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
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.
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/41148
专题	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).