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 1; Hou, Qianqian 1; Dong, Lihua 2; Liu, Yongjun 1,2; Liu, Chengbu 1
	2011-09-01
发表期刊	JOURNAL OF MOLECULAR GRAPHICS & MODELLING
ISSN	1093-3263
卷号	30 期号:14 页码:148-152
文章类型	Article
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.
关键词	Glycosylation Beta-glucosidases Qm/mm Laminaribiose Mechanism
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Technology ; Physical Sciences
关键词[WOS]	CRYSTAL-STRUCTURE ; MOLECULAR-DYNAMICS ; SUBSTRATE-SPECIFICITY ; AGLYCONE SPECIFICITY ; CATALYTIC MECHANISM ; ZEOLITE STRUCTURE ; GLYCOSIDASE ; INSIGHTS ; MAIZE ; TRANSGLYCOSYLATION
收录类别	SCI
语种	英语
WOS研究方向	Biochemistry & Molecular Biology ; Computer Science ; Crystallography ; Mathematical & Computational Biology
WOS类目	Biochemical Research Methods ; Biochemistry & Molecular Biology ; Computer Science, Interdisciplinary Applications ; Crystallography ; Mathematical & Computational Biology
WOS记录号	WOS:000297093600017
引用统计	被引频次：16[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/2176
专题	中国科学院西北高原生物研究所
作者单位	1.Shandong Univ, Sch Chem & Chem Engn, Key Lab Colloid & Interface Chem, Minist Educ, Jinan 250100, Shandong, Peoples R China 2.Chinese Acad Sci, NW Inst Plateau Biol, Xining 810001, Qinghai, Peoples R China
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,2011,30(14):148-152.
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,30(14),148-152.
MLA	Wang, Jinhu,et al."QM/MM studies on the glycosylation mechanism of rice BGlu1 beta-glucosidase".JOURNAL OF MOLECULAR GRAPHICS & MODELLING 30.14(2011):148-152.

条目包含的文件		下载所有文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
QM MM studies on the（420KB）			开放获取	--	浏览下载