Theoretical studies on the common catalytic mechanism of transketolase by using simplified models

doi:10.1016/j.jmgm.2012.11.001

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	Theoretical studies on the common catalytic mechanism of transketolase by using simplified models
	Sheng, Xiang 1; Liu, Yongjun1,2 ; Liu, Chengbu 1
	2013-02-01
发表期刊	JOURNAL OF MOLECULAR GRAPHICS & MODELLING
ISSN	1093-3263
卷号	39 页码:23-28
文章类型	Article
摘要	Transketolase is a convenient model system to study enzymatic thiamin catalysis. By using density functional theory (DFT) method, the transfer mechanism of a 2-carbon fragment between a donor ketose X5P and an acceptor aldose R5P catalyzed by transketolase has been studied on simplified models. The calculation results indicate that the whole reaction cycle contains several proton transfer processes as well as C-C bond formation and cleavage steps. Each C-C bond formation or cleavage step is always accompanied by a proton transfer process, which follows a concerted but asynchronous mechanism. The C-C bond formation is always prior to the proton transfer, and the C-C bond cleavage is always later than proton transfer, suggesting that the C-C bond ligation facilitates the proton transfer, and proton transfer promotes the C-C bond cleavage. In the first half- and second half-reactions, the energy barriers of C-C bond formations are always higher than those of C-C bond cleavages. The 4-amino group of cofactor ThDP and histidine residue can act as the proton donor/acceptor during the catalytic reaction. (C) 2012 Elsevier Inc. All rights reserved.
关键词	Transketolase Density Functional Theory (Dft) Method Reaction Mechanism Thdp-dependent Enzyme 2-carbon Fragment Transfer
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Technology ; Physical Sciences
DOI	10.1016/j.jmgm.2012.11.001
关键词[WOS]	DENSITY-FUNCTIONAL THERMOCHEMISTRY ; DIPHOSPHATE DEPENDENT ENZYME ; THIAMIN DIPHOSPHATE ; PYRUVATE DECARBOXYLASE ; YEAST TRANSKETOLASE ; ACETOHYDROXYACID SYNTHASE ; SACCHAROMYCES-CEREVISIAE ; BINDING ; ACTIVATION ; EXCHANGE
收录类别	SCI
语种	英语
项目资助者	Natural Science Foundation of China(21173129)
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:000315839400003
出版者	ELSEVIER SCIENCE INC
引用统计	被引频次：10[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/363003/3962
专题	中国科学院西北高原生物研究所
通讯作者	Liu, Yongjun
作者单位	1.Shandong Univ, Sch Chem & Chem Engn, Jinan 250100, Shandong, Peoples R China 2.Chinese Acad Sci, Northwest Inst Plateau Biol, Key Lab Adaptat & Evolut Plateau Biota, Xining 810001, Qinghai, Peoples R China
推荐引用方式 GB/T 7714	Sheng, Xiang,Liu, Yongjun,Liu, Chengbu. Theoretical studies on the common catalytic mechanism of transketolase by using simplified models[J]. JOURNAL OF MOLECULAR GRAPHICS & MODELLING,2013,39:23-28.
APA	Sheng, Xiang,Liu, Yongjun,&Liu, Chengbu.(2013).Theoretical studies on the common catalytic mechanism of transketolase by using simplified models.JOURNAL OF MOLECULAR GRAPHICS & MODELLING,39,23-28.
MLA	Sheng, Xiang,et al."Theoretical studies on the common catalytic mechanism of transketolase by using simplified models".JOURNAL OF MOLECULAR GRAPHICS & MODELLING 39(2013):23-28.

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