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中国生物工程杂志

CHINA BIOTECHNOLOGY
中国生物工程杂志
中国生物工程杂志  2010, Vol. 30 Issue (06): 144-150    DOI: Q555+.4
综述     
环糊精葡萄糖基转移酶的结构特征与催化机理
李兆丰1,2**,顾正彪1,2**,堵国成1,3,吴敬1,3,陈坚1,3
1.江南大学食品科学与技术国家重点实验室 无锡 214122
2.江南大学食品学院 无锡 214122
3.江南大学生物工程学院工业生物技术教育部重点实验室 无锡 214122
Structural Characteristics and Catalytic Mechanisms of Cyclodextrin Glycosyltransferase
LI Zhao-feng1,2,GU Zheng-biao1,2,DU Guo-cheng1,3,WU Jing1,3,CHEN Jian1,3
1.State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China
2.School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
3.School of Biotechnology and Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China
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摘要：

随着环糊精在食品、医药等领域的应用越来越广，生产环糊精所必需的环糊精葡萄糖基转移酶 (CGT酶) 已经成为当今研究的热点。特别是近二十年来，国外对该酶进行了比较深入的研究。首先介绍了CGT酶的功能特性与结构特征。CGT酶是一种多功能型酶，能催化三种转糖基反应（歧化、环化和耦合反应）和水解反应，其中，能将淀粉转化为环糊精的环化反应是特征反应；作为α-淀粉酶家族的成员，CGT酶除了具有与α-淀粉酶相同的A、B、C结构域外，还存在D和E结构域。另外，对CGT酶的催化机理包括底物结合方式、转糖苷反应机理以及环化机理等进行了详细的讨论。
关键词： 环糊精;  环糊精葡萄糖基转移酶;  结构特征;  催化机理;  环化反应    
Abstract:

With the applications of cyclodextrins expanding in the industries related to food, pharmaceuticals, etc, cyclodextrin glycosyltransferase (CGTase), the essential enzyme for the production of cyclodextrins, has become the focus of scientific research nowadays. Especially in recent twenty years, CGTase has been studied extensively, leading to increasing knowledge of its structure and function. Firstly the function and structural characteristics of CGTase were focused on. CGTase is a multifunctional enzyme. It can catalyze three transglycosylation reactions (disproportionation, cyclization, and coupling), and a hydrolysis reaction. The specific CGTase reaction is the cyclization reaction, which can result in the formation of a cyclodextrin. CGTase is a member of the α-amylase family of glycosyl hydrolases. α-Amylases generally consist of three structural domains, A, B, and C, while CGTases show a similar domain organization with two additional domains, D and E. In addition, substrate binding of CGTase and mechanisms of transglycosylation and cyclization reactions catalyzed by CGTase were discussed in detail. Domain B contributes to substrate binding by providing several amino acid side chains alongside a substrate binding groove on the surface of the CGTase protein. Maltose binding site assists in guiding the linear starch chains into the substrate binding groove containing at least nine subsites. After the glycosidic bond cleavage reaction has taken place between subsites ＋1 and －1, the non-reducing end of the oligosaccharide at the groove is transferred to the reducing end of the same oligosaccharide chain, leading to cyclic products.
Key words: Cyclodextrin    Cyclodextrin glycosyltransferase    Structural characteristics    Catalytic mechanism    Cyclization reaction
收稿日期: 2010-01-19 出版日期: 2010-06-12
基金资助:

国家“863”计划资助项目(2006AA10Z235)
通讯作者: 李兆丰     E-mail: zhengbiaogu@yahoo.com.cn;zfli@jiangnan.edu.cn
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引用本文:

李兆丰 顾正彪 堵国成 吴敬 陈坚. 环糊精葡萄糖基转移酶的结构特征与催化机理[J]. 中国生物工程杂志, 2010, 30(06): 144-150.

LI Zhao-Feng, GU Zheng-Biao, DU Guo-Cheng, TUN Jing, CHEN Jian. Structural Characteristics and Catalytic Mechanisms of Cyclodextrin Glycosyltransferase. China Biotechnology, 2010, 30(06): 144-150.

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https://manu60.magtech.com.cn/biotech/CN/Q555+.4    或    https://manu60.magtech.com.cn/biotech/CN/Y2010/V30/I06/144

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