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Studies on structure-function relationships of acetolactate decarboxylase from Enterobacter cloacae

文献类型：期刊论文

作者Ji, Fangling1; Feng, Yanbin3; Li, Mingyang1; Yang, Yongliang1; Wang, Tianqi1; Wang, Jingyun1; Bao, Yongming1,2; Xue, Song3
刊名RSC ADVANCES
出版日期2018
卷号8期号:68页码:39066-39073
ISSN号2046-2069
DOI10.1039/c8ra07379a
通讯作者Ji, Fangling(fanglingji@dlut.edu.cn) ; Xue, Song(xuesong@dicp.ac.cn)
英文摘要Acetoin is an important bio-based platform chemical with wide applications. Among all bacterial strains, Enterobacter cloacae is a well-known acetoin producer via -acetolactate decarboxylase (ALDC), which converts -acetolactate into acetoin and is identified as the key enzyme in the biosynthetic pathway of acetoin. In this work, the enzyme properties of Enterobacter cloacae ALDC (E.c.-ALDC) were characterized, revealing a K-m value of 12.19 mM and a k(cat) value of 0.96 s(-1). Meanwhile, the optimum pH of E.c.-ALDC was 6.5, and the activity of E.c.-ALDC was activated by Mn2+, Ba2+, Mg2+, Zn2+ and Ca2+, while Cu2+ and Fe2+ significantly inhibited ALDC activity. More importantly, we solved and reported the first crystal structure of E.c.-ALDC at 2.4 angstrom resolution. The active centre consists of a zinc ion coordinated by highly conserved histidines (199, 201 and 212) and glutamates (70 and 259). However, the conserved Arg150 in E.c.-ALDC orients away from the zinc ion in the active centre of the molecule, losing contact with the zinc ion. Molecular docking of the two enantiomers of -acetolactate, (R)-acetolactate and (S)-acetolactate allows us to further investigate the interaction networks of E.c.-ALDC with the unique conformation of Arg150. In the models, no direct contacts are observed between Arg150 and the substrates, which is unlikely to maintain the stabilization function of Arg150 in the catalytic reaction. The structure of E.c.-ALDC provides valuable information about its function, allowing a deeper understanding of the catalytic mechanism of ALDCs.
WOS关键词CIRCULAR-DICHROISM ; PURIFICATION ; ACETOIN ; ELECTROSTATICS ; MECHANISM ; AEROGENES ; CLONING ; PYTHON
资助项目National Science Foundation of China[21506025] ; Dalian University of Technology Science Foundation[DUT8LK08]
WOS研究方向Chemistry
语种英语
WOS记录号WOS:000451090800044
出版者ROYAL SOC CHEMISTRY
资助机构National Science Foundation of China ; National Science Foundation of China ; Dalian University of Technology Science Foundation ; Dalian University of Technology Science Foundation ; National Science Foundation of China ; National Science Foundation of China ; Dalian University of Technology Science Foundation ; Dalian University of Technology Science Foundation ; National Science Foundation of China ; National Science Foundation of China ; Dalian University of Technology Science Foundation ; Dalian University of Technology Science Foundation ; National Science Foundation of China ; National Science Foundation of China ; Dalian University of Technology Science Foundation ; Dalian University of Technology Science Foundation
源URL[http://cas-ir.dicp.ac.cn/handle/321008/166610]  
专题大连化学物理研究所_中国科学院大连化学物理研究所
通讯作者Ji, Fangling; Xue, Song
作者单位1.Dalian Univ Technol, Sch Life Sci & Biotechnol, Dalian 116024, Liaoning, Peoples R China
2.Dalian Univ Technol, Sch Food & Environm Sci & Engn, Panjin 12422, Liaoning, Peoples R China
3.Chinese Acad Sci, Dalian Inst Chem Phys, Marine Bioengineering Grp, Dalian 116023, Liaoning, Peoples R China
推荐引用方式
GB/T 7714		 Ji, Fangling,Feng, Yanbin,Li, Mingyang,et al. Studies on structure-function relationships of acetolactate decarboxylase from Enterobacter cloacae[J]. RSC ADVANCES,2018,8(68):39066-39073.
APA Ji, Fangling.,Feng, Yanbin.,Li, Mingyang.,Yang, Yongliang.,Wang, Tianqi.,...&Xue, Song.(2018).Studies on structure-function relationships of acetolactate decarboxylase from Enterobacter cloacae.RSC ADVANCES,8(68),39066-39073.
MLA Ji, Fangling,et al."Studies on structure-function relationships of acetolactate decarboxylase from Enterobacter cloacae".RSC ADVANCES 8.68(2018):39066-39073.

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来源：大连化学物理研究所

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