Studies on structure-function relationships of acetolactate decarboxylase from enterobacter cloacae
文献类型：期刊论文
| 作者 | Ji, Fangling1; Feng, Yanbin2; Li, Mingyang1; Yang, Yongliang1; Wang, Tianqi1; Wang, Jingyun1; Bao, Yongming1,3; Xue, Song2 |
| 刊名 | Rsc advances
 |
| 出版日期 | 2018 |
| 卷号 | 8期号:68页码:39066-39073 |
| ISSN号 | 2046-2069 |
| DOI | 10.1039/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 |
| WOS研究方向 | Chemistry |
| WOS类目 | Chemistry, Multidisciplinary |
| 语种 | 英语 |
| WOS记录号 | WOS:000451090800044 |
| 出版者 | ROYAL SOC CHEMISTRY |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2373062 |
| 专题 | 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.Chinese Acad Sci, Dalian Inst Chem Phys, Marine Bioengineering Grp, Dalian 116023, Liaoning, Peoples R China 3.Dalian Univ Technol, Sch Food & Environm Sci & Engn, Panjin 12422, 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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