High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism
文献类型：期刊论文
| 作者 | Song, Liya; Wang, Mingzhu; Shi, Jiaji; Xue, Zhiquan; Wang, Mei-Xiang; Qian, Shijun |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2007-10-19 |
| 卷号 | 362期号:2页码:319-324 |
| 关键词 | Nitrile Hydratase Rhodococcus Erythropolis Aj270 Post-translational Modification Mechanism |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2007.07.184 |
| 英文摘要 | The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3 angstrom resolution. The two cysteine residues (alpha Cys(112) and alpha Cys(114)) equatorially coordinated to the ferric ion were post-translation ally modified to cysteine sulfinic acids. A glutamine residue (alpha Gln(90)) in the active center gave double conformations. Based on the interactions among the enzyme, substrate and water molecules, a new mechanism of biocatalysis of nitrile hydratase was proposed, in which the water molecule activated by the glutamine residue performed as the nucleophile to attack on the nitrile which was simultaneously interacted by another water molecule coordinated to the ferric ion. (C) 2007 Elsevier Inc. All rights reserved. |
| 语种 | 英语 |
| WOS记录号 | WOS:000249464800017 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/62201]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Wang, Mei-Xiang |
| 作者单位 | 1.Chinese Acad Sci, Inst Chem, Ctr Mol Sci, Biol Chem Lab, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Inst Microbiol, State Key Labs Transducer Technol, Beijing 100101, Peoples R China 3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China 4.Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Song, Liya,Wang, Mingzhu,Shi, Jiaji,et al. High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2007,362(2):319-324. |
| APA | Song, Liya,Wang, Mingzhu,Shi, Jiaji,Xue, Zhiquan,Wang, Mei-Xiang,&Qian, Shijun.(2007).High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,362(2),319-324. |
| MLA | Song, Liya,et al."High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 362.2(2007):319-324. |
入库方式： OAI收割
来源：化学研究所
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