Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei
文献类型：期刊论文
| 作者 | Qin, Zhen1; Yan, Qiaojuan2; Ma, Qingjun3; Jiang, Zhengqiang1 |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2015-10-23 |
| 卷号 | 466期号:3页码:431-437 |
| 关键词 | Crystal structure L-Serine ammonia-lyase Serine dehydratase beta-Elimination enzymes Rhizomucor miehei Pyridoxal-5 '-phosphate |
| 英文摘要 | L-serine ammonia-lyase, as a member of the beta-family of pyridoxal-5'-phosphate (PLP) dependent enzymes, catalyzes the conversion of L-serine (L-threonine) to pyruvate (a-ketobutyrate) and ammonia. The crystal structure of L-serine ammonia-lyase from Rhizomucor miehei (RmSDH) was solved at 1.76 A resolution by X-ray diffraction method. The overall structure of RmSDH had the characteristic beta-family PLP dependent enzyme fold. It consisted of two distinct domains, both of which show the typical open twisted alpha/beta structure. A PLP cofactor was located in the crevice between the two domains, which was attached to Lys52 by a Schiff-base linkage. Unique residue substitutions (Gly78, Pro79, Ser146, Ser147 and Thr312) were discovered at the catalytic site of RmSDH by comparison of structures of RmSDH and other reported eukaryotic L-serine ammonia-Iyases. Optimal pH and temperature of the purified RmSDH were 7.5 and 40 degrees C, respectively. It was stable in the pH range of 7.0-9.0 and at temperatures below 40 degrees C. This is the first crystal structure of a fungal L-serine ammonia-lyase. It will be useful to study the catalytic mechanism of beta-elimination enzymes and will provide a basis for further enzyme engineering. (C) 2015 Elsevier Inc. All rights reserved. |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000363094400025 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/73939]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing 100083, Peoples R China 2.China Agr Univ, Coll Engn, Beijing 100083, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Qin, Zhen,Yan, Qiaojuan,Ma, Qingjun,et al. Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2015,466(3):431-437. |
| APA | Qin, Zhen,Yan, Qiaojuan,Ma, Qingjun,&Jiang, Zhengqiang.(2015).Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,466(3),431-437. |
| MLA | Qin, Zhen,et al."Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 466.3(2015):431-437. |
入库方式： OAI收割
来源：海洋研究所
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