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Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei
Qin, Zhen1; Yan, Qiaojuan2; Ma, Qingjun3; Jiang, Zhengqiang1
2015-10-23
Source PublicationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume466Issue:3Pages:431-437
SubtypeArticle
AbstractL-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.
KeywordCrystal Structure L-serine Ammonia-lyase Serine Dehydratase Beta-elimination Enzymes Rhizomucor Miehei Pyridoxal-5 '-phosphate
DOI10.1016/j.bbrc.2015.09.043
Indexed BySCI
Language英语
WOS IDWOS:000363094400025
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/73939
Collection实验海洋生物学重点实验室
Affiliation1.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
Recommended Citation
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.
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