Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum
文献类型：期刊论文
| 作者 | Liu, Weidong; Li, Zhe; Huang, Chun-Hsiang; Guo, Rey-Ting; Zhao, Leiming; Zhang, Dalong; Chen, Xi; Wu, Qiaqing; Zhu, Dunming |
| 刊名 | CHEMBIOCHEM
 |
| 出版日期 | 2014-01-24 |
| 卷号 | 15期号:2页码:217-222 |
| 关键词 | amination enzyme catalysis meso-diaminopimelate dehydrogenase mutagenesis protein structure |
| 英文摘要 | Wild-type meso-diaminopimelate dehydrogenase (DAPDH) is usually specific to the native substrate, meso-2,6-diaminopimelate. Recently, a DAPDH from Symbiobacterium thermophilum (StDAPDH) was found to exhibit expanded substrate specificity. As such, its crystal structures in apo form and in complex with NADP(+) and both NADPH and meso-DAP were investigated to reveal the structural basis of its unique catalytic properties. Structural analysis results show that StDAPDH should prefer an ordered kinetic catalytic mechanism. A second substrate entrance tunnel with Met152 at its bottleneck was found, through which pyruvate/D-alanine might bind and enter the catalytic cavity, providing some structural insights into its high activity toward pyruvate. The side chain of Met152 might interact with Asp92 and Asn253, thus affecting the domain motion and catalysis. These results offer useful information for understanding the unique catalytic properties of StDAPDH and guiding further engineering of this enzyme. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Medicinal |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Pharmacology & Pharmacy |
| 关键词[WOS] | AMINO-ACID DEHYDROGENASE ; ALPHA-KETO ACIDS ; CORYNEBACTERIUM-GLUTAMICUM ; BACILLUS-SPHAERICUS ; CRYSTALLOGRAPHY ; PURIFICATION ; REFINEMENT ; REDUCTION ; CREATION ; BINDING |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000329877400005 |
| 公开日期 | 2014-12-23 |
| 源URL | [http://124.16.173.210/handle/311007/548]  |
| 专题 | 天津工业生物技术研究所_结构生物学与蛋白酶学实验室 郭瑞庭_期刊论文 |
| 作者单位 | Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin Airport Econ Area, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Weidong,Li, Zhe,Huang, Chun-Hsiang,et al. Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum[J]. CHEMBIOCHEM,2014,15(2):217-222. |
| APA | Liu, Weidong.,Li, Zhe.,Huang, Chun-Hsiang.,Guo, Rey-Ting.,Zhao, Leiming.,...&Zhu, Dunming.(2014).Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum.CHEMBIOCHEM,15(2),217-222. |
| MLA | Liu, Weidong,et al."Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum".CHEMBIOCHEM 15.2(2014):217-222. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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