Structural Analysis Reveals the Substrate-Binding Mechanism for the Expanded Substrate Specificity of Mutant meso-Diaminopimelate Dehydrogenase
Liu, Weidong; Guo, Rey-Ting; Chen, Xi; Li, Zhe; Gao, Xiuzhen; Huang, Chun-Hsiang; Wu, Qiaqing; Feng, Jinhui; Zhu, Dunming
刊名CHEMBIOCHEM
2015-04-13
卷号16期号:6页码:924-929
关键词amination dehydrogenases enzyme catalysis protein structures structural biology
英文摘要A meso-diaminopimelate dehydrogenase (DAPDH) from Clostridium tetani E88 (CtDAPDH) was found to have low activity toward the D-amino acids other than its native substrate. Site-directed mutagenesis similar to that carried out on the residues mutated by Vedha-Peters et al. resulted in a mutant enzyme with highly improved catalytic ability for the synthesis of D-amino acids. The crystal structures of the CtDAPDH mutant in apo form and in complex with meso-diaminopimelate (meso-DAP), D-leucine (D-leu), and 4-methyl-2-oxopentanoic acid (MOPA) were solved. meso-DAP was found in an area outside the catalytic cavity; this suggested a possible two-step substrate-binding mechanism for meso-DAP. D-leu and MOPA each bound both to Leu154 and to Gly155 in the open form of CtDAPDH, and structural analysis revealed the molecular basis for the expanded substrate specificity of the mutant meso-diaminopimelate dehydrogenases.
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 ; CORYNEBACTERIUM-GLUTAMICUM ; SYMBIOBACTERIUM-THERMOPHILUM ; 3-DIMENSIONAL STRUCTURE ; CRYSTALLOGRAPHY ; MICROBIOLOGY ; MUTAGENESIS ; REFINEMENT ; NUTRITION ; CREATION
收录类别SCI
语种英语
WOS记录号WOS:000352489300006
内容类型期刊论文
源URL[http://124.16.173.210/handle/834782/1453]  
专题天津工业生物技术研究所_生物催化与绿色化工 朱敦明_期刊论文
作者单位Chinese Acad Sci, Ind Enzymes Natl Engn Lab, Tianjin Inst Ind Biotechnol, Tianjin Airport Econ Area, Tianjin 300308, Peoples R China
推荐引用方式
GB/T 7714
Liu, Weidong,Guo, Rey-Ting,Chen, Xi,et al. Structural Analysis Reveals the Substrate-Binding Mechanism for the Expanded Substrate Specificity of Mutant meso-Diaminopimelate Dehydrogenase[J]. CHEMBIOCHEM,2015,16(6):924-929.
APA Liu, Weidong.,Guo, Rey-Ting.,Chen, Xi.,Li, Zhe.,Gao, Xiuzhen.,...&Zhu, Dunming.(2015).Structural Analysis Reveals the Substrate-Binding Mechanism for the Expanded Substrate Specificity of Mutant meso-Diaminopimelate Dehydrogenase.CHEMBIOCHEM,16(6),924-929.
MLA Liu, Weidong,et al."Structural Analysis Reveals the Substrate-Binding Mechanism for the Expanded Substrate Specificity of Mutant meso-Diaminopimelate Dehydrogenase".CHEMBIOCHEM 16.6(2015):924-929.
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