Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum

CORC > 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

	Structural and Mutational Studies on the Unusual Substrate Specificity of meso-Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum
	Liu, Weidong; Li, Zhe; Huang, Chun-Hsiang; Guo, Rey-Ting; Zhao, Leiming; Zhang, Dalong; Chen, Xi; Wu, Qiaqing; Zhu, Dunming
刊名	CHEMBIOCHEM
	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
内容类型	期刊论文
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.