Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase
文献类型:期刊论文
作者 | Wang, Shanshan1,2; Nie, Yao1,2; Xu, Yan1,2; Zhang, Rongzhen1,2; Ko, Tzu-Ping3; Huang, Chun-Hsiang4; Chan, Hsiu-Chien4; Guo, Rey-Ting4; Xiao, Rong5 |
刊名 | CHEMICAL COMMUNICATIONS
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出版日期 | 2014 |
卷号 | 50期号:58页码:7770-7772 |
英文摘要 | Structure-guided design of substrate-binding pocket inversed the stereoselectivity of an NADH-dependent medium-chain alcohol dehydrogenase (MDR) from Prelog to anti-Prelog. The pocket-forming amino acids, especially the unconserved residues as hotspots, play critical roles in directing MDRs' stereoselectivity. |
WOS标题词 | Science & Technology ; Physical Sciences |
类目[WOS] | Chemistry, Multidisciplinary |
研究领域[WOS] | Chemistry |
关键词[WOS] | THERMOANAEROBACTER-ETHANOLICUS ; P450 BM3 ; REDUCTION ; MUTATION ; HYDROXYLATION ; SPECIFICITY ; INVERSION ; KETONES |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000338296300003 |
公开日期 | 2014-12-23 |
源URL | [http://124.16.173.210/handle/311007/538] ![]() |
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 | 1.Jiangnan Univ, Minist Educ, Sch Biotechnol, Wuxi 214122, Peoples R China 2.Jiangnan Univ, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Peoples R China 3.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan 4.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China 5.Rutgers State Univ, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA |
推荐引用方式 GB/T 7714 | Wang, Shanshan,Nie, Yao,Xu, Yan,et al. Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase[J]. CHEMICAL COMMUNICATIONS,2014,50(58):7770-7772. |
APA | Wang, Shanshan.,Nie, Yao.,Xu, Yan.,Zhang, Rongzhen.,Ko, Tzu-Ping.,...&Xiao, Rong.(2014).Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.CHEMICAL COMMUNICATIONS,50(58),7770-7772. |
MLA | Wang, Shanshan,et al."Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase".CHEMICAL COMMUNICATIONS 50.58(2014):7770-7772. |
入库方式: OAI收割
来源:天津工业生物技术研究所
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