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Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(−)-tartaric acid†
Chemical Communications ( IF 4.9 ) Pub Date : 2018-07-09 00:00:00 , DOI: 10.1039/c8cc04398a
Sheng Dong 1, 2, 3, 4, 5 , Xi Liu 6, 7, 8, 9, 10 , Gu-Zhen Cui 1, 2, 3, 4, 5 , Qiu Cui 1, 2, 3, 4, 5 , Xinquan Wang 6, 7, 8, 9, 10 , Yingang Feng 1, 2, 3, 4, 5
Affiliation  

Crystal structure determination and mutagenesis analysis of a cis-epoxysuccinate hydrolase which produces enantiomerically pure D(−)-tartaric acids revealed a zinc ion and essential residues in the stereoselective mechanism for the catalytic reaction of the small mirror symmetric substrate.

中文翻译:

顺式环氧琥珀酸水解酶产生对映体纯的d(-)-酒石酸 的催化机理的结构见解

产生对映体纯的D(-)-酒石酸的顺式-环氧琥珀酸水解酶的晶体结构确定和诱变分析显示,在小的镜对称底物的催化反应的立体选择机理中,锌离子和必要残基存在。
更新日期:2018-07-09
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