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顺式-环氧琥珀酸水解酶产生手性纯 d(-)-酒石酸的催化机制的结构见解。

Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(-)-tartaric acid.

机构信息

Shandong Provincial Key Laboratory of Synthetic Biology and CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Songling Road 189, Qingdao, Shandong 266101, China.

出版信息

Chem Commun (Camb). 2018 Jul 26;54(61):8482-8485. doi: 10.1039/c8cc04398a.

DOI:10.1039/c8cc04398a
PMID:30003205
Abstract

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.

摘要

顺式-环氧琥珀酸水解酶的晶体结构测定和突变分析，该酶产生对映体纯的 d(-)-酒石酸，揭示了锌离子和必需残基在小对称底物催化反应的立体选择性机制中的作用。

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