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

Sheng Dong; Xi Liu; Gu-Zhen Cui; Qiu Cui; Xinquan Wang; Yingang Feng

doi:10.1039/c8cc04398a

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

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

Authors

Sheng Dong¹, Xi Liu, Gu-Zhen Cui, Qiu Cui, Xinquan Wang, Yingang Feng

Affiliation

¹ 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. cuiqiu@qibebt.ac.cn fengyg@qibebt.ac.cn.

PMID: 30003205
DOI: 10.1039/c8cc04398a

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.