Issue 61, 2018
From the journal:

Chemical Communications

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

Sheng Dong,ab   Xi Liu,‡c   Gu-Zhen Cui,§ab   Qiu Cui,*ab   Xinquan Wang*c  and  Yingang Feng ORCID logo *ab  

* Corresponding authors

a 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
E-mail: cuiqiu@qibebt.ac.cn, fengyg@qibebt.ac.cn

b Qingdao Engineering Laboratory of Single Cell Oil, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, Shandong 266101, China

c Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China
E-mail: xinquanwang@mail.tsinghua.edu.cn

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.

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

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Article information

DOI
https://doi.org/10.1039/C8CC04398A
Article type
Communication
Submitted
01 Jun 2018
Accepted
09 Jul 2018
First published
09 Jul 2018

Chem. Commun., 2018,54, 8482-8485

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

S. Dong, X. Liu, G. Cui, Q. Cui, X. Wang and Y. Feng, Chem. Commun., 2018, 54, 8482 DOI: 10.1039/C8CC04398A

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