Issue 58, 2014
From the journal:

Chemical Communications

Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase†

Shanshan Wang,‡a   Yao Nie,‡a   Yan Xu,*a   Rongzhen Zhang,a   Tzu-Ping Ko,b   Chun-Hsiang Huang,c   Hsiu-Chien Chan,c   Rey-Ting Guo*c  and  Rong Xiaod  

* Corresponding authors

a School of Biotechnology and Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China
E-mail: yxu@jiangnan.edu.cn
Fax: +86-510-85864112
Tel: +86-510-85918201

b Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan

c Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China
E-mail: guo_rt@tib.cas.cn
Fax: +86-022-84861926
Tel: +86-022-84861999

d Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ 08854, USA

Abstract

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.

Graphical abstract: Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase

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Article information

DOI
https://doi.org/10.1039/C4CC01752H
Article type
Communication
Submitted
08 Mar 2014
Accepted
30 Apr 2014
First published
01 May 2014

Chem. Commun., 2014,50, 7770-7772

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Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase

S. Wang, Y. Nie, Y. Xu, R. Zhang, T. Ko, C. Huang, H. Chan, R. Guo and R. Xiao, Chem. Commun., 2014, 50, 7770 DOI: 10.1039/C4CC01752H

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