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Issue 58, 2014
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Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase

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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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Supplementary files

Article information


Submitted
08 Mar 2014
Accepted
30 Apr 2014
First published
01 May 2014

Chem. Commun., 2014,50, 7770-7772
Article type
Communication

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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