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

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' st...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2014-01, Vol.50 (58), p.7770-7772
Main Authors: Wang, Shanshan, Nie, Yao, Xu, Yan, Zhang, Rongzhen, Ko, Tzu-Ping, Huang, Chun-Hsiang, Chan, Hsiu-Chien, Guo, Rey-Ting, Xiao, Rong
Format: Article
Language:English
Subjects:
Alcohol dehydrogenase
Alcohol Dehydrogenase - chemistry
Amino acids
Binding Sites
Hot spots
Humans
Molecular Docking Simulation
Pocket
Residues
Stereoisomerism
Stereoselectivity
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc01752h