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

@article{Wang2014UnconservedSS,
  title={Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.},
  author={Shanshan Wang and Yao Nie and Yan Xu and Rongzhen Zhang and Tzu-Ping Ko and Chun-Hsiang Huang and Hsiu-chien Chan and Rey-Ting Guo and Rong Xiao},
  journal={Chemical communications},
  year={2014},
  volume={50 58},
  pages={7770-2}
}
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. 
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