4.7 Article

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

Journal

CHEMICAL COMMUNICATIONS
Volume 50, Issue 58, Pages 7770-7772

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c4cc01752h

Keywords

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Funding

  1. National Key Basic Research and Development Program of China [2011CB710800]
  2. National Hi-Tech Research and Development Program of China [2011AA02A209, 2011AA02A210]
  3. National Natural Science Foundation of China [21336009, 21376107]
  4. Program of Introducing Talents of Discipline to Universities [111-2-06]
  5. High-End Foreign Experts Recruitment Program [GDW20133200113]
  6. Priority Academic Program Development of Jiangsu Higher Education Institutions

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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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