Structure-guided engineering ofmeso-diaminopimelate dehydrogenase for enantioselective reductive amination of sterically bulky 2-keto acids
Author:
Affiliation:
1. University of Chinese Academy of Sciences
2. Beijing 100049
3. PR China
4. National Engineering Laboratory for Industrial Enzymes and
5. Tianjin Engineering Research Center of Biocatalytic Technology
Abstract
Structure-guided reshaping the substrate-binding pocket of ameso-diaminopimelate dehydrogenase (StDAPDH) led to a mutant W121L/H227I, which catalyzed the enantioselective reductive amination of some sterically bulky 2-keto acids.
Funder
Natural Science Foundation of Tianjin Municipal Science and Technology Commission
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Catalysis
Link
http://pubs.rsc.org/en/content/articlepdf/2018/CY/C8CY01426D
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