Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 26, Pages 6641-6644Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201402653
Keywords
enantioselectivity; enzyme catalysis; kinetic resolution; protein engineering; structure-activity relationships
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Funding
- National Natural Science Foundation of China [21276082]
- Ministry of Science and Technology, P.R. China [2011AA02A210, 2011CB710800]
- Shanghai Commission of Science and Technology [11431921600]
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Microtuning of the enzyme active pocket has led to a smart library of epoxide hydrolase variants with an expanded substrate spectrum covering a series of typical beta-blocker precursors. Improved activities of 6- to 430-fold were achieved by redesigning the active site at two predicted hot spots. This study represents a breakthrough in protein engineering of epoxide hydrolases and resulted in enhanced activity toward bulky substrates.
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