Enhancing the Enantioselectivity of an Epoxide Hydrolase by Directed Evolution
Organic Letters2003Vol. 6(2), pp. 177–180
Citations Over TimeTop 10% of 2003 papers
Manfred T. Reetz, Claudia Torre, Andreas Eipper, Renate Lohmer, Marcus Hermes, Birgit Brunner, Andrea J. Maichele, Marco Bocola, Michael Arand, Annette Cronin, Yvonne Genzel, Alain Archelas, Roland Furstoss
Abstract
[reaction: see text] The epoxide hydrolase (EH) from Aspergillus niger, which shows a selectivity factor of only E = 4.6 in the hydrolytic kinetic resolution of glycidyl phenyl ether, has been subjected to directed evolution for the purpose of enhancing enantioselectivity. After only one round of error-prone polymerase chain reaction (epPCR), enantioselectivity was more than doubled (E = 10.8). The improved mutant enzyme contains three amino acid exchanges, two of which are spatially far from the catalytically active center.
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