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Merck

Enhancing the enantioselectivity of an epoxide hydrolase by directed evolution.

Organic letters (2004-01-16)
Manfred T Reetz, Claudia Torre, Andreas Eipper, Renate Lohmer, Marcus Hermes, Birgit Brunner, Andrea Maichele, Marco Bocola, Michael Arand, Annette Cronin, Yvonne Genzel, Alain Archelas, Roland Furstoss
ABSTRAKT

[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.

MATERIAŁY
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Sigma-Aldrich
1,2-Epoxy-3-phenoxypropane, technical grade
Sigma-Aldrich
1,2-Epoxy-3-phenoxypropane, 99%