The halohydrin dehalogenase from Agrobacterium radiobacter AD1 (HheC) catalyzes nucleophilic ring opening of epoxides with cyanide and azide. In the case of 2,2-disubstituted epoxides, this reaction proceeds with excellent enantioselectivity (E values up to >200), which gives, by kinetic resolution, access to various enantiopure epoxides and β-substituted tertiary alcohols (ee up to 99%). Since the enzyme has a broad substrate range and because these tertiary alcohols are difficult to prepare in other ways, HheC is an attractive biocatalyst for the production of β-cyano and β-azido tertiary alcohols.
|Nummer van het tijdschrift||7|
|Status||Published - 2007|