engleski

Enantioselective formation and ring-opening of epoxides catalyzed by halohydrin dehalogenases

Halohydrin dehalogenases catalyze the conversion of vicinal halohydrins to their corresponding epoxides, while releasing halide ions. They can be found in several bacteria that use halogenated alcohols or compounds that are degraded via halohydrins as a carbon source for growth. Biochemical and structural studies have shown that halohydrin dehalogenases are evolutionary and mechanistically related to enzymes of the short-chain dehydrogenase/reductase (SDR) superfamily. In the reverse reaction, which is epoxide-ring opening, different nucleophiles can be accepted, including azide, nitrite and cyanide. This allows the biocatalytic production of several β -substituted alcohols from epoxides. In these oxirane-ring opening reactions, the halohydrin dehalogenase from Agrobacterium radiobacter displays high enantioselectivity, making it possible to use the enzyme for the preparation of enantiopure building blocks for fine chemicals.

biocatalysis; azide; cyanide; epoxide; halohydrin dehalogenase

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