Enzyme catalysed ring opening of epoxides (CROSBI ID 544248)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa
Podaci o odgovornosti
Majerić Elenkov, Maja ; Janssen B. Dick
engleski
Enzyme catalysed ring opening of epoxides
Halohydrin dehalogenase catalyse ring opening of epoxide with remarkably wide range of non-natural ionic nucleophiles, such as cyanide, azide and nitrite. The natural role of these enzymes is reversible dehalogenation of vicinal haloalcohols. What makes Hhe attractive for synthetic purposes is the fact that ring opening reactions are irreversible and highly b-regioselective. Morover, reactions can proceed with high enantioselectivity with a wide variety of synthetic substrates. Although not yet commercially available, these enzymes are highly promising biocatalytic tools for the synthesis of optically pure b-substituted alcohols. In our screening among wild-type halohydrin dehalogenases, we have identified enzyme from Agrobacterium radiobacter as the most enantioselective in the cyanide-mediated ring opening reaction of epoxides. The present work reports examples of highly enantioselective production of b-hydroxynitriles and b-azidoalcohols.
halohydrin dehalogenase; epoxides; kinetic resolution; nucleophile
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Podaci o prilogu
2006.
objavljeno
Podaci o matičnoj publikaciji
Book of abstracts, NCCC, Nizozemska, 2006
Podaci o skupu
7th Netherlands Catalysis and Chemistry Conference
predavanje
06.03.2006-08.03.2006
Noordwijkerhout, Nizozemska