STRUCTURAL EVALUATION OF THE ENZYMATIC RESOLUTION OF TRICYCLO[5.2.1.02,6]DECENE-2-CARBOXYLATES USING PIG’S LIVER ESTERASE

Abstract

Moderate to excellent entantio- and stereoselectivities (ee’s 54-100%) were observed in PLE catalyzed hydrolysis of (±)-ethyl 5-oxo-endo-tricyclo[5.2.1.02,6] deca-8-ene-2-carboxylate 5 and the structurally related open chain bicyclic structures (±)-ethyl 3-acetylbicyclo[2.2.1]hept-5-ene-2-carboxylates 7, 9 and (±)-ethyl 3-propanoylbicyclo[2.2.1]hept-5-ene-2-carboxylates 8, 10. A pronounced preference for hydrolysis of the exo- vs. the endo-ester function was observed.