Andujar, S.A.

Enriz, R.D.

Loandos, M.D.H.

Luiten, P.G.M.

Masman, M.F.

Muro, A.C.

Suvire, F.D.

Villecco, M.A.B.

Rabbit liver carboxylesterase (rCE) was evaluated as the catalyst for the enantioselective hydrolysis of (+/-)-3-endo-acetyloxy-1,8-cineole [(+/-)-4], which yields (1S,3S,4R)-(+)-3-acetyloxy-1,8-cineole [(+)-4] and (1R,3R,4S)-(-)-3-hydroxy-1,8-cineole [(-)-3]. Enantioselective asymmetrization of meso-3,5-diacetoxy-1,8-cineol (5) gives (1S,3S,4R,5R)-(-)-3-acetyloxy-5-hydroxy-1,8-cineole (6), with high enantioselectivity. rCE has been chosen to perform both experiments and molecular modeling simulations. Docking simulations combined with molecular dynamics calculations were used to study rCE-catalyzed enantioselective hydrolysis of cineol derivatives. Both compounds were found to bind with their acetyl groups stabilized by hydrogen bond interactions between their oxygen atoms and Ser221.</p

ARTS repository - University of Groningen

Catalytic and molecular properties of rabbit liver carboxylesterase acting on 1,8-cineole derivatives

Catalytic and molecular properties of rabbit liver carboxylesterase acting on 1,8-cineole derivatives

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ARTS repository - University of Groningen