Catalytic and Molecular Properties of Rabbit Liver Carboxylesterase Acting on 1,8-Cineole Derivatives

MARÍA DEL H. LOANDOS; ANA C. MURO; MARGARITA B. VILLECCO; MARCELO F. MASMAN; PAUL G.M. LUITEN; SEBASTIAN A. ANDUJAR; FERNANDO D. SUVIRE; RICARDO D. ENRIZ

NATURAL PRODUCT COMMUNICATIONS

NATURAL PRODUCTS INC

Lugar: Westerville, Ohio; Año: 2012 vol. 7 p. 1117 - 1122

1934-578X

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.