INVESTIGADORES
ENRIZENRIZ] ricardoricardo] danieldaniel]
artículos
Título:
Catalytic and Molecular Properties of Rabbit Liver Carboxylesterase Acting on 1,8-Cineole Derivatives
Autor/es:
LOANDOS M.; MURO A.; VILLECO M.; MASMAN M.; LUITEN P.; ANDUJAR S.; SUVIRE F.; ENRIZENRIZ] R.
Revista:
NATURAL PRODUCT COMMUNICATIONS
Editorial:
NATURAL PRODUCTS INC
Referencias:
Lugar: Westerville, Ohio; Año: 2012
ISSN:
1934-578X
Resumen:
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
rds']