Enzyme-catalyzed asymmetric acylation and hydrolysis of cis-2,5-disubstituted tetrahydrofuran derivatives: Contribution to development of models for reactions catalyzed by porcine liver esterase and porcine pancreatic lipase

Article abstract of DOI:10.1016/S0957-4166(00)80131-7

Pig liver esterase, lipase from porcine pancreas, lipase from Pseudomonas sp. (lipase YS), and lipase from Candida cylindracea catalyzed hydrolyses of the cis-diacetate 1 and the trans-diacetate (±)-4 to give the cis-monoacetate 3 and the trans-monoacetate 6 in optically active forms, respectively. Lipase YS-catalyzed acylations of the cis-diol 2 and the trans-diol (±)-5 with an acylating agent in cyclohexane yielded (-)-3 and (-)-6, respectively. The group adjacent to the R stereogenic center preferentially reacted in lipase YS-catalyzed hydrolyses of 1 and (±)-4 and acylations of 2 and (±)-5, and the enantioselectivites are rationalized by our rule recently proposed for lipase YS.