Lipase-catalyzed kinetic resolution of 2-aminocyclopentane- and 2-aminocyclohexanecarboxamides

Abstract

Candida antarctica lipase B (CAL-B)-catalyzed N-acylation with 2,2,2-trifluoroethyl butanoate in solvent mixtures of tert-butyl methyl ether and tert-amyl alcohol was used to prepare all the enantiomers of cis- and trans-2-aminocyclopentane- and -cyclohexanecarboxamides. An unexpected change in enantiopreference, accompanied by low enantioselectivity, was observed when Pseudomonas cepacia lipase (cis-cyclohexane substrate) or C. antarctica lipase A (cis-cyclopentane and -cyclohexane substrates) replaced CAL-B. © 2006 Elsevier Ltd. All rights reserved.