Lipase-catalyzed kinetic resolution of 7-, 8- and 12-membered alicyclic β-amino esters and N-hydroxymethyl-β-lactam enantiomers

Zsuzsanna Cs Gyarmati, Arto Liljeblad, Mikko Rintola, Gábor Bernáth, Liisa T. Kanerva

Research output: Article

25 Citations (Scopus)


Enzymatic kinetic resolutions of methyl cis-2-aminocycloheptane-, 2-aminocyclooctane- and 2-aminocyclododecanecarboxylates with Candida antarctica lipase A in diisopropyl ether (E >200) and of the corresponding N-hydroxymethyl-β-lactams with Pseudomonas cepacia lipase in dry acetone (E from 27 to >200) has been performed with 2,2,2-trifluoroethyl butanoate as the best acyl donor, with both enantiomers being obtained. trans-13-Hydroxymethyl-13-azabicyclo[10.2.0]tetradecan-14-one was resolved with vinyl butanoate and Candida antarctica lipase B (E=26) in acetone.

Original languageEnglish
Pages (from-to)3805-3814
Number of pages10
JournalTetrahedron Asymmetry
Issue number23
Publication statusPublished - nov. 28 2003


ASJC Scopus subject areas

  • Catalysis
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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