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

@inproceedings{Gyarmati2003LipasecatalyzedKR,
  title={Lipase-catalyzed kinetic resolution of 7-, 8- and 12-membered alicyclic β-amino esters and N-hydroxymethyl-β-lactam enantiomers},
  author={Zsuzsanna Cs. Gyarmati and Arto Liljeblad and Mikko Rintola and G{\'a}bor Bern{\'a}th and Liisa T. Kanerva},
  year={2003}
}
  • Zsuzsanna Cs. Gyarmati, Arto Liljeblad, +2 authors Liisa T. Kanerva
  • Published 2003
  • Chemistry
  • 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… CONTINUE READING

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