Facile biocatalytic syntheses of optically active 4-hydroxycyclohex-2-enone and 4-benzylthiacyclopent-2-enone

Autor: Ben S. Morgan, Stanley M. Roberts, Dorothée Hoenner, Paul Evans
Rok vydání: 2004
Předmět:
Zdroj: Tetrahedron: Asymmetry. 15:2807-2809
ISSN: 0957-4166
DOI: 10.1016/j.tetasy.2004.07.042
Popis: Novozyme 435® (Candida antarctica Lipase B) effects the kinetic resolution of both 3-benzylthia-4-hydroxycyclopentanone and its six-membered ring analogue, providing a novel route to both enantiomers of 4-benzylthiacyclopent-2-enone and the two enantiomers of 4-hydroxycyclohex-2-enone, all in a state of very high optical purity.
Databáze: OpenAIRE