ENZYMATIC RESOLUTION OF OXATHIOLANE INTERMEDIATES - AN ALTERNATIVE APPROACH TO THE ANTIVIRAL AGENT LAMIVUDINE (3TC(TM))

Authors
COUSINS RPC MAHMOUDIAN M YOUDS PM
Citation
Rpc. Cousins et al., ENZYMATIC RESOLUTION OF OXATHIOLANE INTERMEDIATES - AN ALTERNATIVE APPROACH TO THE ANTIVIRAL AGENT LAMIVUDINE (3TC(TM)), Tetrahedron : asymmetry, 6(2), 1995, pp. 393-396
Citations number
12
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Inorganic & Nuclear","Chemistry Physical
Journal title
Tetrahedron : asymmetry → ACNP
ISSN journal
09574166
Volume
6
Issue
2
Year of publication
1995
Pages
393 - 396
Database
ISI
SICI code
0957-4166(1995)6:2<393:EROOI->2.0.ZU;2-A
Abstract
A number of commercially available lipases and proteases was screened for the ability to hydrolyse enantioselectively racemic oxathiolane 2. Mucor miehei lipase was identified as the most efficient biocatalyst. Bioconversion of 2 afforded enantiomerically-enriched residual ester of the correct absolute stereochemistry, (-)-2R for subsequent synthes is of the anti-viral agent lamivudine, (3TC(TM)).