Pig liver esterase (PLE)-mediated resolution of N-substituted 4-benzoyloxy-3-carbomethoxypiperidines: a convenient preparation of 4-hydroxy- and 4-benzoyloxy-3-carbomethoxypiperidines in enantiomerically pure form

Pig liver esterase (PLE) afforded smooth chemical resolution of racemic N-substituted 4-(benzoyloxy)-3-carbomethoxypiperidines. The enzyme showed good chemo- and enantioselective properties, thus allowing discrimination between the carbomethoxy and benzoate ester groups, the latter being more easily...

Full description

Saved in:
Bibliographic Details
Published inTetrahedron: asymmetry Vol. 11; no. 21; pp. 4397 - 4405
Main Authors Roberti, Marinella, Rondanin, Riccardo, Ferroni, Roberto, Baruchello, Riccardo, Invidiata, Francesco Paolo, Andrisano, Vincenza, Bertucci, Carlo, Bertolasi, Valerio, Grimaudo, Stefania, Tolomeo, Manlio, Simoni, Daniele
Format Journal Article
LanguageEnglish
Published OXFORD Elsevier Ltd 03.11.2000
Elsevier
Subjects
Chemistry
Chemistry, Inorganic & Nuclear
Chemistry, Organic
Chemistry, Physical
Physical Sciences
Science & Technology
CHEMISTRY
COCAINE
LIPASE
ANALOGS
Online AccessGet full text

Cover

More Information
Summary:Pig liver esterase (PLE) afforded smooth chemical resolution of racemic N-substituted 4-(benzoyloxy)-3-carbomethoxypiperidines. The enzyme showed good chemo- and enantioselective properties, thus allowing discrimination between the carbomethoxy and benzoate ester groups, the latter being more easily hydrolyzed. The proposed methodology also represents a practical means for the procurement of N-substituted 4-hydroxy-3-carbomethoxypiperidines in enantiomerically pure form.
ISSN:0957-4166
1362-511X
DOI:10.1016/S0957-4166(00)00404-3