Limitations of enzymatic acylation using oxime esters: Cosubstrate inhibition and the reversibility of the reaction

Summary Enzymatic resolution of (±)-endo-bicyclo2.2.1]hept-5-en-2-ol (1a) catalysed byCandida cylindracea lipase using either acetoneoxime acetate (2a) or biacetyldioxime diacetate (3a) as acyl donor proceeds with moderate to good enantioselectivity (E=13 and 22, resp.) although clear limitations of this method are observed: firstly, a severe depletion of the reaction rate at elevated cosubstrate (acyl donor) concentrations and secondly, the reversibility of the reaction.