Pig liver esterase (PLE) catalyzed hydrolysis of dimethyl and diethyl 2-methyl-2-(o- nitrophenoxy) malonates affords (R)-monoethyl/monomethyl 2-methyl-2-(o-nitrophenoxy) malonates in moderate to good enantiomeric excesses (69–81%). These data indicate that the nitro group may be accommodated in the large hydrophobic pocket of the Jones active- site model of PLE.
