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Investigation of the Cosolvent Effect on Six Isoenzymes of PLE in the Enantioselective Hydrolysis of Selected α,α‐Disubstituted Malonate Esters
Author(s) -
Smith Maureen E.,
Banerjee Souvik,
Shi Yongliang,
Schmidt Marlen,
Bornscheuer Uwe T.,
Masterson Douglas S.
Publication year - 2012
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201100490
Subject(s) - esterase , malonate , hydrolysis , enantioselective synthesis , chemistry , phthalimide , organic chemistry , isozyme , enzyme , catalysis
Six pigs in a pot: Pig liver esterase (PLE) is among the most widely studied esterase enzymes utilized in organic synthesis. Here we illustrate that the six recombinantly produced isoenzymes of PLE exhibit varying enantioselectivity during the hydrolysis of α,α‐disubstituted malonate esters in cosolvent mixtures. We have observed a rare cosolvent‐induced reversal of enantioselectivity for isoenzyme PLE 6 in the hydrolysis of a phthalimide‐containing α,α‐disubstituted malonate ester.