Enantiotopic Selectivity of-Pig Liver Esterase Isoenzymes

Abstract
Pig liver esterase was separated into isoenzyme fractions with known subunit compositions. The fractions showed differences in enantiotopic ester group selectivity in hydrolysis of two substrates of synthetic value, benzylmethylpropanedioic acid dimethyl ester and cis-N-benzyl-2,5-bismethoxy-carbonylpyrrolidine. A difference in aliphatic chain length specificity between the isoenzyme fractions was also observed. The results indicate that pig liver esterase cannot be regarded as homogeneous when used in organic synthesis.

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