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Pure Appl. Chem., 1992, Vol. 64, No. 8, pp. 1187-1191

http://dx.doi.org/10.1351/pac199264081187

Pig liver esterase catalyzed hydrolysis: Substrate specificity and stereoselectivity

Ch. Tamm

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  • Noguchi Naoyoshi, Tsuna Kazuhiro, Nakada Masahisa: Research on the pig liver esterase (PLE)-catalyzed kinetic resolution of half-esters derived from prochiral diesters. Tetrahedron: Asymmetry 2013, 24, 357. <http://dx.doi.org/10.1016/j.tetasy.2013.01.019>
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  • Masterson Douglas S., Rosado Dale A., Nabors Cassie: Development of a practical mass spectrometry based assay for determining enantiomeric excess. A fast and convenient method for the optimization of PLE-catalyzed hydrolysis of prochiral disubstituted malonates. Tet Asymm 2009, 20, 1476. <http://dx.doi.org/10.1016/j.tetasy.2009.05.037>
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  • Hummel Anke, Brüsehaber Elke, Böttcher Dominique, Trauthwein Harald, Doderer Kai, Bornscheuer Uwe T.: Isoenzymes of Pig-Liver Esterase Reveal Striking Differences in Enantioselectivities. Angew Chem Int Ed 2007, 46, 8492. <http://dx.doi.org/10.1002/anie.200703256>
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  • Provencher Louis, Wynn Hla, Jones J.Bryan, Krawczyk Andrzej R.: Enzymes in organic synthesis 51. Probing the dimensions of the large hydrophobic pocket of the active site of pig liver esterase. Tet Asymm 1993, 4, 2025. <http://dx.doi.org/10.1016/S0957-4166(00)82251-X>