Enzymes in organic synthesis. 47. Active-site model for interpreting and predicting the specificity of pig liver esterase

1990 ◽  
Vol 112 (12) ◽  
pp. 4946-4952 ◽  
Author(s):  
Eric J. Toone ◽  
Michael J. Werth ◽  
J. Bryan Jones
Keyword(s):  
Organic Synthesis ◽  
Active Site ◽  
Pig Liver ◽  
Pig Liver Esterase ◽  
Site Model ◽  
Liver Esterase ◽  
Active Site Model ◽  
Enzymes In Organic Synthesis

Enzymic Hydrolysis of Methyl 2,3-O-Acetyl-5-Deoxy-α and β-D-Xylofuranosides - An Active-Site Model of Pig Liver Esterase

1997 ◽  
Vol 16 (7) ◽  
pp. 1011-1028 ◽  
Author(s):  
Jitka Moravcová ◽  
Zita Vanclová ◽  
Jindra Čapková ◽  
Karel Kefurt ◽  
Jan Staněk
Keyword(s):  
Active Site ◽  
Enzymic Hydrolysis ◽  
Pig Liver ◽  
Pig Liver Esterase ◽  
Site Model ◽  
Liver Esterase ◽  
Active Site Model ◽  
Hydrolysis Of

Enzymes in organic synthesis. 33. Stereoselective pig liver esterase-catalyzed hydrolyses of meso cyclopentyl-, tetrahydrofuranyl-, and tetrahydrothiophenyl-1,3-diesters

1985 ◽  
Vol 63 (2) ◽  
pp. 452-456 ◽  
Author(s):  
J. Bryan Jones ◽  
R. Scott Hinks ◽  
Philip G. Hultin
Keyword(s):  
Organic Synthesis ◽  
Absolute Configuration ◽  
Enantiomeric Excess ◽  
Membered Ring ◽  
Pig Liver ◽  
Pig Liver Esterase ◽  
Preparative Scale ◽  
Liver Esterase ◽  
The Absolute ◽  
Enzymes In Organic Synthesis

Preparative-scale pig liver esterase-catalyzed hydrolyses of five-membered ring meso-1,3-diesters are enantiotopically selective. While pro-S enantiotopic selectivity is exhibited in each case, the absolute configuration sense of the hydrolysis in the cyclopentyl series is opposite to that of both the tetrahydrofuranyl and tetrahydrothiophenyl diesters. The enantiomeric excess levels induced are in the 34–46% range.

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