Enzymes in organic synthesis 50. Probing the dimensions of the large hydrophobic binding region of the active site of pig liver esterase using substituted aryl malonate substrates

DOI: 10.1016/S0957-4166(00)86155-8

Source and publish data:

Tetrahedron Asymmetry p. 1041 - 1052 (1991)

Update date:2022-08-06

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Authors:

Toone Toone

Jones Jones

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Article abstract of DOI:10.1016/S0957-4166(00)86155-8

The active side model reported recently for the synthetically useful enzyme pig liver esterase (PLE) permits the structural specificity and stereoselectivity of the enzyme to be interpreted and predicted for a wide range of substrates. The specifications

Full text of DOI:10.1016/S0957-4166(00)86155-8

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