PLE catalyzed hydrolyses of α-substituted α-hydroxy esters: The influence of the substituents

DOI: 10.1016/S0957-4166(00)86125-X

Source and publish data:

Tetrahedron Asymmetry p. 705 - 720 (1991)

Update date:2022-07-30

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Authors:

Moorlag Moorlag

Kellogg Kellogg

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Article abstract of DOI:10.1016/S0957-4166(00)86125-X

The enzymatic hydrolyses of a variety of α-substituted mandelic and lactic esters using pig liver esterase (PLE) have been investigated. High to moderate enantioselectivity was found for various α-substituted mandelic esters, whereas PLE showed low to no enantioselectivity for α-substituted lactic esters. We observed that the enantioselectivity of PLE depends strongly on the length and nature of the substituent at the α-position. Some sequences for an active site model of PLE are discussed.

Full text of DOI:10.1016/S0957-4166(00)86125-X

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