Chymotrypsin selectively catalyzed the hydrolysis of a series of 3-ethoxycarbonyl-Delta(2)-isoxazolines 1-4, whereas lipase from Pseudomonas cepacia (lipase PS) was remarkably selective in hydrolysing the corresponding 3-hydroxymethyl-Delta(2)-isoxazoline butyrates (5-8). The enantio-preference of chymotrypsin for the first set of compounds is the same as that observed for the lipase PS-cataiyzed hydrolysis of the other series of substrates. The hydrolytic activity of lipase PS for compounds 5-8 was considerably higher than that shown by chymotrypsin for substrates 1-4. (C) 1996 Elsevier Science Ltd

Nitrile oxides in medicinal chemistry .6. Enzymatic resolution of a set of bicyclic Delta(2)-isoxazolines / M. De Amici, C. De Micheli, G. Carrea, S. Riva. - In: TETRAHEDRON-ASYMMETRY. - ISSN 0957-4166. - 7:3(1996), pp. 787-796. [10.1016/0957-4166(96)00075-4]

Nitrile oxides in medicinal chemistry .6. Enzymatic resolution of a set of bicyclic Delta(2)-isoxazolines.

M. De Amici;C. De Micheli;
1996

Abstract

Chymotrypsin selectively catalyzed the hydrolysis of a series of 3-ethoxycarbonyl-Delta(2)-isoxazolines 1-4, whereas lipase from Pseudomonas cepacia (lipase PS) was remarkably selective in hydrolysing the corresponding 3-hydroxymethyl-Delta(2)-isoxazoline butyrates (5-8). The enantio-preference of chymotrypsin for the first set of compounds is the same as that observed for the lipase PS-cataiyzed hydrolysis of the other series of substrates. The hydrolytic activity of lipase PS for compounds 5-8 was considerably higher than that shown by chymotrypsin for substrates 1-4. (C) 1996 Elsevier Science Ltd
Settore CHIM/08 - Chimica Farmaceutica
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/184436
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