Effect of substrate concentration on the enantioselectivity of cyclohexanone monooxygenase from Acinetobacter calcoaceticus and its rationalization

The ee values of lactone 3, and not of lactone 2, obtained from the enantiodivergent oxidation of racemic bicyclo[3.2.0]hept-2-en-6-one 1, catalyzed by cyclohexanone monooxygenase from Acinetobacter calcoaceticus, were found to be markedly dependent on the degree of conversion and substrate concentr...

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Published inTetrahedron: asymmetry Vol. 11; no. 18; pp. 3653 - 3657
Main Authors Zambianchi, F, Pasta, P, Ottolina, G, Carrea, G, Colonna, S, Gaggero, N, Ward, J.M
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 22.09.2000
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Summary:The ee values of lactone 3, and not of lactone 2, obtained from the enantiodivergent oxidation of racemic bicyclo[3.2.0]hept-2-en-6-one 1, catalyzed by cyclohexanone monooxygenase from Acinetobacter calcoaceticus, were found to be markedly dependent on the degree of conversion and substrate concentration. The results are rationalized on the basis of a model which hypothesizes the binding of a second substrate molecule to an enzyme site distinct from the catalytic site.
ISSN:0957-4166
1362-511X
DOI:10.1016/S0957-4166(00)00354-2