Modification of the Enzyme Enantioselectivity by Product Inhibition

A kinetic explanation of solvent effects on the enantioselective hydrolysis of racemic methyl and ethyl 2‐chloropropionate by carboxylesterase NP has been studied. After a general ping‐pong model for the kinetic resolution of chiral esters was defined, the progress curves of the reactions were analy...

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Bibliographic Details
Published in:Biotechnology progress 1994-07, Vol.10 (4), p.403-409
Main Authors: Rakels, J. L. L., Caillat, P., Straathof, A. J. J., Heijnen, J. J.
Format: Article
Language:English
Subjects:
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
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Summary:A kinetic explanation of solvent effects on the enantioselective hydrolysis of racemic methyl and ethyl 2‐chloropropionate by carboxylesterase NP has been studied. After a general ping‐pong model for the kinetic resolution of chiral esters was defined, the progress curves of the reactions were analyzed, and a simplified uni‐uni four‐parameter model was selected. First‐order rate constants and alcohol inhibition constants were determined for both enantiomers. Enantiomeric excess values were correctly predicted from the model. According to the kinetic description, the enantioselectivity could be enhanced or decreased by adding the product alcohol as a cosolvent. It appeared that these changes could be predicted quantitatively by enantioselective product inhibition for alcohol concentrations
ISSN:8756-7938
1520-6033
DOI:10.1021/bp00028a010