Kinetics of enzyme-catalysed desymmetrisation of prochiral substrates: product enantiomeric excess is not always constant

Peter J. Halling
Beilstein J. Org. Chem. 2021, 17, 873–884. https://doi.org/10.3762/bjoc.17.73

Supporting Information

A single file of Supporting Information is available. It contains the Methods section, with full details of how simulations were performed and the mathematical analysis of the various kinetic mechanisms. It also gives a fuller index of data files (Maple worksheets for the full derivations; MATLAB code files to run the simulations; Excel files containing all calculated progress curves) that can be downloaded via: https://doi.org/10.15129/fbd7e7c0-9712-41a4-a88d-63eecccdd2d9.

Supporting Information File 1: Methods, full details of simulations, and mathematical analysis of kinetic mechanisms. Index of data files and download link.
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Kinetics of enzyme-catalysed desymmetrisation of prochiral substrates: product enantiomeric excess is not always constant
Peter J. Halling
Beilstein J. Org. Chem. 2021, 17, 873–884. https://doi.org/10.3762/bjoc.17.73

How to Cite

Halling, P. J. Beilstein J. Org. Chem. 2021, 17, 873–884. doi:10.3762/bjoc.17.73

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  • Watts, O. F. B.; Berreur, J.; Collins, B. S. L.; Clayden, J. Biocatalytic Enantioselective Synthesis of Atropisomers. Accounts of chemical research 2022, 55, 3362–3375. doi:10.1021/acs.accounts.2c00572
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