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, doi:10.3762/bjoc.17.73

• Peter J. Halling WestCHEM, Dept Pure & Applied Chemistry, University of Strathclyde, Glasgow G1 1XL, Scotland, UK 10.3762/bjoc.17.73 Abstract The kinetics of enzymatic desymmetrisation were analysed for the most common kinetic mechanisms: ternary complex ordered (prochiral ketone reduction); ping

• study if and how the product ee declines at high conversion. Keywords: enantiomeric excess; enzyme; kinetic mechanisms; kinetic parameters; prochiral; Introduction There is great interest in using enzymatic catalysis in the synthesis of homochiral molecules. An early approach was to use

• , often quite substantially. Understanding this effect, and features of the enzyme and reaction conditions that can minimise it, is important for the optimal design of enzymatic desymmetrisation reactions. Results and Discussion Scheme 1 shows the kinetic mechanisms that cover most applications of