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

• approximation. These had the form of a kcat/KM ratio (a specificity constant), but just for a part of the overall reaction. For example, in a ping-pong reaction, if we think of the first two steps independently, the KM would be (k−1 + k2)/k1, and the kcat would be k2, so the specificity constant equivalent is

• Supporting Information File 1). Hence the eeDP is actually equal to SCRb times this function of other rate constants. It is intuitively reasonable that there should be an important role for this pseudo-specificity constant, which applies to the reaction of the favoured enantiomer product with the acyl enzyme

New standards for collecting and fitting steady state kinetic data

• Kenneth A. Johnson

Beilstein J. Org. Chem. 2019, 15, 16–29, doi:10.3762/bjoc.15.2

• –Menten equation in terms of kcat and kcat/Km values: v = kSP[S]/(1 + kSP[S]/kcat), where the specificity constant, kSP = kcat/Km. In this short review, the rationale for this assertion is explained and it is shown that more accurate measurements of kcat/Km can be derived directly using the modified form

• kcat/Km. Keywords: computer simulation; data fitting; enzyme catalysis; induced-fit; Michaelis constant; specificity constant; Review When Henri, Michaelis and Menten derived the equation for steady state enzyme turnover, they chose to define the rate in terms of Vmax and the substrate dissociation

• is better to fit the data using an equation that provides kcat/Km directly using the following form of the Michaelis–Menten equation: We use the term kSP = kcat/Km to emphasize that the specificity constant (kSP) is a single parameter rather than a ratio and to stress that it represents the apparent