Dipeptide analogues of fluorinated aminophosphonic acid sodium salts as moderate competitive inhibitors of cathepsin C

• Karolina Wątroba,
• Małgorzata Pawełczak and
• Marcin Kaźmierczak

Beilstein J. Org. Chem. 2023, 19, 434–439, doi:10.3762/bjoc.19.33

• = maximum reaction velocity, KM = Michaelis constant, Kic = competitive inhibitory constant, Kiu = uncompetitive inhibitory constant, [S] = concentration of the substrate, [I] = concentration of the inhibitor. Conclusion In conclusion, we demonstrated the solvolysis reaction of dipeptide analogues of

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

• 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

• provides a lower limit for the second order rate constant for substrate binding. Similarly, kcat provides a lower limit for each first order rate constant following substrate binding through product release. On the other hand, the Michaelis constant cannot be interpreted unambiguously in the absence of

• kcat and kcat/Km, so we consider that the Michaelis constant is a derivative of the two primary steady state kinetic parameters. Although this statement appears as trivial algebra, it is profound because kcat and kcat/Km can reflect different steps in the enzyme pathway as will be described below

Hybrid biofunctional nanostructures as stimuli-responsive catalytic systems

• Gernot U. Marten,
• Thorsten Gelbrich and
• Annette M. Schmidt

Beilstein J. Org. Chem. 2010, 6, 922–931, doi:10.3762/bjoc.6.98

• -Bowden plot, Figure 5a), a hyperbolic behavior is observed that can nicely be fitted by the Michaelis Menten equation. The graph trends towards the saturation rate vmax, and the Michaelis constant Km, respectively; where Data linearization can be achieved by the Eadie–Hofstee method [59] (Figure 5b) by

• @P(O8M’84S8)-Try dispersions. While the Michaelis constant Km of free trypsin decreases slowly with temperature, for particle-immobilized trypsin a strong increase is observed for temperatures above the Tc of the polymer, indicating a decrease in complex stability, probably due to shell collapse or

• kinetic data of trypsin activity, and b) Eadie–Hofstee diagram for the temperature-dependent kinetic data of nanocarrier activity. a) Turnover number kcat and b) Michaelis constant Km of particle- immobilized trypsin vs free trypsin. Synthesis of magnetic biocatalyst particles. Reaction scheme of the