With the rise of SARS-CoV-2 and other similar viral infections, the ability to predict rate of mutation and transmissibility has become an increasingly important topic in the science community at large. This infection can be described well by using the enzymatic reaction model; the CoV spike is cleaved by the body’s protease enzyme, and this severed spike then participates in the entry of the virus into the body. Though often overlooked and set to zero, the reverse reaction constant, called k2, may prove to be a critical step in this analysis. The object of this study is to find said rate constant, the Michaelis constant, and the turnover number, so that the above and other related topics may be studied in more depth. Tools derived from enzyme kinetics, paired with simulated and measured reaction data have been used to conduct this study. Trends were analyzed using both algebraic and graphical methods to make connections between our known and desired rate constants. Perhaps determining this reverse constant may help us better understand the reaction and lead to the ability to predict spike protein mutation trends.

Determining enzyme kinetic rate constants to predict viral enzyme mutations

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