Title: Non-markovian effect in inhibited enzymatic catalysis
Author: Tal tslil rotbart
Enzymatic reactions can be generally described as binding of a substrate molecule to an enzyme to form a complex which ultimately leads to the catalysis of the substrate to product and the unbinding of the complex to a product and an enzyme which is free to start another cycle. These reactions have been well described by the Michaelis –Menten model for more than a century now. However, when one only examines enzyme catalysis in the bulk, many details of the inner mechanisms can be averaged in to very few measurable parameters. New experimental practices have opened the door to observing the catalysis of single enzyme molecules. These experiments, among other things, disputed an underlying assumption of the Michaelis-Menten model that the catalysis of substrate to product can be described as a memory-less process. In this work, we build a model which does not assume memory-less processes to describe the steps on the way to enzymatic catalysis and look in to the implication of such model. In particular we look at the non-trivial effect of increased unbinding rate between the substrate and the enzyme. Moreover, we expanded our model to include the interaction with inhibitors, and show what one might learn on the inner workings of the catalysis even in bulk experiments.