Enzymes offer one of the best ways of producing enantiomerically pure compounds due to their great stereoselectivity and therefore they are increasingly being used to obtain pharmaceuticals. Since it is proven that the wrong enantiomer can cause harmful and serious side effects, chirality is a key factor in obtaining safe and effective medications. In this paper, a cascade reaction kinetics has been studied using genetically modified and lyophilized whole cells of Escherichia coli, in which two enzymes that catalyse the reaction were overexpressed. The first step of the reaction was catalysed by the enzyme 2-keto-3-deoxy-L-ramonate-aldolase – YfaU 013. It is an aldol addition between sodium pyruvate and formaldehyde and where 4-hydroxy-2-oxobutanoate is formed which together with L-alanine participates in the second step of reaction called transamination (or reductive amination) catalysed by transaminase – TA 039. The goal of this cascade reaction is to obtain an amino acid L-homoserine which represents a building block for the synthesis of other important and essential amino acids. Kinetics of the cascade reaction were investigated using the initial reaction rate method, and the kinetic parameters (Km, Vm) were estimated from the experimental data. A mathematical model of cascade reaction was developed and simulations were carried out using the program package SCIENTIST to find the conditions at which it is possible to obtain a satisfactory product concentration as well as volume productivity in the reactor.