Catalytic isomerization of glucose to fructose by immobilized glucose isomerase in an aqueous-ethanol medium was studied. Using Michaelis-Menten equation and Haldane relationship, the main kinetic parameters were determined: Kmf, Vmf, Kmr, Vmr. By comparing the aqueous-ethanol medium with an aqueous solution, the measured values of Kmr and Kmf were increased in the aqueous-ethanol solution, whi...

A comparison is made between conventional Michaelis-Menten kinetics and two models that take into account the duration of the conformational changes that take place at the molecular level during the catalytic cycle of a monomer. The models consider the time that elapses from the moment an enzyme-substrate complex forms until the moment a product molecule is released, as well as the recovery tim...

It has been previously proposed that acetylene reduction data at subsaturating acetylene concentrations could be interpreted by use of the Michaelis-Menten equation, based on the acetylene concentration external to the nodules. One difficulty of this view is that the assumption that the system is not diffusion limited is violated when studying intact nodules. The presence of a gas diffusion bar...

Most biological processes are controlled by complex systems of enzymatic chemical reactions. Although the majority of enzymatic networks have very elaborate structures, there are many experimental observations indicating that some turnover rates still follow a simple Michaelis-Menten relation with a hyperbolic dependence on a substrate concentration. The original Michaelis-Menten mechanism has ...