Related Experiment Video
Updated: Jul 5, 2026

Monitoring Intraspecies Competition in a Bacterial Cell Population by Cocultivation of Fluorescently Labelled Strains
Published on: January 18, 2014
Analysis of negative cooperativity for glutamate dehydrogenase
1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow. kurganov@gagarinclub.ru
Abstract:
The empirical equation, which describes negative cooperativity in the enzyme kinetics, has been proposed. The equation is obtained from the Michaelis-Menten equation where the Michaelis constant is replaced by the effective Michaelis constant, which is a linear function of the v/Vmax ratio (v is the rate of the enzymatic reaction and Vmax is the limiting value of v at saturating concentrations of substrate). The equation allows the limiting values of the Michaelis constant at v/Vmax --> 0 and V/Vmax --> 1 to be estimated, K0 and Klim, respectively. The Klim/K0 ratio is considered as a quantitative characteristic of negative cooperativity. The applicability of the equation has been demonstrated for the kinetic data obtained for glutamate dehydrogenases from various sources (negative kinetic cooperativity for coenzyme). The negative cooperativity for the functions of saturation of protein by ligand is also analyzed. The data on binding of spin-labeled NAD, NADH, and NADPH by beef liver glutamate dehydrogenase are used as examples.
More Related Videos
Related Concept Videos
Negative Regulator Molecules
Enzyme Inhibition
Ligand Binding and Linkage
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions

