Enzyme kinetics is the study of enzyme reaction rates. Enzymes act as catalysts and accelerate reactions by lowering activation energy. Determining enzyme kinetics allows understanding of the chemical mechanism of enzyme reactions by measuring how reaction velocity changes with substrate concentration. The Michaelis-Menten model describes this relationship and defines parameters like Vmax and KM. Reaction rates can be zero-order, first-order, or follow the Michaelis-Menten equation.
Enzyme kinetics is the study of enzyme reaction rates. Enzymes act as catalysts and accelerate reactions by lowering activation energy. Determining enzyme kinetics allows understanding of the chemical mechanism of enzyme reactions by measuring how reaction velocity changes with substrate concentration. The Michaelis-Menten model describes this relationship and defines parameters like Vmax and KM. Reaction rates can be zero-order, first-order, or follow the Michaelis-Menten equation.
Enzyme kinetics is the study of enzyme reaction rates. Enzymes act as catalysts and accelerate reactions by lowering activation energy. Determining enzyme kinetics allows understanding of the chemical mechanism of enzyme reactions by measuring how reaction velocity changes with substrate concentration. The Michaelis-Menten model describes this relationship and defines parameters like Vmax and KM. Reaction rates can be zero-order, first-order, or follow the Michaelis-Menten equation.
ENZYME KINETICS • Enzyme kinetics is the study of rates of enzymatic reactions. • Enzyme act as catalyst and play critical role in accelerating reactions 103 to 1017 times faster than the reaction would normally proceed. • Catalysts lower the activation energy of the reaction. Importance of determining enzyme kinetics? • An important goal of measuring enzyme kinetics is to determine the chemical mechanism of an enzyme reaction, i.e., the sequence of chemical steps that transform substrate into product. Each enzyme catalyzes a single reaction or a limited number of chemical reactions, and it is specific for a substrate that it converts to a defined enzyme. The Michaelis-Menten Model • It takes the form of an equation relating reaction velocity to substrate concentration for a system where a substrate S binds reversibly to an enzyme E to form an enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and to regenerate the free enzyme E. This system can be represented schematically as follows: MICHAELIS-MENTEN EQUATION • Vmax represents the maximum velocity achieved by the system, at maximum (saturating) substrate concentrations. • KM (the Michaelis constant; sometimes represented as KS instead) is the substrate concentration at which the reaction velocity is 50% of the Vmax. • [S] is the concentration of the substrate S. • This is a plot of the Michaelis-Menten equation’s predicted reaction velocity as a function of substrate concentration, with the significance of the kinetic parameters Vmax and KM graphically depicted. • The best derivation of the Michaelis-Menten equation was provided by George Briggs and J.B.S. Haldane in 1925, and a version of it follows: ENZYMATIC REACTION • Zero-order reaction – reaction rate depends only on enzyme concentration. • First-order reaction – reaction rate is directly proportional to substrate concentration. • Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934. • https://www.youtube.com/watch?v=Cck3US2EBmU • https://www.youtube.com/watch?v=y43pIHUtjeM