Biochem 5.1 Michaelis-Menten Equation Overview

The study of how quickly enzymes catalyze reactions, focusing on the rate of substrate consumption or product production as a function of substrate and enzyme amounts.

A measure of the amount of substrate consumed or product produced per unit time.

The rate of substrate consumption or product production as a function of substrate and enzyme amounts.

The maximum possible reaction velocity of an enzyme-catalyzed reaction.

A constant that represents the substrate concentration at which the reaction velocity is half of Vmax.

The equation that describes the relationship between reaction velocity, Vmax, Km, and substrate concentration.

Different enzymes that catalyze the same reaction but may have different kinetic parameters.

The first step in an enzyme-catalyzed reaction, where the enzyme binds to the substrate.

The second step in an enzyme-catalyzed reaction, where the substrate is converted to a product.

The final step in an enzyme-catalyzed reaction, where the product is released from the enzyme.

A key assumption in Michaelis-Menten kinetics stating that the enzymatic reaction proceeds only in one direction, from substrate to product. The formation of product is considered irreversible, meaning the product does not revert back to substrate, and the product does not bind back to the enzyme.

A critical assumption in Michaelis-Menten kinetics that posits the concentration of the enzyme-substrate complex (ES) remains constant throughout the experiment. This means the rate of ES formation equals the rate of ES breakdown.

This assumption is crucial for applying Michaelis-Menten kinetics to experimental measurements and states that during the early stages of the reaction, the concentration of free substrate (S) remains constant. This allows for the simplification of the kinetic equations.

The initial velocity of an enzymatic reaction, measured at the very beginning of the reaction when the substrate concentration is high and the product concentration is very low.

The rate constant for the conversion of the enzyme-substrate complex to product, reflecting the efficiency of the enzyme's catalytic activity.

A type of enzyme kinetics that does not follow Michaelis-Menten kinetics, because these enzymes exhibit cooperative binding, meaning the binding of one substrate molecule influences subsequent substrate binding.

Experiments examining the kinetics of enzymes in a controlled laboratory setting, usually using isolated enzymes and specific substrates.

The study of enzyme kinetics as it occurs within a living organism, considering the complex environment and interactions within the cell or tissue.

A principle that states that when a stress is applied to a system in equilibrium, the system will shift in a direction that relieves the stress.

A model that describes enzyme kinetics by assuming a simple, one-step reaction where an enzyme binds to a substrate to form an enzyme-substrate complex, which then breaks down to produce product and release the enzyme.