Enzyme Kinetics and Drug Development

These flashcards cover key vocabulary and concepts related to enzyme kinetics and drug development, aiding in understanding the enzymatic processes that impact drug efficacy and biochemical reactions.

Enzyme Kinetics

The study of the rates of enzyme-catalyzed reactions.

Michaelis-Menten Equation

A mathematical model that describes the rate of enzyme-catalyzed reactions as a function of substrate concentration, which involves parameters such as Km and Vmax.

Vmax

The maximum initial velocity of an enzyme-catalyzed reaction when the enzyme is saturated with substrate.

Km (Michaelis constant)

The substrate concentration at which the reaction rate is half of Vmax, indicating the affinity of the enzyme for its substrate.

Lineweaver-Burk Plot

A double-reciprocal plot that linearizes the Michaelis-Menten equation, allowing for easier determination of Km and Vmax.

Zero Order Kinetics

A situation in enzyme kinetics where the reaction rate is constant and does not depend on substrate concentration, typically occurring at high substrate levels.

Optimum pH

The specific pH level at which an enzyme exhibits maximum activity.

Enzyme Inhibitors

Substances that decrease the activity of an enzyme by binding to it, affecting its ability to convert substrate to product.

Substrate concentration

The amount of substrate present in a reaction which affects the rate of enzyme activity.

Enzyme Activity

The rate at which an enzyme converts substrate into product, influenced by factors such as temperature, pH, and concentration.