Kinetics of Bi-Substrate Enzymes and Allosteric Enzymes

These flashcards cover key vocabulary and concepts related to bi-substrate enzyme kinetics and the characteristics of allosteric enzymes.

Enzyme-Substrate Complex

A transient molecular complex formed when an enzyme binds its substrate.

Allosteric Site

A site on an enzyme where a molecule can bind, influencing the activity of the enzyme.

Kinetics

The study of the rates of enzyme-catalyzed reactions.

Vmax

The maximum reaction velocity achieved by an enzyme at saturated substrate concentration.

Km (Michaelis constant)

The substrate concentration at which the reaction velocity is half of Vmax.

Heterotrophic Interaction

Occurs when the binding of a ligand affects the affinity of another ligand for a different site on the enzyme.

Homotropic Interaction

Binding of a substrate on one subunit affects the binding of the substrate to another subunit of the same enzyme.

Sequential Order Mechanism

A mechanism where substrates must bind to the enzyme in a specific order.

Steady State Hypothesis

Theory that the concentration of the enzyme-substrate complex remains constant over the course of the reaction.

Hill's Equation

An equation used to describe the sigmoidal nature of enzyme activity as a function of substrate concentration.