Enzymatic Catalysis: Mechanisms and Kinetics

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Description

This lecture covers the kinetics of enzymatic catalysis, focusing on the Michaelis-Menten model and sequential reactions. It explains how enzymes lower activation energy, the induced fit model, and the transition state theory. The lecture also discusses equilibrium reactions, pseudo-first order kinetics, and experimental techniques for measuring adsorption and desorption.

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Related concepts (28)

Enzyme catalysis

Enzyme catalysis is the increase in the rate of a process by a biological molecule, an "enzyme". Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site. Most enzymes are made predominantly of proteins, either a single protein chain or many such chains in a multi-subunit complex. Enzymes often also incorporate non-protein components, such as metal ions or specialized organic molecules known as cofactor (e.

Activation energy

In chemistry and physics, activation energy is the minimum amount of energy that must be provided for compounds to result in a chemical reaction. The activation energy (Ea) of a reaction is measured in joules per mole (J/mol), kilojoules per mole (kJ/mol) or kilocalories per mole (kcal/mol). Activation energy can be thought of as the magnitude of the potential barrier (sometimes called the energy barrier) separating minima of the potential energy surface pertaining to the initial and final thermodynamic state.

Transition state

In chemistry, the transition state of a chemical reaction is a particular configuration along the reaction coordinate. It is defined as the state corresponding to the highest potential energy along this reaction coordinate. It is often marked with the double dagger ‡ symbol. As an example, the transition state shown below occurs during the SN2 reaction of bromoethane with a hydroxide anion: The activated complex of a reaction can refer to either the transition state or to other states along the reaction coordinate between reactants and products, especially those close to the transition state.

Enzyme kinetics

Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is typically a protein molecule that promotes a reaction of another molecule, its substrate (S).

Activated complex

In chemistry an activated complex is defined by the International Union of Pure and Applied Chemistry (IUPAC) as "that assembly of atoms which corresponds to an arbitrary infinitesimally small region at or near the col (saddle point) of a potential energy surface". In other words, it refers to a collection of intermediate structures in a chemical reaction that persist while bonds are breaking and new bonds are forming.