Enzymatic Reaction Kinetics

Enzymatic Reaction Kinetics

• The Michaelis-Menten equation describes the relationship between the rate of an enzymatic reaction (v) and the substrate concentration ([S]).

• Vmax represents the maximum velocity of the reaction, achieved when all enzyme active sites are saturated with substrate.

• KM is the Michaelis constant, representing the substrate concentration at which the reaction rate is half of Vmax.

• The Lineweaver-Burk plot (double reciprocal plot) is used to graphically determine Vmax and KM from experimental data.

• Inhibitors can decrease the rate of enzymatic reactions by binding to the enzyme and interfering with its activity.

• Competitive inhibitors bind to the active site of the enzyme, competing with the substrate.

• Non-competitive inhibitors bind to a different site on the enzyme, changing its conformation and reducing its activity.

• Ki is the dissociation constant of the enzyme-inhibitor complex, reflecting the affinity of the inhibitor for the enzyme.

• The co-substrate plays a crucial role in enzymatic reactions alongside the main substrate.

• NAD+ is a common co-substrate in dehydrogenase enzymes.

• ATP acts as a co-substrate in kinase enzymes.

• Enzymes do not affect the equilibrium constant of a reaction, they only accelerate the rate of reaching equilibrium.

• Acetyl CoA is an important reactant in metabolic reactions that involve C-C bond formation.

• Chymotrypsin is a protease enzyme with a catalytic triad consisting of Ser, His, and Asp residues.

• Arrhenius equation describes the relationship between the rate constant (k) of a reaction and temperature (T).

• The activation energy (Ea) is the minimum energy required for reactants to transition into products.

• The pre-exponential factor (A) accounts for the frequency of collisions between reactant molecules.

• KM is expressed in units of concentration, typically molar (M).

• The equilibrium constant (K) is a ratio of product concentrations to reactant concentrations at equilibrium.

• For a forward reaction with rate constant kf and a backward reaction with rate constant kb, the equilibrium constant K is calculated as K = kf/kb.

Explore the fundamentals of enzymatic reactions, including the Michaelis-Menten equation, Vmax, and KM. Learn about different types of inhibitors and how they affect enzyme activity. This quiz covers key concepts and graphical representations used in enzymatic kinetics.