Biochem Chap 12

a mathematical expression for the time-dependent profress of a reaction as a funtion of reactant concentration

The proprtionality constant between the velocity of a cemical reaction and the concentration(s) of the reactant(s)

The enzyme-substrate complex, whose formation is a key component of the Michaelis-Menten model of enzyme action. Also known as the Mechaelis complex

the rate constant for the second step of a simple enzyme-catalyzed reaction that follows Michaelis-Menten kinetics that is the conversion of the ES complex to E + P

the rate constant for the reverse reaction e.g. breakdown of the ES complex to E+S

a set of conditions in an open system under which the formation and degradation of individual components are balanced such that the system does not change over time

a condition for the application of the Michaelis-Menten model to an enzymatic reaction, in which the concentration of the ES complex remains unchanged over the course of the reaction

for an enzyme that follows the Michaelis-Menten model, K_M= (k_-1+ k₂)/k₁ , K_M is equal to the substrate concentration at which the reaction velocity is half-maximal

mathmatical expression that desribes the activity of an enzyme in terms of the substrate concentration [S], the enzyme maximal velocity (V_max) and its Michaelis constant K_M: v₀= V_max[S]/ (K_M+ [S])

initial velocity of an enzymatic reaction

maximal velocity of an enzymatic reaction

a state in which the substrate concentration is so high that essentially all the enzyme molecules are in the ES form.

the catalytic constant for an enzymatic reaction, equivalent to the ratio of the macimal velocity (V_max) and the enzyme concentration ([E]_T)

the apparent second-order rate constant for an enzyme-catalyzed reaction; it is a measure of an ezyme's catalytic efficiency

the theoretical maximum rate of an enzymatic reaction in solution, about 10⁸ to 10⁹ M^-1s^-1

• a. k₁
• b. None of these
• c. k_-1
• d. k₂