Which expression best describes the enzyme kinetics of the protease found in solution SM?A.V0 = (KM + [S])/Vmax[S]B.V0 = KM[S]/(Vmax + [S])C.V0 = Vmax[S]/(KM + [S])D.V0 = (Vmax + [S])/KM[S]
Question
Which expression best describes the enzyme kinetics of the protease found in solution SM?A.V0 = (KM + [S])/Vmax[S]B.V0 = KM[S]/(Vmax + [S])C.V0 = Vmax[S]/(KM + [S])D.V0 = (Vmax + [S])/KM[S]
Solution
The expression that best describes the enzyme kinetics of the protease found in solution SM is C. V0 = Vmax[S]/(KM + [S]). This is the Michaelis-Menten equation, which is commonly used to describe the kinetics of many enzymes. In this equation, V0 is the initial velocity of the reaction, Vmax is the maximum velocity, [S] is the substrate concentration, and KM is the Michaelis constant, which is the substrate concentration at which the reaction velocity is half of Vmax.
Similar Questions
Which of the following statements is/are correct in enzyme kinetics, if S represents the substrate?Group of answer choicesAt very low substrate concentration, the rate of enzyme reaction is zero order with respect to [S].At all substrate concentrations, the rate of enzyme reaction is first order with respect to [S].At very high substrate concentration, the rate of enzyme reaction is first order with respect to [S].At very high substrate concentration, the rate of enzyme reaction is zero order with respect to [S].At all substrate concentrations, the rate of enzyme reaction is zero order with respect to [S].
Enzyme A catalyzes the conversion of substrate S to product P. When enzyme A is phosphorylated, its kcat value changes from 10 s−1 to 5 s−1 and its KM value changes from 100 μM to 20 μM. If equal concentrations of each enzyme form are used then compared to the unphosphorylated enzyme A, the phosphorylated form:A.has a higher catalytic efficiency and yields a faster reaction rate when [S] < 20 μM.B.has a higher turnover number and yields a faster reaction rate under saturating conditions.C.has a lower affinity for S and yields a slower reaction rate at all [S].D.is allosterically inhibited and yields a lower reaction rate at all [S].
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Velocity Substrate Added (mM)1.3 12.6 24.1 45.1 65.2 10The Vmax for this enzyme is approximately:
A different mode. The kinetics of an enzyme are measured as a function of substrate concentration in the presence and absence of 100 mM inhibitor.aa) What are the values of V max and Km in the presence of inhibitor?
Use the Michaelis-Menten equation to complete the enzyme kinetic data set shown below (fill in the blanks), when Vmax is known to have a value of 100 nM/min. Answer with three significant digits.Substrate concentration (µM) Reaction rate (nM/min)4.00 50.05.00 10.0 20.0
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