What are the benefits of measuring the initial rate of a reaction Vå for use in kineticstudies? (This is a multi-select question).[ES] can be measured accurately.changes in [S] are negligible, so the value of [S] is known.changes in Km are negligible, so Km can be treated as a constant.V₁ = Vmax.-->A negligible amount of product has formed, so that the back reaction P --need not be considered.ES

Recall that the rate of a chemical reaction is dC/dt where dC is the change in the analyte…

Answered: What are the benefits of measuring the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 10²/s. Calculate the Ks and KM for this reaction. Does substrate binding achieve equilibrium or steady state?
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity. K is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (ro) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position. Estimate the values for Vmax and Km- Vmax= µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 75 50 Km = 25 K 0 10 20 30 V max 40 50 [S] (M) 1/2 V max Michaelis-Menten curve 60 70 80 90 100 HM
The typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURK
The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows: Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your work
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Explain how the observation that reaction (B) runs faster than reaction (A) is related to the enzyme catalysis.
A competitive inhibitor interacts with the free enzyme to form an enzyme•inhibitor complex(E•I). This equilibrium reaction can be described as follows:E + I ⇌ EIModify the simplified kinetic scheme for the reaction E + S ⇌ E + P to include this equilibriumexpression
1) Is the ratio of the forward rate constant and reverse rate constant changed by the presence of an enzyme catalyst? 2) 4) What is the simplest mathematical relationship between substrate concentrations [S], initial velocity (Vo) of an enzyme catalyzed reaction, the maximal velocity of the reaction (Vmax), and the ½ maximal Vo (i.e. Km) ? (Hint: what is the Michaelis-Menten Equation? 3) Graphically illustrate the most useful derivation of the Michaelis-Menton equation (that darn linearized, double-reciprocal)

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