Question

In: Chemistry

The data below were collected for an enzyme-catalyzed reaction. [S] (mM) 0.25 0.50 1.00 2.00 V0...

The data below were collected for an enzyme-catalyzed reaction.

[S] (mM)

0.25

0.50

1.00

2.00

V0 (mM*s-1)

2.00

3.33

5.00

6.67

Determine Vmax and Km for this reaction.

Expert Solution

In the question above they have given different substrate concentration and value of V₀ at each substrate concentration so we can plot Lineweaver–Burk plot which is called as double reciprocal plot to get values of Km and Vmax for above reaction,

According to Michealis-Menten equation ,

V= Vmax[S]/Km+[S]

Taking the reciprocals gives ,

1/V = Km/Vmax[S]+1/Vmax

The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents ?1/Km

plotting 1/v against 1/[S] give a straight line:

y intercept = 1 / Vmax

gradient = Km / Vmax

x intercept = -1/ Km

Now y intercept is 0.1 from the graph,

Therefore 0.1 = 1/Vmax; Vmax= 10 mMS^-1

And x Intercept is = - 1 from the graph,

Therefore -1 = -1/Km; Km = 1 mM

queen_honey_blossom answered 2 years ago

The data below were collected for an enzyme-catalyzed reaction. [S] (mM) .20 .50 2.00 4.00 vo...

The data below were collected for an enzyme-catalyzed reaction. [S] (mM) .20 .50 2.00 4.00 vo (mM*s-1) .37 .83 2.22 3.08 Determine Vmax and Km for this reaction

The following reaction rate data are collected upon analysis of an enzyme catalyzed hydrolysis. The reaction...

The following reaction rate data are collected upon analysis of an enzyme catalyzed hydrolysis. The reaction is carried out with two diﬀerent inhibitors. Determine the modes of inhibition for each inhibitor. (The rates provided are relative to the rate measured in the absence of inhibitor. The enzyme concentration for each set of data is equal.) No inhibitor [S]0 (10−2 M) 1.25 3.84 5.81 7.13 v0 0.398 0.669 0.859 1.000 [I1]– –2mmol/L [S]0 (10−2 M) 1.25 2.5 4.00 5.50 v0 0.179...

The data to the below were collected for the bovine carbonic anhydrase-catalyzed reaction described by CO2...

The data to the below were collected for the bovine carbonic anhydrase-catalyzed reaction described by CO2 (aq) + H2O (l) -->H+ (aq) + HCO3- (aq) [CO2] (mmol * L^-1) R (Ýµmol * L^-1 * s^-1) 1.25 28.74 2.50 48.61 5.00 80.28 20.00 155.59 Use these values to determine the value of KM, the Michaelis-Menten constant. Answer the four parts below. a) If you were to plot this data to graphically determine Rmax and KM using a Lineweaver-Burk plot, what would...

An enzyme catalyzed reaction has a Km of 3.76 mM and a Vmax of 6.72 nM/s....

An enzyme catalyzed reaction has a Km of 3.76 mM and a Vmax of 6.72 nM/s. What is the reaction velocity in nM/s, when the substrate concentrations are: A. 0.500 mM B. 15.6 mM C. 252 mM D. Now assume you have added a competitive inhibitor that has a concentration of 15.6 µM with a KI of 7.30 µM to the enzyme in question 9. Calculate the velocity at the same substrate concentrations as above: E. 0.500 mM F. 15.6...

Consider the following data for an enzyme catalyzed hydrolysis reaction in the presence and absence of...

Consider the following data for an enzyme catalyzed hydrolysis reaction in the presence and absence of inhibitor I: [Substrate] M vo (µmol/min) voI (µmol/min) 6x10-6 20.8 4.2 1x10-5 29 5.8 2x10-5 45 9 6x10-5 67.6 13.6 1.8x10-4 87 16.2 Use the above data, do the following: a. Generate Lineweaver-Burk plots of the data. b. Explain the significance of the x-interecpt, y-intercept, and the slope. c. Identify the type of inhibition.

1. If the enzyme-catalyzed reaction E + S ↔ ES ↔ E + P takes place...

1. If the enzyme-catalyzed reaction E + S ↔ ES ↔ E + P takes place near Vmax to the enzyme (E), what can be concluded about the relative concentrations of S and ES? a) High [S], [ES] is low b) High [S], [ES] are at their maximum c) Low [S], [ES] is low d) Low [S], [ES] is at its maximum 2. Which of the following statements about Michaelis-Menten kinetics is correct? a) Km = the substrate concentration required...

1. Starting from the enzyme-catalyzed reaction: S -> P Derive the (a) Michaelis-Menten Equation (b) starting...

1. Starting from the enzyme-catalyzed reaction: S -> P Derive the (a) Michaelis-Menten Equation (b) starting from the Michaelis-Menten equation, derive the Lineweaver-Burker plot. Provide brief explanation in each step. 2. Predict the optimum pH and temperature for human saliat amylase. Why did you arrive on the prediction?

At 125oC Kp for the reaction below is 0.25. 2 NaHCO3 (s) ↔ Na2CO3 (s) +...

At 125oC Kp for the reaction below is 0.25. 2 NaHCO3 (s) ↔ Na2CO3 (s) + CO2 (g) + H2O (g) A 1.00 L containing 10.00 grams of NaHCO3 is heated to 125oC. What are the masses of NaHCO3 and Na2CO3at equilibrium? What is the minimum container size such that there would be no NaHCO3 remaining?

In the reaction below, 4.24 atm each of H2 and I2 were placed into a 1.00...

In the reaction below, 4.24 atm each of H2 and I2 were placed into a 1.00 L flask and allowed to react: H2(g) + I2(g) <=> 2 HI(g) Given that Kp = 33.9, calculate the equilibrium pressure of I2 to 2 decimal places.

For the reaction 2NO_2 (g)→2NO_2 (g)+O_2 (g) The data given below was collected: Time(s) [NO2] Ln[NO2]...

For the reaction 2NO_2 (g)→2NO_2 (g)+O_2 (g) The data given below was collected: Time(s) [NO2] Ln[NO2] 1/[NO2] 0 0.110 -2.205 9.066 1 0.108 -2.229 9.294 2 0.105 -2.254 9.524 3 0.103 -2.277 9.747 Obtain the average rate of decomposition of NO_2 in units of M/s for each interval. What is the order of the reaction with respect to NO_2? How long would it take for the concentration to decrease to .0900M?