1. Define Vmax and Km (Michaelis constant). What is the mathematical relationship between these two values?...
1. Define Vmax and Km (Michaelis constant). What is the mathematical relationship between these two values?
2.What does Km tell you about the affinity of an enzyme for its substrate?
3.Why do we use the slope between the first two data points of Absorbance vs Time to determine V0 when studying enzyme kinetics? Why not use the slope of the entire line?
Homework Answers
Question
1. Vmax is the maximum velocity attained when enzyme is saturated with substrate or no more substrate could not attach to the enzyme. On the other hand,Km is the substrate concentration that permit enzyme to achieve half of maximum velocity.
The mathematical relationship between Vmax and Km is:
![Vo = Vmax [S] Km + [S]](http://img.homeworklib.com/questions/c539f450-e5c8-11eb-9dbb-03b9fcefd43b.png?x-oss-process=image/resize,w_560)
2. When the value of Km is high, it show lower affinity of enzyme for its substrate whereas low Km value indicate that enzyme have high affinity for its substrate. This is due to the fact that high Km means more substrare are required to attain half of Vmax.
3. We use the slope between the first two data points of Absorbance vs Time to determine V0 when studying enzyme kinetics because it give the value of Km/Vmax. We do not use the slope of entire line because the velocity of reaction catalyzed by enzyme keep on changing.
Add Answer to:
1. Define Vmax and Km (Michaelis constant). What is the
mathematical relationship between these two values?...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using...
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]....
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
3. In an enzyme-catalzed reaction, Vmax=0.2mol/sec and Km=5mM. a) What is the rate of the reaction...
3. In an enzyme-catalzed reaction, Vmax=0.2mol/sec and Km=5mM. a) What is the rate of the reaction when [s]=10mM?! b) Draw a Michaelis-Menton plot of the reaction kinetics, labeling the axes and giving values for the two points where you know V.
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the...
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
1. What effect would the inhibitor Phenylalanine have on the Km and Vmax values when added...
1. What effect would the inhibitor Phenylalanine have on the Km and Vmax values when added to a solution with Tyrosinase. 2. Explain why Kojic acid is an inhibitor of Tyrosinase? 3. What is the difference in using D-DOPA vs. DOPA in a substrate experiment with Tyrosinase?
a. what are the values of Vmax and Km in the abscence if the inhibitor what...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...
yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...
ISU Question 3: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo 1/[S1 1/V0 UM (UM/s) M (s/uM) 340 10 2.94E-03 0.2 530 740 0.8 910 1.6 1040 0.4 a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest (SD? c) Using your Vmax estimate, calculate 14 Vmax, and using your curve, estimate Km....
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
3. In an enzyme-catalzed reaction, Vmax=0.2mol/sec and Km=5mM. a) What is the rate of the reaction when [s]=10mM?! b) Draw a Michaelis-Menton plot of the reaction kinetics, labeling the axes and giving values for the two points where you know V.
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
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