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?
Homework Answers
Add Answer to:
1. What effect would the inhibitor Phenylalanine have on the Km
and Vmax values when added...
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...
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?
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
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]...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation is 224M/min, what velocity would be observed in the presence of 2 X 10^M substrate and 5 X10+M a competitive inhibitor. Ki is 3 X 10^M. What is the degree of inhibition? (10pts)
1-The unmutated form of your protein has a Km of 25 µM and a Vmax of...
1-The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, explain the effect of amino acid substitution on the Km and Vmax for the mutated protein. (Up to 50 words) You are not expected to draw a Lineweaver-Burk plot, however a quick sketch of a Vi vs [S]...
Interpret the data above 1. What is the aporoximate Km and Vmax (units matter) 2.Briefly explain...
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
1. When lime is added to an acid soil, explain what it does to 1) soil...
1. When lime is added to an acid soil, explain what it does to 1) soil pH (and what is the mechanism by which it changes the pH); 2) cation exchange capacity (Hint: Think back to pH-dependent charge to understand the effect on cation exchange capacity.) and; 3) the composition of exchangeable cations. 2. Why do some soils need more lime to raise their pH than other soils? Explain your answer in terms of buffering capacity, and active vs. reserve...
Question 13 of 49 A research group discovers a new version of happyase, which they call...
Question 13 of 49 A research group discovers a new version of happyase, which they call happyase,that catalyzes the chemical reaction Map HAPPYSAD The researchers begin to characterize the enzyme a In the first experiment, with [El at 6 nM, they find that the Vmax is 3.50 Ms Based on this experiment, what is the keat for happyase ? In another experiment, with [E] at 3 nM and [HAPPY] at 40 HM, the researchers find that Vo 1390 nM s1....
Kcat =30.0 s-1 Km= 0.005 M Operating at 1/4 Vmax What is [S] ? The solutions...
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
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...
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]...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation is 224M/min, what velocity would be observed in the presence of 2 X 10^M substrate and 5 X10+M a competitive inhibitor. Ki is 3 X 10^M. What is the degree of inhibition? (10pts)
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
Question 13 of 49 A research group discovers a new version of happyase, which they call happyase,that catalyzes the chemical reaction Map HAPPYSAD The researchers begin to characterize the enzyme a In the first experiment, with [El at 6 nM, they find that the Vmax is 3.50 Ms Based on this experiment, what is the keat for happyase ? In another experiment, with [E] at 3 nM and [HAPPY] at 40 HM, the researchers find that Vo 1390 nM s1....
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
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