Question about enzyme kinetics: What is KI, and what property does it portray?
Question about enzyme kinetics:
What is KI, and what property does it portray?
Homework Answers
Answer) KI is inhibitor constant.
It is theorotically defined as the Concentration of inhibitor at which under saturating substrate condition the reaction rate is half of the maximum rate
KI value determines the affinity the inhibitor has for the enzyme.
Lower the value of KI ,higher the affinity and vice versa
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Question about enzyme kinetics:
What is KI, and what property does it portray?
How does temperature affect ADH during enzyme kinetics?
How does temperature affect ADH during enzyme kinetics?
In Michaells-Menten kinetics, we assume steady-state kinetics. What does steady-state kinetics mean in this case? A)...
In Michaells-Menten kinetics, we assume steady-state kinetics. What does steady-state kinetics mean in this case? A) The concentration of the enzyme-substrate complex, [ES], is constant and does not change with time. B) The concentration of enzyme, [E] is fixed. C) The concentration of product, [P], is small and can be ignored. D) The concentration of substrate, [S], is much larger than the concentration of enzyme, [E],
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Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an...
Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an enzyme works? Describe this kinetic parameter in terms of the turnover number and the Michaelis constant and provide an explanation for why triosephosphate isomerase is considered to be 100,000 better than pepsin when this kinetic parameter is used to compare these two enzymes.
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot...
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot Vo versus (substrate), or 1/Vo versus 1/[substrate], how the curves would look like, and how to get Vmax and Km values?
QUESTION 3 The enzyme happyase catalyzes the following reaction: SAD = HAPPY An enzyme kinetics experiment...
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Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the...
Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the mechanism: E+S →ES, rate constant = ki, ES → E+S, rate constant = k-1, ES → E+P, rate constant = k2, E + EI, rate constant = k3. EI → E + I, rate constant = k-3. Assuming that the concentrations of S and I are much larger than the total enzyme concentration, derive an expression for the initial rate of appearance of product,...
General Biology / Biol 101 REVIEW QUESTIONS ON ENZYME KINETICS 10) Why did we do all...
General Biology / Biol 101 REVIEW QUESTIONS ON ENZYME KINETICS 10) Why did we do all of our work in a water bath and use buffer in all of our tubes? 11) What happens to velocity of an enzyme catalyzed reaction as we increase the amount of initial substrate available with a constant amount of enzyme? Be specific. 12) What is the purpose of calculating Km? (What does it tellus about an enzyme?) 13) What are the advantages of the...
A class conducts an enzyme kinetics experiment using the digestive enzyme, trypsin and an unknown inhibior....
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
Enzyme Kinetics - Farrell/Taylor 133 3. Enzyme X has a molecular weight of 48,000. It converts...
Enzyme Kinetics - Farrell/Taylor 133 3. Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. a. At what wavelength do you measure the change in absorbance to assay for enzyme X? Does the absorbance increase or decrease over time? b. If Vmax = 60 pmol/min and you use 400L of a 0.1 mg/mL solu- tion of enzyme, what is the turnover number? 4....
In Michaells-Menten kinetics, we assume steady-state kinetics. What does steady-state kinetics mean in this case? A) The concentration of the enzyme-substrate complex, [ES], is constant and does not change with time. B) The concentration of enzyme, [E] is fixed. C) The concentration of product, [P], is small and can be ignored. D) The concentration of substrate, [S], is much larger than the concentration of enzyme, [E],
Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an enzyme works? Describe this kinetic parameter in terms of the turnover number and the Michaelis constant and provide an explanation for why triosephosphate isomerase is considered to be 100,000 better than pepsin when this kinetic parameter is used to compare these two enzymes.
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot Vo versus (substrate), or 1/Vo versus 1/[substrate], how the curves would look like, and how to get Vmax and Km values?
QUESTION 3 The enzyme happyase catalyzes the following reaction: SAD = HAPPY An enzyme kinetics experiment gave the data shown in the table below. The concentration of happyase used in the experiment was 25.00 UM. [SAD] (MM) 1.000 2.000 3.000 4.000 Vo (mm/s) 3.700 6.727 9.250 11.385 Determine the value of Vmax for happyase (in mM/s). QUESTION 4 Using the information above, determine the value of Km for happyase (in mm). QUESTION 5 How long (in milliseconds) does a single...
Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the mechanism: E+S →ES, rate constant = ki, ES → E+S, rate constant = k-1, ES → E+P, rate constant = k2, E + EI, rate constant = k3. EI → E + I, rate constant = k-3. Assuming that the concentrations of S and I are much larger than the total enzyme concentration, derive an expression for the initial rate of appearance of product,...
General Biology / Biol 101 REVIEW QUESTIONS ON ENZYME KINETICS 10) Why did we do all of our work in a water bath and use buffer in all of our tubes? 11) What happens to velocity of an enzyme catalyzed reaction as we increase the amount of initial substrate available with a constant amount of enzyme? Be specific. 12) What is the purpose of calculating Km? (What does it tellus about an enzyme?) 13) What are the advantages of the...
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
Enzyme Kinetics - Farrell/Taylor 133 3. Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. a. At what wavelength do you measure the change in absorbance to assay for enzyme X? Does the absorbance increase or decrease over time? b. If Vmax = 60 pmol/min and you use 400L of a 0.1 mg/mL solu- tion of enzyme, what is the turnover number? 4....
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