1. Which substrate have the highest affinity for the enzyme? Explain. 2. Which will show higher efficiency of converting the substrate to the product? Show solutions and explain.
Q: 1. explain why the substitution of Leu > Val and Arg Lys in protein does not cause a decrease in the…
A: Mutation is the change in nucleotide sequences, which ultimately alters the amino acid and protein…
Q: Enzyme Substrate Competitive Noncompetitive inhibitor inhibitor Which two substance both compete for…
A:
Q: 3. What is the marker for the enzyme’s optimum condition?
A: The conditions under which an enzyme is most active are the optimum conditions(like pH,temperature)
Q: Briefly describe the series of events must take place between the binding of substrate to enzyme,…
A: Enzymes are found in all body fluids and tissues. It is composed wholly of protein which is simple…
Q: 1. Using the following data, graph percent enzyme activity on the y-axis and pH on the x-axis 2.Do…
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Q: 2. Enzyme X has an optimum pH = 9.5. Which buffer solution below is the most appropriate to maintain…
A: pH is the measure of the strength of H+ ion or Hydronium ions in solution. pOH is the…
Q: 3. 4. 2 3 4. 5 6 7 8 pH of reaction According to Figure 1.7 which enzyme is most likely found in a…
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Q: 2. Explain why enzyme activity declines at (a)high temperature and (b) presence of heavy metal ions.
A: Enzymes are proteins that aid in the speeding up of our bodies' metabolism, or chemical processes.…
Q: 6. Using graph C: a. Explain what happens when hypothermia sets in (when enzymes get too cold!)…
A: Note: As per guidelines we answer the first question. Kindly resubmit the questions to be answered…
Q: If an enzyme is functioning at 75% of Vmax, the substrate concentration must be than the Km of the…
A: Introduction: Proteins called enzymes aid in accelerating the body's chemical reactions, or…
Q: Label the x axis in each graph below with the appropriate factor (possible factors: temperature, pH,…
A: Introduction: Enzymes are proteins that function as biological catalysts to accelerate the rate of…
Q: -Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005…
A: Km of an enzyme is the substrate concentration at half Vmax. It can be calculated from lb plot by…
Q: -Inhibitor +Inhibitor _[S] (mM) νο&νβσπ:(μmol/sec) ν0&νβσπ; &νβσπ;(μmol/sec) 0.0001 33 17 0.0005 71…
A: From the given data, I have calculated 1/S and 1/V0 in absence and presence of inhibitor. The plot…
Q: -Inhibitor +Inhibitor [S] (mM) Vη&νβσπ:(μmol/sec). V0&νβσπ&ν βσπ (μmol/sec) 0.0001 33 17 0.0005 71…
A: Km is the michaelis menton constant which is a substrate concentration at half Vmax. This can be…
Q: 2. The effect of pH on enzyme activity. Reaction rate pH 1.0 8.5 10.0 1.5 2.0 8.5 2.5 3.0 7.0 5.5…
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Q: 1. Give the substrate for each of the following enzymes:
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Q: Explain why the maximum initial reaction rate cannot be reached at low substrate concentrations
A: Note- As per the guidelines only one question can be answered at a time. Hence, the first question…
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Q: Substrate KM (M) N-Acetylvaline ethyl ether 8.8 X 10 -2 N-Acetyltyrosine ethyl ether…
A: The Km of an enzyme is inversely proportional to the affinity for its substrate. This is because a…
Q: 1. Define the following: Active site Substrate • Enzyme-substrate complex • Rate of reaction 2. What…
A: Active site:- In an enzyme, that area where the substrate molecules bind and undergo a chemical…
Q: The figure below shows the dependence of the enzyme's rate, v (in uM/min), as a function of…
A: Proteins that catalyze all biochemical reactions are called enzymes. Enzymes affect the rate of…
Q: 1. Explain what "optimum" means. Do all enzymes have the same optimum pH and temperature?
A: Optimum means a state at which the best of a reaction or outcome occurs.And it is a level at which…
Q: Explain how enzymes work, what is their chemical composition (i.e., protein, carbohydrate, or…
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Q: Under conditions where this enzyme is saturated, which parameter will change significantly as you…
A: Saturation of enzyme means all the enzyme molecules are occupied by the substrate molecule. No free…
Q: The following data were collected for an enzyme that can be described by Michaelis Menton kinetics.…
A: In-order to get accurate Km and Vmax values, we need to draw the LB plot. The LB plot has 1V (i.e.…
Q: 1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first…
A: Thank you for the question, as per the honor code, we are allowed to answer the first question at a…
Q: 2. Indicate whether each of the following statements describes a reversible competitive inhibito…
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Q: At steady state,[Es} stays the same although substrate concentraion is steadily decreasing and…
A: According to steady-state assumption, the concentration of [ES] (Enzyme –substrate) complex is…
Q: 6. Which of the following is true of the binding energy derived from enzyme-substrate interactions?…
A: Introduction: Those proteins that increase the rate of the reaction without undergoing any change…
Q: when the substrate concentration of certain enzyme is quarter than Michaelis constant, the velocity…
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Q: Explain why the P/O ratio for a given substrate is not necessarily an integer.
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Q: How would you be able to increase the rate of reaction after C? * A substrate concentration Late
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Q: Explain the details in the individual steps in the Michaelis-Menten mechanism of converting…
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Q: 1. If the Km of an enzyme for substrate A is 1 x 106 and for substrate B, is 4 x 10°, it means a.…
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Q: How would a competitive inhibitor change the Km and the Vmax for an enzyme? Explain why a…
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Q: The hydrolysis of a substrate, S, by an enzyme has been studied in the lab. The following initial…
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Q: 1.With the data shown below, please answer the following: A. Which of the two inhibitors is more…
A: Vmax is the maximum velocity. Michaelis menten constant, Km is the substrate concentration required…
Q: An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time…
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Q: please answer this question
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Q: What effect will competitive inhibitor have on the apparent Km of an enzyme for its substrate?
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Q: Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest…
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Q: 2. Describe the relationship between substrate and the product. What happens when you increase the…
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Q: Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20 KM.…
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- An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.Consider an enzyme that follows standard Michaelis-Menten kinetics and has the following kinetic constants: %3| k2 = 1.5 x 10? s1 Еo 3D 1 х 104 М = 1 x 104 M a. What is the value of the maximum rate VM? b. Prepare a hand-drawn quantitative plot on graph paper (not a simple sketch nor an EXCEL-generated graph) of the enzymatic reaction rate versus substrate concentration (like Fig 3-3) using the kinetic parameters given above. Be sure to label the axes and include numeric values on the axes. C. Based upon your hand drawn saturation plot, at what substrate concentration is the enzymatic reaction rate 75% of Vm?In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM b. What type of inhibitor is Inhibitor PQR? Why do you say so?
- Please note the following Lineweaver-Burk plot for the enzyme Virbraniumase reacting with a substrate: -0.4 . 1/V 5 4 3 2 -0.2 0 0.2 y = 5.2781x + 1.3338 R² = 0.9967 0.4 0.6 0.8 1/[S] 1 Based on the information provided, what is the Vmax for this reaction?A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence and presence of 0.1µM inhibitor (ketoconazole). O Estimate Vmax and Km in the absence and presence of the inhibito.. (ii) Determine the type of inhibition shown by the inhibitor. Explain. 0.1- 0.08 0.06 - With inhibitor 0.04 0.02 Without inhibitor 0.4 -0.2 -0.02 0.2 0.4 0.6 0.8 1.0 1/{S\(&M-1) 1/vo (pmol-11 min)
- Staphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseIn an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.
- The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate reaction in the presence of the inhibitor hydroxymethylaspartate (3.8 M), determine KM and whether the inhibition is competitive or noncompetitive (KI = 1.0 M). In the ABSENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= __________ (1[S])(1[S]) + __________, and the KM is __________ M. In the PRESENCE of inhibitor: The Lineweaver-Burke equation is 1V=1V= ____________ (1[S])(1[S]) + ___________, and the KM is ___________ M. The type of inhibition is ____________. Round-off all answers to two (2) significant figures.The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.you are trying to come up with a drug to inhibit the activity of an enzyme thuogth to have a role in a liver disease. in the lab the enzyme was shown to have a Km of 1x10-6 M and Vmax of 0.1 micromoles/min.mg measruing at room temperature. you developed a mixed non-competitve inhibitor with a ki=0.4x10-6M and a Ki` pf 0/2 x 10-5 What will be the apparent Km in the presence of 1.0x10-6 M?