The investigators examined thebehavior of the ATCase enzymein the presence of CTP, and inthe presence of both CTP andATP. The concentration ofCTP is 0.1 mM and the concen-tration of ATP is 2 mM. Theresults are shown in Figure3. What is the significance ofthese observations?% Activity1009080706050403020100control+ CTP+CTP +ATP

Enzymes are the proteins that catalyse a chemical reaction by reducing the activation energy of the…

Answered: The investigators examined the behavior…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The following kinetic data were collected for prostaglandin endoperoxide synthase, an enzyme involved in pain and inflammation. Using data in the first two columns, use a graphical analysis to determine the Vmax and the Km of the enzyme. Ibuprofen (Advil) is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting this enzyme, ibuprofen helps to reduce pain and fever. Using the data in the first and third columns, determine the type of inhibition that ibuprofen exerts on prostaglandin endoperoxide synthase. In the presence of the inhibitor, determine the Vmax and the Km of the enzyme. [S] mM Product formed Product formed (mmol/min) with 10 mg/mL ibuprofen mmol/min) 0.5 23.5 16.67 1.0 32.2 25.25 1.5 36.9 30.49 2.5 41.8 37.04 3.5 44.0 38.91
What percentage of max is obtained when the substrate is present at 80% of the Km? Use two digits in your answer.
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
O Att Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Nat-glucose symporter. Recall that the Nat concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Nat ions into the cell to the "uphill" transport of glucose into the cell. If the Nat concentration outside the cell ([Na lout) is 161 mM and that inside the cell ([Na* Jm) is 17.0 mM, and the cell potential is -50.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. What is the maximum ratio of (glucose] to [glucoselout 10.62 kJ AG gluc mol that could theoretically be produced if the energy Incorrect coupling were 100% efficient? O 1.13 8.24 3800 2.6 x 10 Incorrect
A newly developed drug is suspected to act by inhibiting its enzymatic target. To test this, the rates of reaction in the presence and absence of the new drug were determined. The results of these experiments have been plotted as a double reciprocal plot shown in figure 1 below. Using this figure, calculate the values of Vmax and Km for the enzyme in the presence and absence of the drug. 2. Based on the figure and your answer, what type of inhibition is the new drug displaying? 3. Briefly explain how this type of inhibition exerts its action on an enzyme. Figure 1: Double reciprocal plot of reaction rate against substrate concentration in the presence and absence of a new drug.
Indicate the hinge region, GK kinaseselectivity pocket and explain "Solvent AccessibilitySurface" and indicate the salt forming group at ATPbinding site
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
1, For EACH of the following enzyme categories, (1) describe what the general function of the enzyme is; (2) identify a SPECIFIC enzyme in glycolysis that performs this function; and (3) identify the names of the organic substrate and product for the specific enzyme identified. Remember that the name of the category need not appear in the actual name of the enzyme. A. First enzyme category: kinase (answer (1), (2), and (3) B. Second enzyme category: dehydrogenase (answer (1), (2), and (3) C. Third enzyme category: isomerase (answer (1), (2), and (3)
If 10 µM enzyme was used to obtain the data in the summary plot below, k-cat = ________________ sec-1 and efficiency = _________________ sec-1 M-1 for this enzyme. (Enter numeric answers to the nearest integer; Do NOT write unts.)
A protein (PrX) was heated in vitro to 45C for 15 min, in the presence or absence of Hsp40, Hsc70, and ATP. The amount of PrX in aggregated (P, pellet) and soluble (S) fractions was then quantified (Bars, 1 SD). Based on these data, answer the following questions. In all cases, give brief justification for your answer. a) How does Hsp40 alone influence the solubility of PrX? b) How does Hsc70 alone influence the solubility of PrX? c) Do Hsp40 and Hsc70 co-operate in this experiment? d) Which components combined provide maximal solubility of PrX after heat shock?
Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Na*-glucose symporter. Recall that the Na+ concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Na+ ions into the cell to the "uphill" transport of glucose into the cell. If the Na+ concentration outside the cell ([Na* lout) is 147 mM and that inside the cell ([Na+]in) is 17.0 mM, and the cell potential is -54.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. AG gluc kJ mol What is the maximum ratio of [glucose]in to [glucose] out that could theoretically be produced if the energy coupling were 100% efficient? 1.13 2.3 × 10-4 8.36 4300
Michaelis Menton Plot and a Lineweaver-Burke plot using this data

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