Concept explainers
SCIENTIFIC INQUIRY
DRAW IT A researcher has developed an assay to measure the activity of an important enzyme present in liver cells growing in culture. She adds the enzyme’s substrate to a dish of cells and then measures the appearance of reaction products. The results are graphed as the amount of product on the y-axis versus time on the x-axis. The researcher notes four sections of the graph. For a short period of time, no products appear (section A). Then (section B) the reaction rate is quite high (the slope of the line is steep). Next, the reaction gradually slows down (section C). Finally, the graph line becomes flat (section D). Draw and label the graph, and propose a model to explain the molecular events occurring at each stage of this reaction profile.
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EBK CAMPBELL BIOLOGY IN FOCUS
- cells can regulate different processes in two ways. they can turn on and off the genes that make enzymes, or they can: A. decrease the amount of energy needed to carry out the preferred process B. increase the activation energy of a reaction C. regulate the enzymes that are already made D. increase the amount of energy needed to carry out the preferred processarrow_forwardDescribe what is happening at the low, middle, and high points in the graph you made on the previous page. Be sure to use your knowledge of enzymes to explain the results of the experiment.arrow_forwardStep 1: Depict E + S • Draw an enzyme and one substrate. Show and label the substrate binding site on the enzyme. Step 2: Depict ES • Draw the enzyme bound to the substrate in the substrate binding site. Step 3: Depict EP • Draw the enzyme bound to the product (the changed substrate). Step 4: Depict E + P • Draw the enzyme with the product released. (Note: the enzyme is returned to its original state and can be reused.) Step 5: Impact of Inhibitors • Go to the prompts that have arrows pointing to the E + S picture you drew and fill in the blanks with the appropriate type of inhibitor (competitive or non-competitive/allosteric).arrow_forward
- The image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.arrow_forwardConsider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?arrow_forwarddraw the enzyme binding pocket and active site draw the curved arrows showing the reaction proceeding toward the products show how the enzyme facilitates the reaction write a description of how the enzyme works Propose a name for the enzyme based on the rules from classarrow_forward
- A technician investigated the effect of temperature on the rate of an enzyme- controlled reaction. At each temperature, she started the reaction using the same concentration of substrate. 15 amount of 37 C product in 11. Give one other factors the technician would have controlled. 10 60 "C 12. Explain the difference in the initial rate of reaction at 60°C and 37°C. 13. Explain the difference in the rates of reaction at 60°C and 37°C between 20 and 10 20 30 Time after start of reaction i minutes 40 minutes.arrow_forwardThe diagram shows the mechanism of a general enzyme‑catalyzed reaction. Put the labels in the correct locations. The abbreviations E, P and S indicate the enzyme, product, and substrate, respectively.arrow_forwardYou have cloned a gene for an enzyme in E.coli and want to increase its catalytic activity. Describe how you would achieve this if you know the DNA sequence of the gene but not the regions of the enzyme that are important for its catalytic activityarrow_forward
- Which of the following describes a reaction that requires substrate 1 to bind the the enzyme, then substrate 2 binds, and then the products are produced? A. No ternary complex B. Ordered ternary complex C. Ping-Pong D. Random ternary complexarrow_forwardExamine the figure below, which compares the energetics of a catalyzed and uncatalyzed reaction during the progress of the reaction from substrate (S) to product (P). The highest peak in such a diagram corresponds to the transition state, which is an unstable, high-energy arrangement of substrate atoms that is intermediate between substrate and product. The free energy required to surmount this barrier to the reaction is termed the activation energy. Enzymes function by lowering the activation energy, thereby allowing a more rapid approach to equilibrium. UNCATALYZED activation energy progress of reaction CATALYZED activation energy S ES | progress of reaction free energy free energyarrow_forwardLeia wants to determine the effect of enzyme concentration on enzyme activity using potato samples and hydrogen peroxide. However, her results do not follow the theoretical trend and thus she can't draw any conclusions from the data obtained. What might have caused errors in the experiment? I. Placing potato samples under room temperature II. Different treatments, with potato being proportional to the volume of hydrogen peroxide III. Placed the same amount of hydrogen peroxide for a different amount of potatoes IV. Placed the same amount of potatoes for a different volume of hydrogen peroxidearrow_forward
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