When an enzymatic reaction is in progress, do you expect to see happen to the amount of substrate? A It will increase as the reaction proceeds. B It will decrease as the reaction proceeds. C The amount will not change as reaction proceeds. D It is not possible to predict what will happen to it as the reaction proceeds.
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When an enzymatic reaction is in progress, do you expect to see happen to the amount of substrate?
A It will increase as the reaction proceeds.
B It will decrease as the reaction proceeds.
C The amount will not change as reaction proceeds.
D It is not possible to predict what will happen to it as the reaction proceeds.
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- For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DGWhat are the steps for an enzyme to create a product in order: The energy of activation is lowered so the reaction can happen quicker. Substrate attaches to the active site. The product is created and released from the active site. The energy of activation is lowered so the reaction can happen slower. A specific substrate attaches to the active site.Which of the following statements is true for the shown reaction? Substrate level phosphorylation occurs during the reaction Phosphoryl transfer occurs during the reaction Both A and B Neither A nor B
- An enzyme can organize substrates to be nearby in such a way where the local/nearby concentration of substrate is much higher than the actual cellular concentration of substrate. What phenomenon is described here? Orientation O Proximity Concentration O OrganizationYou are studying the enzyme Homerase and you notice that the rate of product formation increases as you add more substrate to a constant number of enzymes. However past a certain concentration of added substrate molecules, the rate no longer increases even though you keep increasing the substrate concentration. Which of the following statements likely accounts for this observation? a. This is an example of feedback inhibition b. Since the free energy for the reaction doesn't change in the presence of an enzyme, it can only reach a certain energy level maximum c. The product molecules must be acting as competitive inhibitors d. All the enzymes are complexed with substrate moleculesA competitive inhibitor competes with substrate for binding to the active site of the enzyme. The enzyme, once bound by the inhibitor, is unable to form product. How would a competitive inhibitor affect the velocity of product formation? Would you need more or less of the substrate to get the same velocity as found before the inhibitor was added?
- Enzymes catalyze the rapid formation of product by: lowering the Gibbs free energy of the product raising the Gibbs free energy of the substrate lowering the activation energy between the substrate and the product raising the activation energy between the substrate and the product changing the AG (the change in Gibbs free energy) of the reactionAn allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %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.
- An enzyme facilitate catalysis by formation of ester bond with an alcoholic substrate. Which amino acid residues can facilitate such mechanism of catalysis? Select the correct response: Cys and Met Lys and Arg Ser and Tyr Glu and AspIn an enzymatic reaction of maltase, the disaccharide maltose is hydrolyzed to glucose. In an experiment, an inhibitor X was added to the reaction. The addition of the inhibitor brought about a change in the activity of the enzyme. When the substrate concentration was 0.125 mM, the initial velocity was 0.10 mM per minute. However, Vo / Initial velocity changed to 0.25 mM per minute when the substrate concentration was 0.50 mM. Hence, calculate the of the reaction.Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site