The turnover number of an enzyme catalyzed :reaction is equal to .K2 .a O .K1 .b O .K3/1 .c O .K3 .d O .К2 + КЗ .е O
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A: Option c The ability to form permanent covalent bonds with the substrate
Q: 10 20 30 40 50 60 70 80 Temperature (°C)
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A: B) allosteric inhibition is the correct answer.
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A: Answer is a.) substrate .
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Q: Which of the following is incorrect? a. Without an enzyme, reaction rate can be increased by…
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A: Turnover number = Vmax/[ET] Vmax is maximum velocity of reaction ET is given enzyme concentration
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- Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correctWhich of the following is a primary function of the active site of an enzyme? a. It binds allosteric regulators of the enzyme. b. It binds noncompetitive inhibitors of the enzyme. c. It catalyzes the reaction associated with the enzyme. d. It is activated by the presence of the end product of the metabolic pathway in which the enzyme is involved. Clear my choice Question 2 Not yet answered Points out of 2.00 Flag question Question text Which of the following statement about the mass spectrometry is true? a. Large amount of protein sample is needed for mass spectrum, and thus it is very expensive. b. It is a powerful method to determine the 3-dimensional structure of proteins. c. It can be sued for protein location in a living cell. d. It can be used to measure the molecular weight of proteins. e. It can be used to determine the stability of a protein structure in solution. Clear my choice…The enzyme becomes denatured if the temperature is compared to its optimal temperature: O a. Too low O b. Too high O c. Too high or too low
- Which of the following is incorrect about the rate of an enzyme-catalyzed reaction? a. It does not change when changing [enzyme] The more enzyme present, the faster the reaction b. c. None; all the other choices are correct Od. It will double, if [enzyme] is doubledWhich of the following statements is/are TRUE about the Lock and Key model of enzyme-substrate interaction? I. The active site of the enzyme has flexible conformation. II. Only a certain number of substrates can fit on the enzyme's active site. O Both I and II O Neither I nor II O I only O II onlyWhich of the following statements is/are true about enzyme-catalyzed reactions? A. The reaction is faster than the same reaction. B. The free energy change of the reaction is opposite from the reaction in the absence of the enzymes. C. The reaction always goes in the direction toward chemical equilibrium. D. A and B only E. A, B and C
- Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pesIf a competitive inhibitor of an enzyme is added to the mixture of the enzyme and its substrate, the inhibitor will: O a. decrease the value of Vmax for the chemical reaction catalyzed by this enzyme O b. decrease the value of KM for the chemical reaction catalyzed by this enzyme O c. increase the value of KM for the chemical reaction catalyzed by this enzyme O d. increase the value of Vmax for the chemical reaction catalyzed by this enzymeWhich of the following statements regarding enzymes and metabolic reactions is correct? All enzyme reactions proceed towards a higher entropic state for the products. О а. O b. Enzymes set the pace and direction of metabolic reactions. Enzymes allow endergonic reactions to proceed towards the product by lowering the activation energy Ос. O d. The amount of free energy (AG) in a reaction is dependent on the ratio of the reactants to the products.
- An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE The Km for X will be affected if Y is present in the reaction mixture. a Y is a competitive inhibitor of X. The Km for X will increase. d The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken). A mutation in the active site of an enzyme resulting in a large increase in…Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate siteWhich of the following statement/s is/are TRUE of enzymes? 1. They increase the rate of reaction by stabilizing the transition state. II. They raise activation energy to shift the equilibrium to favor the products. . They lower activation energy by altering the products of a reaction. O l and III O Il and III O III only o l only