Which of the following statements about Competitive and noncompetitive inhibition is false? a. A noncompetitive inhibitor does not change the Km of the enzyme. b. A competitive inhibitor does not change the Vmax of the enzyme c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex. d.A competitive inhibitor decreases the apparent Km for a given substrate.
Q: A) Which substrate A or B had the greater affinity for the enzyme? How did you make your conclusion?…
A: Enzymes are substances that increase the velocity of a chemical reaction. They are the biocatalysts,…
Q: Answer TRUE or FALSE. a. If both the inhibitor and the substrate bind at the active site on a random…
A: Dear students, According to the guidelines, we are attempting the first three subparts of a question…
Q: Which of the following is incorrect about enzyme inhibitors? a. They can be reversible or…
A: Aspirin irreversibly inhibits the COX-1 enzyme. It covalently modifies this enzyme and is used to…
Q: Which of the following statements helps best explain the reaction specificity of an enzyme? a)…
A: Enzymes can be defined as the proteins which work as the biological catalyst and they help in the…
Q: Which of the following statements about the Michaelis Menten constant (Km) is correct...... A. can…
A: Michaelis Menten constant (Km); It is the concentration of substrate at which the reaction rate is…
Q: Characterization of enzyme activity does not allow us to: a. determine how different variables…
A: Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy. It…
Q: You are studying the enzyme Homerase and you notice that the rate of product formation increases as…
A: In order to catalyze a reaction, enzyme will interact with one or more reactant molecules. This…
Q: Consider the following data set of enzymes A, BC and D which catalyze the same reaction. Enzyme A km…
A: Introduction: Catalysts are those substances that increase the rate of the reaction without…
Q: Which of the following types of inhibitors binds to the active site of an enzyme? Select one: a.…
A: Inhibitors are the substances that bind the enzyme and decrease the catalytic activity of the…
Q: Enzymes have similar responses to both changes in temperature and pH. The effect of both is on the…
A: Enzymes are the biological polymers which are formed from the tertiary structure of the protein…
Q: The table below provides kinetic information when ADH is reacted with ethanol alone, NAD+ alone, and…
A: Enzyme kinetics is the study of an enzyme catalyzed biochemical reactions. Usually it is studied by…
Q: Substrate A exhibits a Km toward a given enzyme of 11.32 mM, while substrate B exhibits a Km toward…
A: Km is the substrate concentration at which half Vmax. It is Michaelis menton constant which is used…
Q: A biochemist discovers and purifies a new enzyme, generating the purification table below. (a) From…
A: Enzymes can serve as biological catalysts to increase the rate of a chemical reaction by lowering…
Q: In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same…
A: Enzymes are substances that aid in increasing the rate at which a reaction occurs. It does so by…
Q: In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of…
A: This question can be solved by using three different equations which are as aresult of compitative…
Q: An enzyme with a high turnover number has A. a high Kcat. B. a low Km. C. a high Vmax. D. a high…
A: Turnover number = Vmax/[ET] Vmax is maximum velocity of reaction ET is given enzyme concentration
Q: . Based on what you know about enzyme inhibition, classify the following examples as irreversible,…
A: “Since you have posted a question with multiple sub-parts, we will solve first three subparts for…
Q: The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole…
A: Enzymes are the proteins that participates in the chemical reaction and enhance the rate of…
Q: Which of the following analogies best describes the induced-fit model of enzyme-substrate binding?…
A: Each enzyme consists of a substrate binding site which is known as active site. When a substrate…
Q: Which of the following terms best describes a drug that binds to an active site and inhibits the…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…
Q: The picture shown depicts what type of compound binding to an enzyme? A) A competitive inhibitor B)…
A: Regulatory enzymes show increased or decreased catalytic activity in response to specific types of…
Q: Given below are five Km values for the binding of substrates to a particular enzyme. Which substrate…
A: Those proteins or biological catalysts which help to speed up the chemical reaction are termed…
Q: the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C…
A: Introduction:- The steady-state approximation is a rate law derivation approach. The technique is…
Q: A noncompetitive inhibition can be overcome/reverse by which of the following:
A: There are three types of reversible inhibition: Competitive inhibition Non-competitive inhibition…
Q: In pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does…
A: Enzymes refer to the protein that acts as a catalyst for the biochemical reaction. It facilitates…
Q: What are allosteric modulators? A. These are inhibitors that bind at sites other than the active…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: You are performing an enzyme kinetics experiment testing the effect of pH on reaction rate. You…
A: Enzymes are the proteins that act as biological catalyst. They catalyze a biochemical reaction…
Q: Create a graph that represents the predicted results of the experiment, based on your hypothesis,…
A: Biocatalysts (biological catalysts) that help in speeding up chemical reactions are known as…
Q: Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are…
A: Enzymes are proteinous compounds. They act as catalysts for biochemical reactions. Like inorganic…
Q: Which of the following is NOT true about enzymes A. they do not alter reaction equilibria…
A: All Enzymes are actually proteins they act as biocatalysis in any chemical or metabolic reaction by…
Q: A mixed inhibitor (sometimes called a mixed non-competitive inhibitor) of an enzyme: a decreases…
A: A type of inhibition where the inhibitor may bind to the enzyme irrespective of the enzyme being…
Q: An attempt was made to inhibit Enzyme X by adding compounds M and L. The results are summarized in…
A: Inhibitors are substances that inhibit the enzyme and decrease enzyme activity. Inhibitors are…
Q: A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown…
A: To determine the values of km and Vmax by lineae regression, we need to plot lb plot. LB plot can be…
Q: inhibitor that binds the active site of an enzyme? Select all that apply, there may be one correct…
A: COMPETITIVE INHIBITION It is interruption of a chemical pathway where one chemical substance…
Q: Which of the following statements is/are true about enzyme-catalyzed reactions? A. The reaction is…
A: Enzymes are bio-catalysts that help to increase the rate of biochemical reaction. A typical enzyme…
Q: Please choose one of these answers A. An allosteric inhibitor appeared B. There was a dramatic…
A: Enzymes are the molecules which speed up the rate of biological reactions without being consumed in…
Q: Choose the best description of an enzyme: (a) It allows a chemical reaction to proceed extremely…
A: Enzyme are biocatalyst molecules that increases the rate of reaction by binding to the transition…
Q: An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme…
A: Enzymes are proteins which can convert substrate molecules to products. Substrate molecules bind…
Q: Which of the following is not a type of specificity for an enzyme when binding substrates? A)…
A: The enzymes are biocatalysts that increase the rate of reaction by decreasing the activation energy.…
Q: In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of…
A: Inhibitors bind to the enzyme and affect enzyme activity and they bind to it covalently and…
Q: Enzymes act by: a. increasing the activation energy for a reaction b. lowering the activation energy…
A: An enzyme has the ability to attract the substrate to the active site which further results in the…
Q: Enzymes work by at least three mechanisms. Which of the following is NOT a mechanism by which…
A: Introduction Enzymes are the molecules that catalyse biochemical reactions, while a catalyst is a…
Q: Which of the following is true for competitive inhibition? A) The affinity of the enzyme to its…
A: competitive inhibition: The binding of the inhibitor to the active site of the enzyme preventing…
Q: Which of the following is the correct value of the KM? a. It is [substrate] at half Vmax b. It is…
A: Michaelis Menten Equation is given as v=Vmax[S]Km+[S] Here, v is the Initial reaction velocity…
Q: Given: Your professor gives you a vial of enzyme and a vial of substrate. The product of this…
A: Michaelis-Menten kinetics describes the rate of enzyme-catalyzed reactions. It relates the rate of…
Q: There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km,…
A: Proteins are biomolecules present in living organisms. Enzymes are mostly protein molecules. They…
Q: Which phrase characterizes a uncompetitive inhibitor? binds either enzyme or enzyme-substrate…
A: Introduction: The enzymes are proteins that increase the rate of chemical reactions that occurs…
Q: he figure displays the relationship between initial rate of product formation and reactant…
A: in this Figure At low concentration rate of product formation is directly proportional to…
Q: A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion…
A: Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…
Q: What would be the expected effect of this change on the enzyme’s catalytic activity?
A: Enzyme activity is the rate of the reaction catalyzed by the enzyme expressed. It is measured as…
Trending now
This is a popular solution!
Step by step
Solved in 3 steps
- An enzyme has 10 times greater affinity for substrate "A" than for substrate "B". Which of the following is true? a.) KM of A is 10 times the KM of B b.) The concentration of B is 10 times that of A c.) Vmax of A is 1/10 the Vmax of B d.) KM of A is 1/10 the KM of B e.) Vmax of A is 10 times the Vmax of BAn enzyme has the ability to catalyze reactions of several unrelated compounds. The mechanism of how this enzyme operates is best explained by a. the lock-and-key theory b. the induced-fit theory c. the enzyme-substrate complex d. the efficiency of the enzymeMolecule X is expected to be a non-competitive inhibitor of an enzyme. If the inhibitor was tested at a saturating level of substrate the following would be observed: a. The inhibitor would decrease the Vmax b. The inhibitor would increase the Km c. The inhibitor would decrease the Km d. The inhibitor would increase the Vmax e. The inhibitor would not change the Vmax
- Which of the following statements about non-competitive inhibitors is true? A) They bind at the active site of the enzyme and block access to the substrate. B) They bind at a location away from the active site. C) They function by changing the shape of the enzyme's active site. D) B and CWhich of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workAn enzyme-substrate solution has been "poisoned" with a noncompetitive inhibitor. It is expected that the addition of more substrate to the solution will _____ the activity of the enzyme. a. increase b. decrease c. have no effect on
- Given the following equations of the line, a) determine the KM of the substrate that binds the strongest with the enzyme. b) determine which of the following substrates binds the least with the enzymeA) Which substrate A or B had the greater affinity for the enzyme? How did you make your conclusion? B) Define enzyme competition.The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time. b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time. c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.
- 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.Enzymes have similar responses to both changes in temperature and pH. The effect of both is on the a. rate of movement of the substrate molecules. b. strength of the chemical bonds within the substrate. c. three-dimensional shape of the enzyme. d. rate of movement of the enzyme.In competitive inhibition, increasing concentrations of the inhibitor will have the following effect on the kinetics of the enzyme: A. Km will decrease. B. Vmax will stay the same. C. The reaction will cease because the inhibitor binds irreversibly. D. Km / Vmax will stay the same.