Concept explainers
(a)
Interpretation: The validation of the given statement about allosteric enzymes has to be stated.
Concept introduction: The enzyme that has two or more protein chains and two kind of binding sites are called allosteric enzymes. Allosteric enzymes have the quaternary structure.
(b)
Interpretation: The validation of the given statement about allosteric enzymes has to be stated.
Concept introduction: The enzyme that has two or more protein chains and two kind of binding sites are called allosteric enzymes. Allosteric enzymes have the quaternary structure.
(c)
Interpretation: The validation of the given statement about allosteric enzymes has to be stated.
Concept introduction: The enzyme that has two or more protein chains and two kind of binding sites are called allosteric enzymes. Allosteric enzymes have the quaternary structure.
(d)
Interpretation: The validation of the given statement about allosteric enzymes has to be stated.
Concept introduction: The enzyme that has two or more protein chains and two kind of binding sites are called allosteric enzymes. Allosteric enzymes have the quaternary structure.
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EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Select all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formarrow_forwardWhich of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.arrow_forwardWhich 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 workarrow_forward
- What are allosteric modulators? A. These are inhibitors that bind at sites other than the active site of enzymes resulting in the reduction of enzyme activities B. These are activators that bind at sites other than the active sites of enzymes resulting in enhanced enzyme activities. C. These are either inhibitors or activators that bind at the active site of enzymes. D. These are either inhibitors or activators that bind at sites other than the active sites of enzymes reducing or enhancing the latter's activities. E. These are small molecules that bind to an ES complex only.arrow_forwardWhich of the following statements about allosteric enzyme regulations are true. A. Allosteric regulations is always used to negatively regulate enzyme activity. B. Allosteric regulations are often end products of a biochemical pathway. C. Diffrent allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme. B only B and C B and D D only A and Darrow_forwardWhich of the following is true about the phosphorylation of proteins? A. Proteins are usually phosphorylated at amino acids that have hydroxyl group-containing side chains. B. Phosphorylation of proteins is catalyzed by phosphatases. C. Phosphoryation always activates enzymes. D. The specificity in phosphorylation is conferred solely by the amino acid to be phosphorylated.arrow_forward
- The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.arrow_forwardSelect all the true statements about sequential versus concerted models of allostery. Group of answer choices A. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme B. No conformational changes occur in either model C. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding D. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formarrow_forwardWhich of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.arrow_forward
- Which of the following statements about enzyme regulation is NOT true? a. covalent modification is one type of enzyme regulation. b. biologically most important type of regulation is standard inhibition. c. allosteric regulation can involved feedback inhibition. d. some types of enzume regulation are not widely used in biology. e. none of the abovearrow_forwardWhich 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…arrow_forwardSelect all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.arrow_forward
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