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Concept explainers
(a)
Interpretation: The validation of the given statement about an enzyme active site has to be stated.
Concept introduction: The site that is comparatively a small part of the enzyme’s structure involved in catalysis is known as the active site.
(b)
Interpretation: The validation of the given statement about an enzyme active site has to be stated.
Concept introduction: The site that is comparatively a small part of the enzyme’s structure involved in catalysis is known as the active site.
(c)
Interpretation: The validation of the given statement about an enzyme active site has to be stated.
Concept introduction: The site that is comparatively a small part of the enzyme’s structure involved in catalysis is known as the active site.
(d)
Interpretation: The validation of the given statement about an enzyme active site has to be stated.
Concept introduction: The site that is comparatively a small part of the enzyme’s structure involved in catalysis is known as the active site.
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Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Characterization of enzyme activity does not allow us to: a. determine how different variables affect the enzyme's ability to function b. determine the molecular composition of the enzyme c. determine the optimal environment for an enzyme to function d. determine the effect of inhibitors on the enzymearrow_forwardIndicate whether each of the following statements describes a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. More than one answer may apply.a. Both inhibitor and substrate bind at the active site on a random basis.b. The inhibitor effect cannot be reversed by the addition of more substrate.c. Inhibitor structure does not have to resemble substrate structure.d. The inhibitor and substrate can bind to the enzyme simultaneouslyarrow_forwardThe active site of an enzyme binds specifically to a substrate. Your text mentions an early idea which is that this enzyme-to-substrate interaction is like a lock and key, but it then describes a more accurate model for how enzymes bind to their substrates. Explain why the interaction is not like a lock and key and more like a hand grasping a doorknob. What is the specific name of the 'model' of how enzymes bind to their substrates?arrow_forward
- Which 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 onlyarrow_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 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
- 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 Barrow_forwardThe following statements are either True or False. Please label accordingly. a. L-Amino reductase is an enzyme. b. Allosteric enzymes are composed of two or more protein chains. Heavy metals are examples of inhibitors. They function by binding to sulfur on cysteine amino acid residues. C. d. A reversible noncompetitive inhibitor temporarily blocks an enzyme's active site. Enzymes don't denature as easily as smaller proteins when heated or stressed due to their complex secondary and tertiary structure. e. Oxidative phosphorylation is the biochemical process by which ATP is synthesized from ADP when protons cross the inner mitochondrial membrane. f. g. DNA and RNA strands differ only in the fact that DNA forms a double helix. h. There is no secondary structure in RNA strands.arrow_forwardMany 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 sitearrow_forward
- A small molecule is produced from a set of enzymatic reactions from a precursor substrate. It has been shown that the small molecule is able to regulate its own production. In your own words, and based on course material only: a. Identify the regulatory process and; b. Explain how this process worksarrow_forwardChoose only the letter, no explanation needed. Enzyme activity is affected by a variety of factors. What factor causes the enzyme to denature if it becomes extremely high? * Choices: A. Water's Effect B. pH C. Temperature D. Activator's Effect An inhibitor binds to the enzyme's active site, preventing the substrate from binding to it. What conclusions can you make from this situation? * A. No reaction occurred B. Non-competitive inhibition occurred C. Enzyme activity occurred D. Competitive inhibition occurred Each enzyme is very selective when it comes to its substrate. What can you conclude from this statement? * A. Any substrate can bind to the active site. B. Enzymes are used up in the reaction. C. Only a specific substrate can bind to the active site. D. Enzymes break down when not used. Lock : Key :: Active Site : _____________________________ * A. Substrate B. Active Site C. Coenzyme D. Cofactor Enzymes only speed up biological functions, so they are NOT used up in the…arrow_forwardIndicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.arrow_forward
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