Match the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive inhibition. Competitive inhibition Uncompetitive inhibition Noncompetitive inhibition
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- A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the aboveAll of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.
- Indicate 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 simultaneouslyWhich of the following statements about enzyme character-istics is true?(a) Enzymes generally exhibit a high degree of specificityfor one particular substrate.(b) Enzyme-substrate complexes occur when a substratemolecule collides with the allosteric site of an enzyme.(c) Chemical bonds within a substrate are strength-ened when this substrate forms an enzyme-substratecomplex.(d) Enzymes have a region called the active site, which pro-vides an area where it can form a loose association withits substrate.(e) a and d.Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
- 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.an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form CAssume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thx
- One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?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.A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme B