what are correct about enzyme kinetic parameters
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what are correct about enzyme kinetic parameters
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- When the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increasesIn a plot of 1/v vs 1/[S] for an enzyme-catalyzed reaction, presence of a competitive inhibitor will alter the: ? Intercept on the 1/v axis. Intercept on the 1/[S] axis. Curvature of the plot. Intercept on both axes.Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
- Many biosynthetic pathways are regulated by feedback control, where the product of a pathway turns off an enzyme that catalyzes an early step in the pathway. Usually, this control comes from an allosteric interaction. Of the types of reversible enzyme inhibition (Competitive inhibition, Noncompetitive inhibition, and Uncompetitive inhibition), what type is most likely to occur in a feedback control mechanism like this and why?The figure displays the relationship between initial rate of product formation and reactant concentration in an enzyme-catalyzed reaction with a fixed amount of enzyme. Which of the following statements best explains the shape of the rate curve at high reactant concentration?Enzyme cofactors are usually inorganic ions that enhanceenzymatic activity by improving the “fit” between an enzymeand its substrate. True or false?
- Select the graph that correctly illustrates the effect of a positive modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector. R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that this is a positively cooperative enzyme, meaning that the affinity for substrate increases with increasing substrate concentration.When k2 >> k-1, KM approximates the affinity of the enzyme•substrate complex.The (circle one) higher / lower the KM, the more tightly the enzyme binds to its substrateAn enzyme is mutated such that the KM of the mutated enzyme is lower than the KM of the original enzyme. Which of the following statements is true (select all correct answers)? Question 2 options: If the original enzyme and the mutated enzyme are mixed with the same concentration of substrate, the mutated enzyme will have v0 closer to Vmax (hint: consider the Michaelis-Menten equation) The effect of a particular competitive inhibitor will be less on the mutated enzyme than it is on the original enzyme (hint: consider the reaction scheme for a competitive inhibitor) The effect of a particular uncompetitive inhibitor will be less on the mutated enzyme than it is on the original enzyme (hint: consider the reaction scheme for an uncompetitive inhibitor) The mutated enzyme has higher affinity for the substrate than the original enzyme does
- When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibitionThe Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.Which 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.