Concept explainers
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme
a. effector inhibition
b. allosteric inhibition
c. feedback inhibition
d. competitive inhibition by nonproduct
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Chapter 20 Solutions
Chemistry for Today: General, Organic, and Biochemistry
- Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forwardCompare the lock-and-key and induced-fit models for substrate binding to an enzyme.arrow_forwardList two ways that enzyme catalysis of a reaction is superior to normal conditions.arrow_forward
- . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?arrow_forwardThe site on an enzyme molecule that does the catalytic work is called the: a. binding site. b. allosteric site. c. lock. d. active site.arrow_forwardBased on the graphical information in Problem 21-41 about enzymes A and B a. What is the optimum pH for enzyme B? b. What is the optimum temperature for enzyme A? c. Which enzyme has the greater activity at a pH of 7.2? d. Which enzyme has the greater activity at a temperature of 37.2C?arrow_forward
- Why are enzymes that are used for laboratory or clinical work stored in refrigerators?arrow_forwardBased on the graphical information in Problem 21-41 about enzymes A and B indicate whether the enzyme activity of enzyme B increases or decreases when the following changes in reaction conditions are made. a. pH decreases from 7.6 to 7.2 b. pH increases from 7.2 to 7.4 c. temperature decreases from 37.8C to 37.6C d. temperature increases from 38.2C to 38.4Carrow_forward
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