© Macmillan Learning Penalized Classify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive Reversible noncompetitive Answer Bank inhibitor does not alter the maximum reaction rate inhibitor structure resembles substrate structure inhibitor binds covalently and permanently at active site inhibitor binds noncovalently at site other than active site Irreversible Atte

© Macmillan Learning Penalized Classify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive Reversible noncompetitive Answer Bank inhibitor does not alter the maximum reaction rate inhibitor structure resembles substrate structure inhibitor binds covalently and permanently at active site inhibitor binds noncovalently at site other than active site Irreversible Atte

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.33E

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In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
Based 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 38.4C
The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
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. It bonds covalently to the enzyme active site. b. The inhibitor effect can be reversed by the addition of more substrate. c. Inhibitor structure must be somewhat similar to that of the substrate. d. The inhibitor and substrate cannot bind to the enzyme simultaneously.
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
Write a brief description of the relationships among each of the following groups of terms or phrases. Answers to the Concept-Linking Exercises are given at the end of the chapter. Enzyme, enzyme substrate, active site, induced fit model
Based 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?
Classify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive Reversible noncompetitive Irreversible Answer Bank inhibitor binds covalently and permanently at active site inhibitor binds noncovalently at site other than active site inhibitor does not alter the maximum reaction rate inhibitor structure resembles substrate structure
Explain why an irreversible inhibitor of an enzyme might be more toxic to humans than a reversible inhibitor.
Please don't use hend raiting and step by step solutions
Part A Heavy metals such as lead and mercury are poisonous because they bind to and inhibit enzymes through which of the following mechanisms? > View Available Hint(s) reversible competitive inhibition reversible mixed inhibition uncompetitive inhibition irreversible inhibition Submit
Draw the structures of the substrate (pNPP) and of the inhibitors (Pi and Phe). Consider them in the fully deprotonated states. What similarities can you detect between each inhibitor and the substrate?