ChemistryMany drugs are competitive inhibitors of specific enzymes.For drugs that act as competitive inhibitors,the enzymes must be allosterically regulated.the substrate must be bound to the enzyme before the drug can bind.O the amount of drug needed to achieve the same effect is increased as the substrate concentration increases.the amount of drug needed to achieve the same effect is increased as the substrate concentration decreases.

The branch of chemistry which deals with the physical or chemical interactions of two substances on…

Many drugs are competitive inhibitors of specific enzymes. For drugs that act as competitive inhibitors, O the enzymes must be allosterically regulated. the substrate must be bound to the enzyme before the drug can bind. the amount of drug needed to achieve the same effect is increased as the substrate concentration increases. the amount of drug needed to achieve the same effect is increased as the substrate concentration decreases.

Many drugs are competitive inhibitors of specific enzymes. For drugs that act as competitive inhibitors, O the enzymes must be allosterically regulated. the substrate must be bound to the enzyme before the drug can bind. the amount of drug needed to achieve the same effect is increased as the substrate concentration increases. the amount of drug needed to achieve the same effect is increased as the substrate concentration decreases.

General, Organic, and Biological Chemistry

7th Edition

ISBN:9781285853918

Author:H. Stephen Stoker

Publisher:H. Stephen Stoker

Chapter21: Enzymes And Vitamins

Section: Chapter Questions

Problem 21.49EP

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Similar questions

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
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
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 site on an enzyme molecule that does the catalytic work is called the: a. binding site. b. allosteric site. c. lock. d. active site.
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?
Match the following enzymes and substrates: Enzyme Substrate a. sucrase b. amylase c. lactase d. maltase e. arginase maltose amylose sucrose arginine lactose
. 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?
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
The process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.
Describe the importance of zymogens in the body. Give an example of an enzyme that has a zymogen.