3. Some medications permanently inactivate their target enzyme by forming a covalent bond to an amino acid in the enzyme's active site. Aspirin is one example of a pharmaceutical that uses this type of mechanism. So is penicillin. As you saw in the last chapter, the active portion of penicillin is the B-lactam ring. Penicillin forms a covalent bond to serine in the active site of transpeptidase, an enzyme that is essential for forming the bacterial cell wall. Propose a mechanism for the inactivation of transpeptidase by penicillin and show the final product of the reaction. R. NH Он CH3 CH, -N- CH3 backbone

3. Some medications permanently inactivate their target enzyme by forming a covalent bond to an amino acid in the enzyme's active site. Aspirin is one example of a pharmaceutical that uses this type of mechanism. So is penicillin. As you saw in the last chapter, the active portion of penicillin is the B-lactam ring. Penicillin forms a covalent bond to serine in the active site of transpeptidase, an enzyme that is essential for forming the bacterial cell wall. Propose a mechanism for the inactivation of transpeptidase by penicillin and show the final product of the reaction. R. NH Он CH3 CH, -N- CH3 backbone

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

According to the following graph, the activity of the enzyme decreases more sharply at high temperature than at low temperature. What are the reasons for this observation? Enzyme activity Optimum temperature Temperature, °C I. As temperature is increased, the substrate binding slowly becomes poorer. II. As temperature is decreased, the enzyme moves more slowly and so reacts more slowly. III. At higher temperatures, the enzyme is denatured and stops working entirely. IV. Temperature has no effect on enzyme activity. ○ I only O IV only I and III O II and III
How does changing the concentration of enzyme at a fixed concentration of substrate affect the rate of decomposition of H2O2?
An enzyme has an optimal pH of 7.1 and an optimal temperature at 37° C. Which statement describes a reaction catalyzed by this particular enzyme at a constant temperature of 20° C? the reaction will slow down and then increase as the temperature increases O there is no effect O the reaction will be slower than if it ran at 37° C O the enzyme will provide an alternate active site so the reaction can proceed the enzyme will be denatured
Please don't use hend raiting and step by step solutions
How does the metal ion in carboxypeptidase A increase the enzyme’s catalytic activity.
Questions #58 and #59 please
The following graph is showing the effect of catalyzed reaction. Rate of reaction A enzyme concentration substrate concentration pH temperature B on the rate of an enzyme
Which of the following is not a property of enzyme? * Specificity Efficiency of the catalyst Active site Location within the cell None of the given options
9. Describe the binding between an irreversible inhibitor, such as arsenic, and an enzyme. 10. Explain the difference between reversible competitive and noncompetitive inhibition.
The following graph of an enzyme catalyzed reaction what does B represen Rate of reaction A B maximum velocity minimum velocity competitive inhibition non-competitive inhibition
Derive a general equation for the relative activity (a) of an enzyme in the presence of a competitive inhibitor.
The lock and key model and the induced fit model are two models of enzyme action explaining both the specificity and the catalytic activity of enzymes. Indicate whether each statement is part of the lock and key model, the induced fit model, or is common to both models. Lock and key model Induced fit model Common to both models Answer Bank The substrate binds to the enzyme at the active site, forming an enzyme-substrate complex. The substrate binds to the enzyme through noncovalent interactions. The enzyme conformation changes when it binds the substrate so that the active site fits the substrate. The enzyme active site has a rigid structure complementary to that of the substrate.