Answered: What are prodrugs? How is the…

Science

Biochemistry

What are prodrugs? How is the therapeutic effect of a prodrug affected by enzyme inhibition and induction?

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter9: Cell Communication

Section: Chapter Questions

Problem 17RQ: What is the effect of an inhibitor binding an enzyme? The enzyme is degraded. The enzyme is...

See similar textbooks

Related questions

Q: What is the relationship between the cooling of organs and tissues for medical transplants and the…

A: For patients with a terminal illness, organ transplantation is the most effective therapy. The…

Q: a compettitive inhibitor interferes with?

A: The enzyme generally binds with the substrate but in competitive inhibition, the inhibitor is…

Q: What is the mechanism of chymotrypsin catalysed by enzymes without cofactors?

A: CHYMOTRYPSIN is a digestive enzyme of pancreatic juice acting on the duodenum where it performs…

Q: What are the possible effects and changes on the Michaelis-Menten equation that can result from…

A: Michaelis-Menten equation: An equation that states the rate at which one substrate enzyme-catalyzed…

Q: How does penicillin binding stop the enzyme from functioning?

A: Penicillin: It is a class of antibiotics. Penicillin was generated from Penicillium moulds. There…

Q: What are the four key types of irreversible inhibitors that can be used to study enzyme function?

A: An enzyme is defined as a substance that is capable of accelerating the rate of a biochemical…

Q: What is the difference between competitive and noncompetitive inhibitors?

A: Competitive inhibitionIn competitive inhibition, an inhibitor molecule competes with a substrate by…

Q: Given the active site and reaction mechanism, identify the mechanism of irreversible inhibition for…

A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…

Q: Do Non-competitive inhibitors have medicinal uses? Give one example and explain

A: Non-competitive inhibitors are inhibitors that reduce the activity of an enzyme by binding to the…

Q: Can enzyme inhibition be reversed in all cases?

A: Enzymes can be regulated to increase or decrease their catalytic activity. When it comes to…

Q: What is enzyme immobilization? What are the different methods of enzyme immobilization? What are the…

A: Enzymes are known as biological catalysts in which help to catalyze the different biochemical…

Q: What is the difference between competitive and non-competitive inhibition?

A: The activity of the enzyme can be inhibited wither reversibly or irreversibly. Irreversible…

Q: What are the cellular advantages to feedback inhibition?

A: Feedback inhibition is a cellular control mechanism in which an enzyme's activity is inhibited by…

Q: What is the source of Chemokines?

A: The heparin binding proteins that direct the movement of circulating leukocytes to the site of…

Q: What is purine catabolism?

A: Nucleic acids are the major class of biomolecules that are important for all forms of the organism.…

Q: What is contact inhibition?

A: Contact inhibition is a phenomenon shown by the normal cells in the animals which involves when two…

Q: Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition…

A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…

Q: two other enzymes that are used in therapeutic use in humans and why they do not affect human cells?

A: ENZYMES:- It is defined as a complex biological catalyst i.e produced by living organisms in its…

Q: Why does the apparent KM decrease in the presence ofan uncompetitive inhibitor?

A: An enzyme inhibitor is a molecule that binds to enzyme and decreases its activity. By binding to the…

Q: What is the importance in glycosylation in rtPA in terms of its activity as a protein therapeutic?

A: Tissue plasminogen activator (tPA) is a serine protease that catalyzes the formation of plasmin…

Q: How will raising the temperature affect the regulation of RodA? what are the possible results and…

A: Introduction :- Temperature effects different biological processes and structures differently . The…

Q: What are the mechanism of action for proton pump inhibitors (PPIs).

A: PROTON PUMP INHIBITORS- Proton pump inhibitors are a type of drug that works by inhibiting the…

Q: Under what conditions, a higher rate in the presence of the inhibitor observed? (how could the…

A: There is a gradual increase in reaction rate because competitive inhibitors are occupying only some…

Q: What is the difference between pure and mixed noncompetitive inhibition?

A: Pure competitive inhibition is the type of inhibition in which the inhibitor binds to the site other…

Q: Does the behavior of allosteric enzymes become more or less cooperative in the presence of…

A: Introduction: Cooperativity is a phenomenon where the binding of more than one ligand on a protein…

Q: How are H^3 peptides used to study intracellular pathways?

A: A chain of reactions that transmits signals from the cell surface to intracellular targets. This…

Q: What is TCA? What are the different enzymes involved in TCA? What are the important products in…

A: Cellular respiration is a series of metabolic reactions and activities that occur in organisms'…

Q: Where is the site of action of inhibitor 2?

A: Inhibitors are the substances that interrupt the interaction of enzyme and substrate complex.

Q: What role do low-barrier hydrogen bonds play in serine protease catalysis?

A: A low barrier hydrogen bond is a special type of hydrogen bond which can occur when the pKa of the…

Q: How is the importance of folic acidrelated to chemotherapy?

A: Folic acid is the synthetic form of folate which is a naturally occurring B vitamin. It helps to…

Q: What exactly are prodrugs? How do enzyme inhibition and induction impact the therapeutic action of a…

A: Before demonstrating pharmacological effects, prodrugs go through a metamorphosis. They are composed…

Q: What are the two essential amino acids in the active site of chymotrypsin?

A: Serine-195 and Histidine-57 (involved in catalytic actions) are the two essential amino acids in…

Q: What are the meanings and differences between Ki, Km, and IC50? Are there certain advantages or…

A: Enzymes are biocatalyst. They speed up the rate of biochemical reaction. Enzyme binds with substrate…

Q: What roles do proximity and orientation play in enzymatic catalysis?

A: Enzymes are the catalytic protein which helps to produce the product when the enzyme act on the…

Q: How can competitive and pure noncompetitive inhibition be distinguished in terms of KM?

A: Km is also known as Michaelis constant. It is one of the parameters to determine enzyme activity.…

Q: What is the need of adding DNS solution to the enzyme substrate solution? What is the problem in…

A: The substance which helps to catalyze the living organisms is called an enzyme. It helps in the…

Q: What happened if we add normal saline instead of PBS during beta-amylase extraction?

A: Most enzymes are proteins. Their catalytic activity depends on the integrity of their native…

Q: What is a pacemaker enzyme? Feedback inhibition? How does feedback inhibition automatically adjust…

A: Pacemaker enzyme and feedback inhibition are the terms generally utilized in medical writing. The…

Q: How do the critical amino acids catalyze the chymotrypsin reaction?

A: Chymotrypsin is synthesized in the pancreas as a precursor called chymotrypsinogen that is…

Q: Explain the importance of Stemoamide ?

A: Stemoamide is a tricyclic alkaloid compound extracted from the plant Stemona tuberosa Lour. These…

Q: When the enzyme is incubated with oxaloacetate, will oxaloacetate be observed?

A: Many amino acid biosynthetic pathways involve transamination reactions. The α-amino group from one…

Q: Why are uncompetitive and mixed inhibitors generally considered to be more eff ective in vivo than…

A: Enzyme inhibitors are those that block the enzyme activity. Enzyme inhibitors are of several types.

Q: What is the site of action of inhibitor 1?

A: inhibitors are the compounds that modify the catalytic properties of the enzyme and, therefore, slow…

Q: Inhibition of oxamic acid causes what type of inhibition?

A: Oxamic acid is an organic acid with the molecular formula H2NC(O)CO2H. Oxamic acid is synthesized…

Question

100%

12. What are prodrugs? How is the therapeutic effect of a prodrug affected by
enzyme inhibition and induction?

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.

Similar questions

1. Explain the formation of thioether-linked prenyl anchor proteins and also explain the structure of caveolae.
1. What is the significance of the different diameters of zones of inhibition?
1. What is the action of invertase? 2. What is the reagent used to detect glucose in the detection of invertase? What is its principle?
What is the effect of an inhibitor binding an enzyme? The enzyme is degraded. The enzyme is activated. The enzyme is inactivated. The complex is transported out of the cell
1. Why is the use of monosodium glutamate (MSG) highly debated?
1. Explain chemotherapy in terms of specific inhibition 2. Explain why enzyme activity declines at (a)high temperature and (b) presence of heavy metal ions.
6. If inhibitor X changes lactase activity to a Vo of 0.333333333333 mM per minute when [S] = 2.0 mM, and a Vo of 0.50 mM per minute when [S] = 3.33333333333 mM, calculate the new Vmax. 1.0 mM per minute 2.0 mM per minute 2.5 mM per minute 5.0 mM per minute 10.0 mM per minute 7. Calculate the new Km of the lactase reaction with inhibitor X. 1.0 mM 2.0 mM 2.5 mM 5.0 mM 10.0 mM 8. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. 1.0 per minute 2.0 per minute 2.5 per minute 5.0 per minute 10.0 per minute Inhibitor X exerts which of the following effects on the above enzyme (lactase)? uncompetitive inhibition mixed noncompetitive inhibition competitive inhibition pure noncompetitive inhibition all of the above
1. Write the ten reactions of the glycolytic pathway, naming all enzymes and providing the structural formulas of their substrates and products.
5.Aspirin isthedrug,used for the decreasing ofinflammatory reaction and temperature. 1)Describe the mechanism of aspirin action. 2) What types of reversible inhibition do you know.3)Give the examples of drugs acting as such inhibitors.
1.Why do you think glutathione occurs in a concentration as high as glucose? 2.Explain why glutathione must be transported from cytosol to mitochondria. 3.Explain why glutathione can confer therapeutic benefit when taken orally.
1. Explain the biochemical formation of creatinine, urea, and uric acid. 2. State the principle of the Jaffe (end-point, and kinetic) and the enzymatic methods for measuring creatine.
2. Which of the following statements is TRUE about phosphofructokinase-1? Select one: a. It is stimulated by AMP and ADP. b. It is inhibited by AMP and ADP. c. It is stimulated by citrate and ADP. d. It is stimulated by citrate and ATP.