Answered: How can inhibitor binding to an enzyme…

Science

Biochemistry

How can inhibitor binding to an enzyme be quantified?

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter7: Basic Clinical Microbiology

Section7.7: Bacterial Identification And Antibiotic Susceptibility Testing

Problem 11RQ

See similar textbooks

Related questions

Q: For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value…

A: An enzyme is a biological catalyst and is almost always a protein. It speeds up the rate of specific…

Q: a compettitive inhibitor interferes with?

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

Q: Match the different names for inhibition mechanisms (1-5) with a description of their properties…

A: An inhibition mechanism refers to the process by which a substance or molecule, called an inhibitor,…

Q: What is the effect of each of the 4 types of inhibitors on the initial rate of an enzyme catalyzed…

A: Inhibitors of enzyme catalyzed reactions are broadly classified into reversible and irreversible…

Q: describe the mechanism of each class of inhibitor, including how they impact the effective…

A: There are mainly four types of inhibitors . Competitive inhibitor Non-competitive inhibitor…

Q: Inhibitors of acetylcholinesterase, such as edrophonium, are used to treat Alzheimer’s disease. The…

A: Inhibitor of an enzyme can be reversible or irreversible. The reversible inhibitors are those whose…

Q: How can we tell whether a reversible inhibitor inhibits in a competitive, noncompetitive, or…

A: Reversible inhibition refers to inhibition that does not result in a permanent change in the…

Q: A C -1/a K 1-a' Wen a'Nmax (a-1) Var 1/v₂ 1/5) Slope - akma (1) a=1+- am 1 (no inhibitor) Increasing…

A: The Lineweaver–Burk plot or the double reciprocal plot is a graphical representation of the…

Q: (c) When [S] = 0.0004, what will Vo be in the absence of inhibitor? (d) When [S] = 0.0004, what will…

A: Km is the MM constant which is used as an affinity measurement for an enzyme. Km is equal to the…

Q: C) Mixed inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme do…

A: Inhibitors are the substances which inhibit the enzymes from performing its catalytic role in the…

Q: Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor…

A: Ki is the inhibitor constant, that tells how potent an inhibitor is. It gives an idea of the…

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: . Based on what you know about enzyme inhibition, classify the following examples as irreversible,…

A: “Since you have posted a question with multiple sub-parts, we will solve first three subparts for…

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: sing equilibrium argument, why does Km apparently increase, decrease or stay the same in…

A: Inhibition in biochemistry occurs in different enzymes. Inhibition of enzymes means blocking or…

Q: A) Competitive inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme do…

A: The competitive inhibitor is a type of inhibition process in which an enzyme is analogous to the…

Q: Match the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: Can increasing enzyme concentration overcome the effects of an inhibitor?

A: Enzyme inhibitors decreases the activity of a reaction by interfering with the enzyme catalysis…

Q: Noncompetitive inhibition can often be explained by which of the following models? the induced fit…

A: The action of enzyme depends on different factors. Enzymes are biocatalysts in nature. All the…

Q: Activity of threonine deaminase

A: Enzymes are biological catalysts that speed up the chemical reaction by lowering activation energy,…

Q: Why might an enzyme’s substrate, transition state, and product all serve as starting points for the…

A: Enzymes are proteins, which acts as a catalyst and helps to convert substrate into the product,…

Q: Regarding the physical condition (characteristics of the solution/environment) in which an enzyme…

A: Enzymes are large molecular weight proteins that catalyse biochemical reaction. An enzyme's…

Q: For a weak ester drug that is unstable in highly acidic or alkaline solutions, what strategies could…

A: Bioavailability relates to the ability and rate of the active ingredient (drug or metabolite) that…

Q: One of the hallmarks of competitive inhibition is that there is constant competition between the…

A: Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an…

Q: Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct…

A: Metabolic pathways are of two types. They are Catabolic pathways in which larger compounds are…

Question

How can inhibitor binding to an enzyme be quantified?

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

If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
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
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
With regard to enzymes, why are vitamins necessary for good health? Give examples.
The ability of an enzymes active sites to bind only substrates of compatible shape and charge is known as ________. selectivity specificity subjectivity specialty
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Explain in your own words how enzyme feedback inhibition benefits a cell.
In the experiments of Aery, MacLeod, and McCarty, what was the purpose of treating the transforming extract with enzymes?
What is the primary difference between a circular pathway and a linear pathway?
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.