Answered: Please name the differences between…

Science

Biology

Please name the differences between competitive and noncompetitive inhibition.

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.5: Blood Glucose And Hemoglobin A1c

Problem 8RQ

See similar textbooks

Related questions

Q: Which of the following statements about non-competitive inhibitors is true? A) They bind at the…

A: Inhibitors are specific chemicals which binds to an enzyme shuts off the enzyme activity and this…

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

A: An enzyme inhibitor is a molecule that will bind to an enzyme to decrease or slow down its activity.…

Q: A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for…

A: Lineweaver-Burk plot is also known as the double reciprocal plot. Plot between the reciprocal of…

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: 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: PMSF is a protease inhibitor that binds to enzyme active site. What is the possible mode of…

A: A competitive inhibitor is a molecule that competes with the substrate to get bind to the enzyme…

Q: Please fill in the four boxes bolded below you KM (MM) Vmax (nM/s) Type of inhibition…

A: Competitive inhibitors are the substances which are similar to substrate molecules in their…

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: If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the…

A: Enzymes are substance produced by a living organism which acts as a catalyst to perform specific…

Q: The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm +…

A: Hence solved.Km=[S][αV0Vmax−1]Explanation:Determine the rate constant's expression, r.First, in…

Question

Please name the differences between competitive and noncompetitive inhibition.

Expert Solution

This question has been solved!

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

SEE SOLUTION Check out a sample Q&A here

Step 1: Introduction:

Step 2: Explanation:

Step 3: Explanation:

Solution

Step by step

Solved in 4 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, biology and related others by exploring similar questions and additional content below.

Similar questions

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.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
How Do Catabolism and Anabolism Differ? What are the features that generally distinguish pathways of catabolism from pathways of anabolism?
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
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.
An allosteric inhibitor does which of the following? Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding Binds to the active site and blocks it from binding substrate Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate Binds directly to the active site and mimics the substrate.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.