Answered: How can competitive and pure…

Science

Biochemistry

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

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: Please note the reaction expression below. Which of the following rate constants describes the…

A: Michaelis-Menten equation provides us with a general explanation of the velocity and gross mechanism…

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: Does the presence of a competitive inhibitor increase / decrease the apparent affinity of the…

A: There are three types of enzyme inhibitors. They are competitive, non-competitive and mixed…

Q: VA 256 192 128 9 1.5 10- 38 25- 19 125- 64. .032- .023 .047

A: The MIC, or minimum inhibitory concentration, is the lowest concentration (in μg/mL) of an…

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: If you performed a kinetic study of an irreversible inhibitor, such as penicillin, what would you…

A: The apparent Michaelis constant (Km) is unaffected by irreversible inhibitors, however, because the…

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: Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and…

A: Enzyme is a catalytic molecule that increases the rate of any chemical reaction without being used…

Q: Determine whether each of the inhibitors (or inhibitor characteristics) are involved in reversible…

A: Since you have posted a question with multiple sub parts, we will provide the solution only to the…

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: An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate)…

A: We need to draw the Lineweaver Burk (LB) plot to find out the answers. LB plot has 1/[S] as X-axis…

Q: Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and…

A: The Michaelis-Menten plot shows the relationship between substrate concentration and velocity of a…

Q: he Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo max [S] akm + a'…

A: Michaelis-Menten equation represents enzyme-catalyzed reactions with a single substrate. Based on…

Q: Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis,…

A: Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, is an antimicrobial enzyme…

Q: Triclosan is a broad-spectrum antibacterial agent used in many household products. It is…

A: Anti-bacterial agents are chemicals that have the ability to kill bacteria and limit their growth.…

Q: Which one of the following best explains the distinctive effect of an uncompetitive inhibitor on Km,…

A: Enzymes are the protein molecules which are of biological origins or sometimes may be produced…

Q: mTOR is a cytoplasmic kinase that regulates cell division. Its misregulation can lead to cancer. The…

A: Given; mTOR: Cytoplasmic kinase- regulates cell division Rapamycin: Allosteric inhibitor

Q: he figure below shows the dependence of the enzyme's rate, v (in uM/min), as a function of substrate…

A: Enzymes are biological catalysts speeding up rate of a chemical reaction. They are specific for…

Q: Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] k-1 + k2 [ES|…

A: Km : The concentration of substrate at which enzyme achieves half Vmax-maximum velocity

Q: a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and…

A: Enzymes catalyse biochemical reactions by lowering their activation energy. Enzymes bind to their…

Concept explainers

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.

Question

How can competitive and pure noncompetitive inhibition be distinguished in terms of K_M?

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

How Do Catabolism and Anabolism Differ? What are the features that generally distinguish pathways of catabolism from pathways of anabolism?
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.
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?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
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?
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
In the experiments of Aery, MacLeod, and McCarty, what was the purpose of treating the transforming extract with enzymes?
Would you describe metabolic pathways as inherently wasteful or inherently economical, and why?
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.
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