A reversible non-competitive inhibitor binds reversibly at a site other than the active site. This binding leads to a) increase in Km and Vmax remains constant. b) increase in Vmax and km remains constant c) decrease in Vmax and Km remains constant d) no change in Vmax and Km

A reversible non-competitive inhibitor binds reversibly at a site other than the active site. This binding leads to a) increase in Km and Vmax remains constant. b) increase in Vmax and km remains constant c) decrease in Vmax and Km remains constant d) no change in Vmax and Km

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter24: Chemical Communications: Neurotransmitters And Hormones

Section: Chapter Questions

Problem 24.12P

See similar textbooks

Related questions

Q: Arginine and lysine side chains fit into trypsin’s binding pocket (Figure 22.5). One of these side…

Q: 4. How MAP kinase cascade (MKP-1) logic of anti-cancer strategy and the expected outcome? (make…

A: 4. Answer - The MAPK cascades are central signaling pathways that regulate a wide variety of…

Q: a) This compound is an active HIV protease inhibitor b) This compound is an inactive HIV protease…

A: A virus that infects humans and mainly makes their immune system weak is known as the human…

Q: The effect of reversible competitive inhibitor can be cancelled by: increasing the product…

Q: Drugs called COX-2 inhibitors (e.g., Vioxx, Bextra, andCelebrex) were thought to relieve the pain…

A: An observation involves observing and describing any event. It is based on measurements or data.…

Q: Classify the inhibitor characteristics according to one of three types of inhibition: reversible…

A: Inhibitors are those substances which either binds with substrate or make a change in substrate such…

Q: 14.) A reversible inhibitor that is unable to bind to the ES complex A) always binds in the active…

A: Reversible inhibitor that is unable to bind to the ES complex is Competitive inhibitor.

Q: † 14.) A reversible inhibitor that is unable to bind to the ES complex A) always binds in the active…

A: que . 1 A reversible inhibitor that is unable to bind to the ES complex --B) may be an…

Q: Which type of inhibitor is shown in the diagram? non-competitive inhibitor uncompetitive inhibitor…

A: Given options, Non-competitive inhibitor Uncompetitive inhibitor All…

Q: Match the following: Active site adapts to shape of substrate Prevents substrate from entering…

A: This question is related to enzyme inhibition

Q: We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of…

Q: Selective COX-2 inhibitors are preferable than nonselective COX- inhibitors. How can selective COX-2…

A: COX- inhibitors are a type of non-steroidal inhibitors that directly targets cyclooxygenase- 2. It…

Q: How can we determine whether a reversible inhibitor acts by competitive, uncompetitive, or…

A: Enzymes are the biological catalysts that increase the rate of the reactions occurring inside living…

Q: If inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of…

A: Given: Reaction velocity (V0)1 = 0.10 mM/min [S]1 = 1.0 mM Reaction velocity (V0)2 = 0.133333 mM/min…

Q: 3GRS inhibitor sonra oda good ZVIX inhibitor 4ALD inhibitor 120Y inhibitor 2007 Th ofsa OH ON

A: Given:

Q: the advantages and the disadvantages of the catalyst a) aluminosilicate b) trypsin

A: Advantages of catalyst aluminosilicate - aluminum silicate is basically used to dry oozing and…

Q: The vast majority of serine protease inhibitors are competitive inhibitors. Which of the following…

A: Given statements, The Vmax of a reaction decreases in the presence of a competitive inhibitor. Km…

Q: how many drugs could we test for antitumor activity with a 51x41 grid ofcompounds?

Q: 8. Which of the following is true of a noncompetitive inhibitor? a. resembles the substrate b. binds…

A: The rate of a chemical reaction can increase with the help of certain substances. These substances…

Q: (a) What is the difference between a zymogen and an allosteric enzyme? (b) Why would the active…

A: (a) the difference between enzyme and zymogen is that enzyme is a globular protein that catalyses…

Q: 8. Identify the inhibitor from the following list for the selective target of the enzyme having C in…

A: o Acrylamide groups act as Michael acceptors and thus react with nucleophiles like thiol (SH) groups…

Q: Incubation with primary antibody should be accompanied with agitation, why?

Q: 7. 116.5 ug of trypsin (MW 23.3 kDa) was mixed in a l ml solution with an excess of a peptide…

A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…

Q: Which protein folding interaction(s) is/are most likely to occur on the outside of a protein pocket…

A: Hydrophobic effects describe the energetic preference of non polar molecular surfaces interacting…

Q: MCQ 25: Enzymes do not A. produce side products B. get consumed up during the process C. do not…

A: Enzymes are biocatalysts, which are chemically globular proteins. These have general Molecular mass…

Q: Molecule AE is and allosteric effector of an enzyme. In its presence, the curve of enzyme activity…

A: Allosteric effect is the binding of one molecules effect the binding of other molecules with…

Q: Comporund rat Contains ma8se teis substance?

A: Gha

Q: 42.) On a Lineweaver-Burk plot, a changing slope upon addition of increasing concentration of…

A: Hello. Since your question has multiple parts, we will solve the first question for you. If you want…

Q: A. Determine the type of interaction and what protein residues for the phenyl ring labeled 1. B.…

A: A question based on intermolecular forces, which is to be accomplished.

Q: Match the words in the left column to the appropriate blanks in The sentences on the right. Reset…

A: In the protein synthesis the inhibitors are the one which delays or stops the growth or…

Q: Following data were obtained for an enzyme in the absence and presence of an inhibitor. What are the…

A: Given data:

Q: Zinc was added to an enzyme-substrate solution and most enzyme activity ceased. Addition of more…

A: As zinc is added to an enzyme substate solution, most of the activities are ceased.

Q: What is the relative activite and the degree of inhibition caused by a competitive inhibitor when…

A: Degree of inhibition The introduction of an internal control—the rate of the uncontrolled…

Q: 21. Which of the following is true of a noncompetitive inhibitor? a. resembles the substrate Ob.…

A: Welcome to bartleby ! Introduction : We have to tell which statement is true about non competitive…

Q: Enzyme activity can be controlled by availability of substrates and cofactors. U The binding of a…

A: Answer - The correct option is -(1) and (5) Solution - According to the question - proteolysis,…

Q: Which of the following signaling proteins have kinase activity (select all that apply)? Insulin…

Q: 2. Which is a false statement regarding non-competitive enzyme inhibitor? (a) It binds to an…

A: 2.) In non-competitive inhibition, the inhibitor does not bind on the active site, it rather binds…

Q: An enzyme catalyzes the reaction M ⇌ N. The enzyme is present at a concentration of 1 nM, and the…

Q: Each compound was tested for its ability to inhibit fatty acid synthase activity in both normal…

A: inhibition of fatty acid synthase in cancer cells by various compounds.

Q: Which interaction(s) is/are involved in the primary structure of a protein (choose all that apply)?…

A: We know that primary structure of protein is the linear sequence of amino acids in a peptide or…

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

A: Various inhibitors shows various affects on the LineWeaver-Burk plot . To check which type of…

Q: The Km value of an enzyme is affected in the presence of a competitive inhibitor because it requires…

Q: Classify each specific inhibitor or inhibitor characteristic according to one of two types of…

A: The solution is given below -

Q: STRENGTH (small,med,large) REACTION OF pH/ SAMPLE med butbles large pudbles bussees Vineegar Baking…

A: The explanation is given below-

Q: 460 410 360 310 260 210 160 110 60 -10 -510 4 5 10 15 20 25 30 35 40 45 50 55 1/[S] per mM 1. What…

A: Michaelis Menten equation shows the effect of the concentration of the substrate on the rate of an…

Q: STRENGTH OF REACTION SAMPLE (small,med.large) +++ large bubbley Small bubbles mo reaction |LIVER…

A: To determine the catalase activity, we would first define what is catalase and then we would learn…

Question

A reversible non-competitive inhibitor binds reversibly at a site other than the active site. This binding leads to

a) increase in Km and Vmax remains constant.
b) increase in Vmax and km remains constant
c) decrease in Vmax and Km remains constant
d) no change in Vmax and Km

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, chemistry and related others by exploring similar questions and additional content below.

Similar questions

How is the Km value influenced in the presence of the inhibitor?
Each compound was tested for its ability to inhibit fatty acid synthase activity in both normal cells and breast cancer cells. ID50 values (the inhibitor concentration required to inhibit cell growth by 50%) are shown in the table. Which inhibitors are most effective? Compound Alkyl side chain (R) Breast cancer cellsID50 (µg/mL) Normal cellsID50 (µg/mL) A −−C13H27 3.9 10.6 B −−C11H23 4.8 29.0 C −−C8H17 5.0 21.3 D −−C6H13 8.4 12.4 Compound D Compound C Compound A Compound B
1. What is the role of initiator and inhibitor? 2. What are short stops?
If we made a Lineweaver-Burk plot of an irreversible inhibitor, which type of reversible inhibition would it be most likely to resemble?
How can we determine whether a reversible inhibitor acts by competitive, uncompetitive, or noncompetitive inhibition?
Question: How can the rational design of small molecule inhibitors be optimized to improve their potency and selectivity?
1) This a model for what type of inhibitor? a) Competitive b) Uncompetitive c) Mixed d) Pure noncompetitive e) All of the above f) None of the above
How is the maximal rate of the enzyme changed in the presence of an inhibitor?
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
Is the inhibitor competitive, uncompetitive or non competitive and why?
If inhibitor X changes maltase activity to a Vo of 0.10 mM per minute when [S] = 0.125 mM, and a Vo of 0.25 mM per minute when [S] = 0.50 mM, calculate the new Vmax. 0.10 mM per minute 0.20 mM per minute 0.50 mM per minute 1.0 mM per minute 2.0 mM per minute
Which type of inhibitor is shown in the diagram? non-competitive inhibitor uncompetitive inhibitor all inhibitors have same effect on Km and vmax competitive inhibitor Attached photo shows the diagram.