6. An allosteric enzyme has which ofthe following properties?1. It can only operate in an acidicenvironment,2. It can only operate in an alkalineenvironment,3. It becomes active only when itbinds with a specific cofactor,4. It can function either as acatabolic or anabolic enzyme.

Allosteric enzymes are the enzymes that changes their conformation according to the binding of…

Answered: 6. An allosteric enzyme has which of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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1. The enzyme you are studying uses the substrate pictured at right. An inhibitor box in the freezer contains two tubes labeled Inhibitor #1 and Inhibitor #2, along with the structures of the compounds contained within them and their respective Ki. Which one is more likely to be the non-competitive inhibitor? Inhibitor #1 K₁ = 10 μM m CH₂OH OH -0, $ OH OH Inhibitor #2 K₁ = 50 μM Briefly Justify: OH CH₂OH OH OH OH Substrate
2. “Most enzymes are gene-encoded proteins." Using this lens, explain: A) effects of increased temperature on the rate of enzymatic reactions, and B) effects of decreased temperature on enzymatic reactions, and C) importance of optimal pH and ionic strength on enzymatic reactions.
4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain:
Match each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. Lyase
5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
20) Normally an enzyme has maximal enzyme activity at 37°C, but once it has been heated to 100°C and then cooled back down to 37°C the enzyme is no longer active. Why?
Which of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
which of the following describes an enzyme ALLOSTERIC site?
1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)
1. Which of the following are general properties of active sites? MARK ALL THAT APPLY. Group of answer choices Multiple interactions with substrate Not very specific Always hydrophobic Small pocket within enzyme.

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6. An allosteric enzyme has which of the following properties? 1. It can only operate in an acidic environment, 2. It can only operate in an alkaline environment, 3. It becomes active only when it binds with a specific cofactor,