b) Briefly explain what happens to vo, rate of product formation, when it is affected by an allosteric inhibitor. This conformation of the enzyme active site is known as -state. c) True/False. Allosteric regulators alter the Vmax of an allosteric enzyme. Question 4. a) Briefly explain what happens to vo, rate of product formation, when it is affected by an allosteric activator. This conformation of the enzyme active site is known as _ -state. V₁ = kcat [ES]

b) Briefly explain what happens to vo, rate of product formation, when it is affected by an allosteric inhibitor. This conformation of the enzyme active site is known as -state. c) True/False. Allosteric regulators alter the Vmax of an allosteric enzyme. Question 4. a) Briefly explain what happens to vo, rate of product formation, when it is affected by an allosteric activator. This conformation of the enzyme active site is known as _ -state. V₁ = kcat [ES]

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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Similar questions

Describe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..
Discuss in a short paragraph (3–5 sentences for each mutation) whether or not the enzyme is likely to completely lose catalytic activity if the following mutations are carried out. You may assume that steric effects do not distort the active site so much that catalysis cannot take place; focus your analysis on discussing the chemistry the amino acid side chains are able to perform and the properties that enable them to do so. Mutation 1: H to E Mutation 2: H to N Mutation 3: S to D Mutation 4: S to C
If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:
Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins
A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?
Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis
3) Read the situations below and indicate which of the four methods of enzyme regulation is occurring for each. a) The energy-carrying molecule ATP is made by the enzyme ATP synthase. Muscle cells use a lot of energy and also have higher amounts of the ATP synthase enzyme than many other cell types. General mechanism of enzyme regulation: S b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as the perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzym called cyclo-oxygenase. "Ibuprofen" is the active ingredient in a variety of anti-inflammatory medications such as Motrin® and Advil®. It reduces pain and swelling by binding to a hydrophobic channel in the active site of cyclo-oxygenase, blocking the polyunsaturated fatty acids from binding to the enzyme, and therefore stopping production of prostaglandins. General mechanism of enzyme regulation:
a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme