Compare and contrast types of inhibition based on information given. Part 1 Complete Table by replacing double question marks (??) with one of the types inhibition indicated below and single question marks with Increase, Decrease, c No change in velocity compared with control Restrict inhibition to the following types • Change • Competitive • Non-competitive Uncompetitive None Trial Km Vmax (S) [Cofactor] V (dp/dt) Inhibition Control 1 1 1 0.5 ?? 1 Decrease Increase 1 Increase 3 ?? 1 1 ?? 1 [E;) represents total enzyme concentration Part 2 Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics Identify the trials that could be explained by allosteric inhibition. Explain. Identify the trials that could be explained by allosteric activation. Explain

Compare and contrast types of inhibition based on information given. Part 1 Complete Table by replacing double question marks (??) with one of the types inhibition indicated below and single question marks with Increase, Decrease, c No change in velocity compared with control Restrict inhibition to the following types • Change • Competitive • Non-competitive Uncompetitive None Trial Km Vmax (S) [Cofactor] V (dp/dt) Inhibition Control 1 1 1 0.5 ?? 1 Decrease Increase 1 Increase 3 ?? 1 1 ?? 1 [E;) represents total enzyme concentration Part 2 Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics Identify the trials that could be explained by allosteric inhibition. Explain. Identify the trials that could be explained by allosteric activation. Explain

Case Studies In Health Information Management

3rd Edition

ISBN:9781337676908

Author:SCHNERING

Publisher:SCHNERING

Chapter4: Revenue Management

Section: Chapter Questions

Problem 4.14.5C

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Inhibitors of acetylcholinesterase, such as edrophonium, are used to treat Alzheimer’s disease. The substrate for acetylcholinesterase is acetylcholine. Structures are attached. What kind of inhibitor is edrophonium? Explain. Can inhibition by edrophonium be overcome in vitro by increasing the substrate concentration? Explain. Does this inhibitor bind reversibly or irreversibly to the enzyme? Explain.
For the competitive, noncompetitive and uncompetitive inhibition type investigate following figures and determine relationship between inhibitor concentration and Vmax and Km for each mechanism.
5.5 Explain the effect of each type of inhibitor on the apparent kinetic parameters: (1) Inhibitor binds only free enzyme does Km increase, decrease, not change? does Vmax increase, decrease, not change? (2) Inhibitor binds only ES complex does Km increase, decrease, not change? does Vmax increase, decrease, not change? (3)Inhibitor binds E and ES equally does Km increase, decrease, not change? does Vmax increase, decrease, not change?
What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
Using equilibrium argument, why does Km apparently increase, decrease or stay the same in uncompetitive inhibition?
The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. Substrate concentration, [S], has units of micromolar, μM. Enzyme velocity, ?0, has units of micromole per minute, (μmol/min). Using data from only the extremes of the [S] range is unreliable. Select the type of inhibition displayed by inhibitor A. competitive noncompetitive uncompetitive Select the type of inhibition displayed by inhibitor B. competitive noncompetitive uncompetitive
List 4 major types of inhibition modes and clearly indicate the effect on Vmax and KM for each mode?2. What is the effect of each of the 4 types of inhibitors on the initial rate of an enzyme catalyzed reaction?3. A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?4. Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.
Hypothetical scenerio: When the membrane potential is 80mV across the digestive vacuoles (DV), inside positive, the Vmax for VF-6-2 efflux is 15pmol/h. However, when the membrane potential is 80mV inside negative, the Vmax of VF-6-2 efflux drops to near zero. Researchers suggest an H+ P-type ATPase is also in the membrane and is required for VF-6-2 efflux. Do these data support their suggestion? What type of transporter might PfCRT be? How can vanadate be used to potentially test their idea?
name and explain the model that most likely accounts for cooperativity in enzymeNADH Also indicate why this is the most likely model.
If intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.
The nerve gas sarin acts as a poison by covalently bonding to a hydroxyl group in the active site of the enzyme acetylcholinesterase. This binding results in a higher-than-normal amount of acetylcholine at a nerve synapse, resulting in muscle spasms. From this description, would you expect sarin to be a competitive, noncompetitive, or irreversible inhibitor? noncompetitive inhibitor irreversible inhibitor competitive inhibitor