multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation: 1. kcat >> k1 or k-1 2. In the presence of a negative allosteric effector 3. At low concentrations, the reaction is first order with respect to substrate concentration 4. At high concentrations the reaction is zero order with respect to substrate

multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation: 1. kcat >> k1 or k-1 2. In the presence of a negative allosteric effector 3. At low concentrations, the reaction is first order with respect to substrate concentration 4. At high concentrations the reaction is zero order with respect to substrate

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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multiple choice, choose the correct answer You stumble upon a potential inhibitor (I) for HIV protease, so you now have to perform a few experiments to characterize its behaviour. You find that if you add an excess of substrate to the reaction in the presence of inhibitor, enzyme activity increases but to only 0.5 Vmax to that observed in the absence of inhibitor. The affinity of the substrate for the enzyme is unaffected by the inhibitor. If you treated the enzyme with inhibitor, then dialyse the protein into a buffer solution without inhibitor, the activity is restored. What type of inhibitor is I?1. Uncompetitive2. Competitive3. Non-competitive 4. Irreversible
I am a bit confused about this PPT slide explanation. Why would a high energy transition state be favored when it requires more activation energy in an enzyme-substrate binding scenario?
An enzyme-catalyzes the isomerization of substrate S to product P. The enzyme has a molecular weight of 120,000 g/mol. In assays using 1 μg of enzyme per assay the Km was 3 x 10^-3M and the Vmax was 2.75 μmole per minute. What would be the Kcat (turnover number or molecular activity) of the enzyme under these conditions? 2.75 min^-1? 3,300,000 min^-1? 330,000 s^-1? 19,800,000 min^-1? 5,500 s^-1?
In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.
If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
Multiple choice correct answer and explain every point 2. The factors that contribute to the enhancement of the rate of reactionsa) Specific inhibitor macromoleculesb) Product inhibitionc) Availability of substrate and activator cofactord) Covalent catalysise) Proximity and orientation effects
Choose False during an enzyme catalyzed reaction. Substrate concentration is typically much larger than that of enzymes. The rate of enzymatic reaction is related to the concentration of ES complex. Velocity of reaction reaches a plateau above certain substrate concentration. Velocity of reaction is linearly dependent on a substrate concentration. Maximum velocity is related to the number of catalytic turnovers in the unit time.
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!
Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical reaction catalyzed. 9. The living cell is the site of tremendous…