Q2: Example of a question that requires understanding of the basic energetics of enzyme action Below is a reaction coordinate diagram for a chemical reaction (conversion of S to P) carried out without an enzyme (dashed black line) and with an enzyme (solid black line). Analogous to the Michaeils- Menten analysis, this diagram is only considering the energy of the enzyme-substrate complex (ES) and not the enzyme-product complex (EP). The numbered blue arrows are indicating the differences in free energy (AG) between different states. ES P Reaction coordinate A) Which number(s) correlate with the overall equilibrium constant of the reaction (i.e. for S S P)? B) Which number(s) correlate with the initial velocity of the reaction without enzyme (i.e. starting from substrate alone)? C) Which number(s) correlate with the initial velocity of the reaction with enzyme (i.e. immediately after mixing substrate and enzyme)? 5. 4) Free energy, 6

Q2: Example of a question that requires understanding of the basic energetics of enzyme action Below is a reaction coordinate diagram for a chemical reaction (conversion of S to P) carried out without an enzyme (dashed black line) and with an enzyme (solid black line). Analogous to the Michaeils- Menten analysis, this diagram is only considering the energy of the enzyme-substrate complex (ES) and not the enzyme-product complex (EP). The numbered blue arrows are indicating the differences in free energy (AG) between different states. ES P Reaction coordinate A) Which number(s) correlate with the overall equilibrium constant of the reaction (i.e. for S S P)? B) Which number(s) correlate with the initial velocity of the reaction without enzyme (i.e. starting from substrate alone)? C) Which number(s) correlate with the initial velocity of the reaction with enzyme (i.e. immediately after mixing substrate and enzyme)? 5. 4) Free energy, 6

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions

Section14.7: Reaction Mechanisms

Problem 1.2ACP

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1. For an enzyme to catalyze a reaction, it must preferentially stabilize the transition state (TS) of the reaction. If an enzyme instead preferentially stabilizes the enzyme-substrate complex (ES), it fails to catalyze the reaction. Justify this observation using a reaction coordinate diagram (free energy (G) vs. reaction coordinate).
One of the free energy (G)-reaction coordinate graphs given below belong to a ligand-binding protein, while the other two belong to two different enzymes. A)Which of the given graphs cannot belong to an enzyme? A, B or C Choose one of the options and explain your reasoning in one or two sentences. B)What does it mean if an enzyme has reached catalytic perfection? means? Which of the graphs of free energy change given above Could it belong to a catalytically perfect enzyme? C)what kinetic parameter/combination of parameters an enzyme shows its efficiency / whether it has reached catalytic perfection? D)Which step in the Michaelis-Menten mechanism is the rate of diffusion? limited to?
7. The following questions deal with a fundamental understanding of enzyme catalysis. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high [S]?
What are the principle and basic concepts of ACID FAST CHAIN? (please explain it thoroughly in a lengthy but clear explanation, thank you so much.)
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An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constant Kd,S of the enzyme-substrate complex ES is 1 mM, for EC it is 10 mM. When the cofactor C is present, Kd,s ’ is decreased to 0.1 mM. What is the value for the dissociation constant Kd,C ’ of the enzyme-cofactor complexing the presence of substrate S? Calculate the interaction energy DDGint for cofactor and substrate binding.
Consider the simple reaction S <--> P, with the forward rate characterized by a rate constant k1, the reverse rate constant characterized by a rate constant k2, and the equilibrium constant for the reaction given by Keq. Which of the listed effects would be brought about by an enzyme catalyzing this reaction?a) increased Keqb) increased k1c) decreased transition state free energy changed) increased k2
In the "Catalysis by Preferential Transition State Binding" mechanism, the substrate perfectly fits with the enzyme binding site after its geometry gets changed. Who does it? And how?
If the AG" of the reaction A --> B is +40 kJ/mol, under standard conditions the reaction: will proceed spontaneously from A to B. ) is endergonic. is at equilibrium. will never reach equilibrium. The number of substrate molecules converted to product in a given unit of time by a single enzyme molecule at saturation is referred to as the: half-saturation constant. Michaelis-Menten number. O turnover number. maximum velocity. dissociation constant.
Enzyme kinctics a. How to determine Km and Vmax of a-glucosidase enzyme isolated from weathered rice b. Curcumin is expected to inhibit the activity of the a-glucosidase enzyme. How to determine the inhibitory activity of curcumin against a -glucosidase? c. If the results of experiment number 3b are known that curcumin can inhibit a -glucosidase, how to determine the type of inhibitor?
The peak on the blue line marked by the #3 represents which of the following? Free energy, G Transition state (#) S 2 (3) EST EP AG* P uncat Reaction coordinate AG* cat Solvation of the product and the active site of the enzyme.. The energy required for the enzymatic conversion of substrate to product. O Desolvation of the product and the active site of the enzyme.. The binding energy (AGB) of the substrate binding the enzyme.