11. (ME.23) Given the pathway below, steps catalyzed by enzymes,are good candidates for regulation and compoundnegatively regulate enzyme 5.A. All steps with -AG; compound HB. Steps catalyzed by enzymes 2 and 5 only; compound CC. Steps catalyzed by enzymes 4 and 5 only; compound HD. Steps catalyzed by enzymes 2, 4, 5, 6 & 8; compound CE. Steps catalyzed by enzymes 2, 4, 5, & 8; compound H Ais a good candidate toAG+0.1enz7AGAGAGHAGAG+1.1-23.3-0.7-1.4-16.7enz1enz2enz3AGenz4enz5-

Enzymes are high molecular weight protein compounds, exceptions are ribozymes. Enzymes are…

Answered: 11. (ME.23) Given the pathway below,…

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. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.
1. For enzymatic reaction, a mechanism was proposed by Michaelis and Menten as follows: ES k, and k,' ES à E and P k,. E + S a. Use steady state assumption, derive expression for the reaction rate. Where E is concentration of enzyme, S substrate, ES complex of E and S, E = E, – ES. (If you have difficulty in doing it, please consult lecture note) b. Assume K = 0.038 mol.L' at 25 °C, when the substrate concentration is 0.156 Mol.L', the rate of the reaction is 1.21 m mol/L.s. The maximum rate of conversion reaction is reached at high substrate concentrations. Calculate the maximum rate of this enzyme catalyzed reaction.
1. Amino acid side chains act as nucleophiles and proton donor/acceptors in various enzymatic reactions. We will use them frequently in reactions during 40B and therefore the purpose of this exercise is to review the properties of amino acid side chains you have learned in 40A. Ozempic is a medication used for the treatment of type 2 diabetes and an anti-obesity treatment. Ozempic is a modified peptide that mimics the structure of the natural hormone GLP-1. H-His-N GAU-G H₂C CH₂ Glu-Gly-Thr-Phe-Thr-Ser Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly Gin-Ala-Ala- a. NH H-His- no H₂C CH₂ au Pho Phe-lle Ala Trp Leu-Val-Arg Gly Arg-Gly-OH Add above the tree-letter code of each amino acid the relevant functional group on its side chain. OH I For example: -Ser- will be represented by Ser NH OH b. The protonation state of each functional group depends on the pH of the solution. Assume that Ozempic is in a solution at pH=7. Draw the functional groups at their correct protonation form. Gu-Gy…
Can you explain the answe?
6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
2. (Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? R CO₂H A R SCOA B R R
Q) Can a reversible enzyme be regulated by product inhibition? Justify your reasoning. (4 sentences MAX)
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
The enzyme -catalyzed reaction ratewill be increased if the energy level of ES can be increased by all EXCEPT: destabilization of ES by strain loss of entropy due to binding of E and S. destabilization of ES by distortion destabilization of ES by solvation destabilization of ES by electrostatic effects a. b. с. d. е.
Hb serves as our model for regulation of enzyme reaction rates. But Hb is not an enzyme. Explain the reasoning of Jacque Monod and his colleagues for invoking Hb as a "model enzyme."
7. To what main enzyme class do the enzymes that catalyze the following reaction belong? (Oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) со о 8. Label the following as examples of a "lock and key" model or an "induced fit" enzyme model? substrate a. b. tive sihe a. b. yme-bstrate comples
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

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