Shown below is a substrate for a Trypsin.Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw thecatalytic triad, and show the role of the oxyanion hole. Draw the complete structure of everyintermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R'H₂N_N_CH.сноCH₂CH₂CH₂NHd=19H₂NH₂OCH-H₂CHNOCH

Trypsin is an enzyme which is normally present in living organism to digest proteins but it is also…

Answered: Shown below is a substrate for a…

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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I don't understand it. Can u help me? Can u help me to explain this to me, please
Draw me the inhibition reaction mechanism of Cysteine Protease Inhibitor (E64). How the epoxide ring is opening because of the reaction with the thiol group of cysteine and what product are being made. Please draw with arrow pushing and also explain the reason of each attack.
S 1 CH₂ ✪ NH3 0=0 H₂C HN 6 NH CH₂ 'S Co A L CH₂ NH 4. Describe the role of His in the catalytic mechanism shown.
(b) The values of kinetic parameters for a variety of synthetic ester and peptide substrates ofa- chymotrypsin are compared for the reaction scheme below where ES is the Michaelis complex, ES' E+S Substrate K₁ N-Ac-Trp–OC₂H5 N-Ac-Phe-OC2H5 N-Ac-Leu-OC2H5 N-Ac-Phe-CONH2 N-Ac-Tyr-p-nitro-anilide ES K₂ 3.5 13.0 3.2 1.7 K-₁ is the acylenzyme, P₁ is the first product to be released, P2 is the second product, k2 is the acylation rate constant, k3 is the deacylation rate constant, and kcat = k2 k3/( k2 + k³). In the table below, N- Ac = N-acetyl; -CONH₂ = carboxamide; -OC₂H5 = ethyl ester; p-nitroanilide = −NH-C6H4-NO2 simulating a peptide group. ES' K2 (S-¹) K3 (S-1) 0.84 2.2 0.19 P₁ K3 0.073 H → E+ P2 Kcat (S-1) 0.82 1.9 0.18 0.070 0.038 KM (MM) 0.08 1.3 4.2 24.0 0.35 1 Kcat/ KM (mM-¹ s¯¹) 10.3 1.5 0.04 0.003 0.11 The value of kcat for N-Ac-Phe-OC2H5 is two-fold greater than that for the L-tryptophanyl analog and more than 10-fold greater than the value of kcat for the ester substrate…
One of the steps in psilocybin biosynthesis is the phosphorylation of 4-hydroxytryptamine By the enzyme Psik as shown below, that involves the hydrolysis of ATP. NH₂ OH HO Psik HO of A& ADP 4-hydroxytryptamine ATP norbaeocystin The standard free energy changes for each reaction is shown in the Table below. J reaction 4-hydroxytryptamine + P₁ → norbaeocystin ATP → ADP+ Pi (b) What is the equilibrium constant at 37 °C? AG 27.7 kJ/mol -32.2 kJ/mol (a) Write the net reaction. What is the standard free energy change for the net reaction? (c) In the cell, the concentration of ATP is 3.1 mM, the concentration of P; Is 5.90 mM, and the Concentration of ADP is 220 μM. What will AG Be if the concentration of norbaeocystin Is always kept at 1/100 of the concentration of 4-hydroxytryptamine?
Which of the following statements regarding the catalytic mechanism of superoxide dismutase is true? The D residue does not participate in acid-base catalysis during the course of the catalyzed reaction All of the answers are true The coordinated Zn2+ participates in stabilizing Cu²+ in the reduction-oxidation reactions to consume O₂ The Cu²+ coenzyme is coordinated by H residues, positioning it precisely for consumption of 0₂ The overall reaction consumes two equivalents of O₂ and two proton equivalents in order to produces one equivalent H₂O2
NH3 H-SCO A LES NH CH₂ NH CH₂ CH₂ 3 H-SCO A H3C SCO A 5. Describe the role of His in the catalytic mechanism shown.
1967, Rabin demonstrated that a single substrate reaction catalised by an enzyme that has a single binding site for the substrate, can show sigmoidal kinetics. Discuss this scenario so that it is clear why a plot of Vo versus [SJ at fixed total enzyme concentration will be sigmoidal.
1. - - Substrate Enzyme - 1 2 3 BOO - Look at the above diagram and understand what is being shown. Explain AND draw a graph depicting how the rate of the reaction depicted here is changing. ☐ L 2. How will the rate of the reaction change with time after 3? How can we increase the rate of the reaction after 3? I 100 B L
If the allosteric coefficient for ATCase increases from 250 to 1300, the rate of the N-carbamoylaspartate formation: O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts up. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O increases and the sigmoidal curve of reaction rate as a function of substrate shifts to the left. O stays the same and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. O decreases and the sigmoidal curve of reaction rate as a function of substrate shifts to the right. Question 9 Which of the following CANNOT be targeted for phosphorylation to modulate the activity of an enzyme? O Ser Ala O None of the amino acids listed can be targeted for phosphorylation to modulate enzyme activity The Tyr
protease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by half
Bypass reaction in the anabolic pathway often occurs when A The ΔG of the reverse reaction in the catabolic pathway has a large negative value B The ΔG of the reverse reaction in the catabolic pathway has a large positive value C The ΔG of the reaction in the anabolic pathway is close to zero D The ΔG of the reaction in the anabolic pathway is positive E None of the above

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