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.
Kk149.
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.
RuBP carboxylaseis by no means an idesl enzyme. Describe some of the problems with its active site and its substrate specificity. If we compare the amino acid sequences of this enzyme from many different species, they are almost identical. What is the significance of this uniformity?
(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…
. The first two steps of ovothiol C biosynthesis are shown below. Propose the rest of the pathway, indicating the potential involve- ment of cofactors. co- coo H NH,* Histidine Fo*, 02 reductant .coo- *H,N° coo- *H,N° COO HS* NH,* 5-Histidylcysteine sulfoxide conjugate 5-Histidylcysteine thioether conjugate Cysteine
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?
Explain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding sitefor the substrate is able to exhibit sigmoidal kinetics.
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.
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