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- Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".
- 7) Many early attempts at enzyme engineering tried to design so-called catalytic antibodies. This strategy was used to create an antibody whose antigen was a transition state analogue of the reaction to be catalyzed. Why was this a sound strategy for engineering a biocatalyst?3. MUTPase from ASFV (aDUT) and from swine (listed as sDUT) were studied in the absence and present of the DUTP substrate. Using the melting temperature data provided below, how does adding the substrate affect enzyme stability? Explain your choice in 25 words or less. TemperatureL°CT protein Tm by thermal denaturation (°C) aDUT 83.1 ± 0.2 SDUT 61.8 + 0.2 aDUT-DUTP-Mg SDUT-dUTP-Mg 84.5 + 0.1 62.7 + 0.2 a. The substrate makes aDUT less stable and SDUT more stable b. The substrate makes aDUT more stable and $DUT less stable c. The substrate makes both ADUT and SDUT less stable d. The substrate makes both aDUT and SDUT more stable sh (United States) D. Focus rch 7:15 80°F ENG 7/10/2 DELL F3 F4A purified protease enzyme from the fungus Aspergillus sp. Is tested in a laboratory. This enzyme was lyophilized as a white powder. When reconstituting with phosphate buffer pH 7.2 the active enzyme is obtained. To check its purity, an electrophoresis is performed where a single band of approximately 70,000 molecular weight is observed. The solution with enzymatic activity was stored at 4ºC for later use. A few days later it was found that the enzymatic activity had been lost and in the electrophoretic analysis, instead of a single band there were three bands of weights 40,000, 20,000 and 10,000. Come up with a reasoned explanation of what might have happened to the enzyme
- 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 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
- 24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.1426. Sweetzyme® IT Extra is a trademarked immobilized enzyme formulation of glucose isomerase sold by the Danish company Novozymes. The following reaction is carried out in a 4.0 L reactor in the presence of an non-competitive inhibitor, I: E + G EG = 2 => E + F EG+1 EIG G=glucose, F = fructose The Sweetzyme beads added to the reactor have a total surface area, a = 342 cm². Kinetic Parameters k₁ = 0.00820 M₁¹ S¹ k.₁ = 0.00190 s¹ k₂ = 0.570 s¹ Initial/Total Enzyme concentration: Initial Bulk Substrate Concentration: Mass transfer coefficient, Eo 2.30 x 105 M Sb = 0.152 M k₁ = 9.15 x 10 cm/s A. What is the maximum reaction velocity with no inhibitor (in mol/L-s)? (recall that Rapid Equilibrium and Quasi steady state approaches predict the same value for Vmax for this mechanism) B. What is the maximum reaction velocity (in mol/L-s) with the non-competitive inhibitor, I, at a concentration of [1] = 0.0029 M, with K₁ = 1.8 x 10³ M. C. Calculate the Dahmköhler number to determine if the…