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- QUESTION 10 Select a property that does not belong to allosteric enzymes. They conform to hyperbolic Michaelis-Menten kinetics They may have binding sites for regulatory molecules that are separate from active sites They tend to have a signmoidal curve of rate versus [S] They undergo conformation changes as a result of modulator binding.QUESTION 38 In a 250µl reaction containing 0.3 nmol of a Michaelis enzyme with Km = 4.4 x 10 M and saturating substrate concentration, product was formed at an initial velocity of 6.3 x 10 M min-1. What is kcat for this enzyme? Give your answer in 3 sigfigs in scientific notation, for example 1.20 e -3 Click Save and Submit to save and submit. Click Save All Answers to save all answers. O Type here to search 78°F Mostly cloudy End 4) DII PrtScn F8 Home F9 F6 F2 F3 F4 *- & 7 8. 4. #3QUESTION 26 During gluconeogenesis, whereby liver cells convert pyruvate to glucose, Fructose-6-phosphate (F6P) is converted to Glucose-6-phosphate (G6P). If the standard equilibrium concentrations are: [F6P] = 0.52 M and [G6P] = 1.48 M, then Keq’ is ______ and the reaction is ________. Fructose-6-P ó Glucose-6-P > 1; exergonic > 1; endergonic < 1; exergonic < 1; endergonic
- QUESTION 18 Stable molecules that resemble the transition state of enzyme catalyzed reactions are very potent inhibitors. Provide an explanation as to why these compounds are better than inhibitors based on the substrate. TT TT Paragraph v v 3 (12pt) = - E · T Arial T T, O Mashups 66 HTHL CSS CS Scanned with CamScannerQuestion 12 The disulfide bridges: A Are generated by an intra- or inter- molecular oxidation reaction B Can be selectively reduced by SDS (Sodium Dodecyl Sulfate) C Are bonds that possess an intermediate in- teraction energy comprised between that hydrogen bonds and that of ionic bonds D Participate in the stabilization of sec- ondary structures E Are established between the side chains of amino acids methionineQuestion 106 Methicillin cannot be destroyed by because O bacterial vanases; becasue it has a postive charge, the bacterial enzyme cannot attach to it O bacterial gyrase; as it is the wrong shape to be destroyed by gyrase heat; it has many disulfide bridges O bacterial beta-lactamases; it cannot fit into the active site of bacterial beta-lactamases
- Question 1. Enzymes, proteins and deoxyribonucleic acid (DNA) are important biological macromolecules. Enzymes are not only speed up the reaction, but also are necessary for DNA reproduction. e) Michaelis - Menten Kinetics model explains how reaction rates are depending on the concentration of enzyme and substrate. i. What is meant by the saturation of enzyme? ii. A decrement in enzyme activity is known as enzyme inhibition. Based on normal enzyme activity, explain the enzyme kinetics for competitive inhibition and noncompetitive inhibition, as shown in Figure 1. Normal enzyme Competitive inhibitor Noncompetitive inhibitor Substrate concentration Figure 1: Enzyme inhibition f) What is the importance of cofactor in the enzyme activity? Give an example of a disease that is related with cofactors. Rate of reactionQUESTION 10 UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
- QUESTION 42 In the pathway M1 + M2 → M3+ M4, enzyme E facilitates the reaction. If compound M4 is further metabolized through a series of steps to form compound M10, and compound M10 inhibits enzyme E, one could conclude that O a. enzyme E is subject to feedback inhibition. O b. enzyme E is subject to feedback stimulation. O c. compound M4 is an allosteric activator of the first reaction. O d. compound M10 is a competitive inhibitor of the first reaction. O e. compound M4 is a coenzyme in the first reaction. Click Save and Submit to save and submit. Click Save All Answers to save all answers. 2 =9³ F2 #3 20 F3 $ 4 F4 % 5 FS. MacBook Pro WERT & 7 Y E * ∞QUESTION 4 Lipids are hydrophobic molecules and have no charge. If they are loaded into a gel, and an electric field is applied, which way will they move, if at all? O Some will migrate to the + electrode and some will migrate to the - electrode. O They will migrate toward the - electrode They will not move They will migrate toward the + electrodeQUESTION 18 In the serine protease trypsin, the specificity for one substrate over another describes what type of catalysis? OA. proximity B. acid-base C. covalent OD. metal ion