a. What is the optimum pH of wild type ß-galactosidase? b. What is the optimum temperature of mutant ß-galactosidase? c. Which enzyme has the greater activity at pH 7.2? d. Which enzyme has the greater activity at a temperature of 42.5°C? e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C?
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- A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)*The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of 3-D-glucose to D-glucono-6- lactose. This enzyme is highly specific for the ß anomer of In spite of this glucose and does not affect the a anomer. specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose that is, for solutions consisting of a mixture of 3- and a-D- glucose. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quan- tities of glucose, what advantage does glucose oxidase offer over non-enzymatic oxidizing agents like Tollens reagent? *Is B-D-glucosamine a reducing sugar?elearn.squ.edu.om/mod/qui ystem (Academic) The enzyme asparaginase is used to reduce the level of asparagine in blood in the treatment of leukemia. Which of the following forms of Asparaginase would be most useful if the blood asparagine level is 0.2 mM? Select one: O a. Km = 2.0 mM; Vmax = 0.1 mM/hour O b. Km = 0.1 mM; Vmax = 0.5 mM/hour %3D О с. Кm 0.2 mM; Vmax = 0.1 mM/hour O d. Km = 0.1 mM; Vmax = 0.1 mM/hour O e. Km = 0.2 mM; Vmax = 0.5 mM/hour Clear my choice In a steady state (of ES formation and ES breakdown) Select one: a The rate of formation of ES is equal to the rate of its degradation during the reaction
- . The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGDecoupling agents such as 2,4-DNP can result in altered metabolic activity. Explain what 2,4-DNP is, describe how it alters metabolic activity, and why this could be dangerous.. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.
- IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--X Incorrect. e. To which classification of amino acids (nonpolar, polar-acidic, polar-basic, polar-neutral) does fluoroalanine belong? nonpolar polar-basic O polar-neutral polar-acidicuizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBC
- . Using the principles described in the text regarding pyridoxal phos- phate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.me (1).docx BIU A A- are they different? 3. What are three ways that 2-deoxystreptamine (2-DOS) aminoglycosides can inhibit protein synthesis? 4. Chloramphenicol: a. Where does this drug bind? b. How does it inhibit protein synthesis?. In Figure 6-11,a. in view of the position of HPA oxidase earlier in thepathway compared to that of HA oxidase, would youexpect people with tyrosinosis to show symptoms ofalkaptonuria?b. if a double mutant could be found, would you expecttyrosinosis to be epistatic to alkaptonuria?