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Briefly, describe enzyme multiplicity and broad substrate selectivity for cytochrome P450.
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- . 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 NAGYou perform Michaelis-Menten kenetics on i) trypsin and ii) a mutant form of the same enzyme (a single amino acid has been changed). The specificity constant for the mutant was 10 times larger than for trypsin. a) Define the specificity constant and explain using this definition how a larger value might occur. b) Explain how, if at all, a non-competitive inhibitor of trypsin would affect the specificity constant.Decoupling 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.
- Since all of the ββ-lactams that you have tested are susceptible to hydrolysis by PaESBL-1, the hospital will not be able to use a single ββ-lactam to combat this P. aeruginosa isolate. You need to consider alternative strategies. From the following list, select all of the strategies that might successfully overcome the broad substrate specificity of PaESBL-1:Recall that vmax is achieved only at high substrate concentrations. Do you predict that vmax will change when an uncompetitive inhibitor is introduced? Why or why not?Identify the effect of lowering the KM of phosphoglucoseisomerase on Phosphofructokinase activity. Group of answer choices Increased Activity Decreased Activity Activity Levels are not Changed
- D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?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)Give a possible set of bacterial factors (or lack thereof) and what properties they have that would explain an increase in the 50% inhibitory concentration for tetracycline by 1,000-fold in an organism.
- Describe type I, II, and III L-asparaginases. Mention characteristics and differences between them with respect to enzyme kinetics (rate, km, etc).Where do each of these 5 main themes occur in the chymotrypsin mechanism? 1) substrate specificity 2) induced fit 3) covalent catalysis 4) acid/base catalysis 5) transition state stabilization1A. In 2-3 sentences, explain what system the authors are studying in this work. Describe what this system does. Enzymatic substrate selectivity is critical for the precise control ofmetabolic pathways. In cases where chemically related substratesare present inside cells, robust mechanisms of substrate selectivityare required. Here, we report the mechanism utilized for catalyticATP versus GTP selectivity during adenylate kinase (Adk) -medi-ated phosphorylation of AMP. Using NMR spectroscopy we foundthat while Adk adopts a catalytically competent and closedstructural state in complex with ATP, the enzyme is arrested in acatalytically inhibited and open state in complex with GTP. X-raycrystallography experiments revealed that the interaction inter-faces supporting ATP and GTP recognition, in part, are mediatedby coinciding residues. The mechanism provides an atomic view onhow the cellular GTP pool is protected from Adk turnover, which isimportant because GTP has many specialized…
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