Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.
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A7.
Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.
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- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.1B. please help me in detail. Draw a graph of free energy G (y-axis) vs reaction progress (x-axis) that illustrates what the kinase is doing in terms of the free energy by showing (i) the substrate (also label what the substrate is [it’s name]), (ii) the products (also give the name of the products), (iii) draw and label the uncatalyzed and catalyzed reactions, and be sure that the parts of the graph are properly labeled..4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
- Compare and contrast Bound Fraction equation in ligand binding and Michaelis-Menten equation in enzyme kinetics, including their double-reciprocal forms. Discuss what Km is important for and what Vmax (or kcat) is important for? Under what (substrate) conditions is Km more important than Vmax, and under what (substrate) conditions is Vmax more important than Km? Based on the discussions in question 2, explain what type of inhibitors works best under (a) high substrate concentration and (b) low substrate concentration.Chemical scheme for enzyme catalysis (a) Write the chemical equations for enzyme,substrate, enzyme•substrate complex, and product as for a typical Michaelis-Mentenenzyme (b) At what condition is half of the enzyme expected to be saturated withsubstrate? (c) Plot the rate of product formation as a function of substrate concentration.(d) Indicate the KM parameter on your rate vs substrate plot.Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: (a) Is high or low KM preferable for an enzyme reaction? Give reason. (b) Draw the Lineweaver-Burk plot and on the same plot, draw a graph to indicate competitive inhibition. (c) Draw another Lineweaver-Burk plot and on the same plot, draw a graph to indicate non-competitive inhibition.
- Item 35 Organic cofactors are referred to as _________. Fill in the blank Item36 Item Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e. substrate, and its effectiveness depends on product concentration. Item37 Item 37 A substance that binds to the active site of an enzyme and turns it off is called a _________ inhibitor. Fill in the blank Item 38 Lactase is an enzyme that digests lactose. True or False Item 39 Exergonic reactions do not require activation energy. True or FalseSelect all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme
- For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absence of the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.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.Describe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..