Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excessuses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A studentsearcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XOhich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct theneweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on TableTable 1. Enzyme Kinetic DataVelocity, mM/sKmp0.0351[S], mMChaХan0.4920.06780.06150.2110.05310.02610.04510.0870.02980.01570.02110.0480.01950.00910.01420.0290.01270.00670.0081Enzyme Kinetic Parameter:ParametersVmax|Ku| Type of InhibitionMode of BindingXanthineKaempferolChlorogenic acidNANALine Weaver Burk Plot:

Kaemferol inhibitory effect on Xanthine oxidase: Enzymatic assays have shown that kaempferol…

Answered: Xanthine oxidase (XO) is the enzyme…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. You have determined the Vmax to be 0.1 mol/sec and the Km to be 2.5 mM. What would the rate of the reaction be when the substrate concentration is 20 mM? 0.09 MS-1 O 0.133 Ms-1 O 0.18 Ms ¹ 9 Ms-1 O 0.018 Ms-1 0.2 MS-1
How is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?
Make tables of reactions of the Glycolysis and Gluconeogenesis with enzyme names and DGo’ values. I provided a template for the table below. With this information, determine the overall free energy of each pathway. Discuss the differences in these values and suggest a reason for this difference. Please answer very soon will give rating surely
Derive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.
Create a ONE page, formal summary, including APA Formatted in-text citations, of the enzyme amalyze and how it is used in the meat processing industry (Address all guiding questions below in your summary). Note, references can be the second page of the assignment. Include the questions in ur answer Which enzyme is used in the industry (if more than one enzyme is included, you can choose one of the enzymes) Describe the molecular structure of the enzyme (how many amino acids; discuss different levels of protein structure-secondary, tertiary, quaternary, key structural components/amino acids in active site) Describe how the enzyme works in the industry and why it is a key component for this industry. What specific reaction(s) are being catalyzed? What types of bonds are being broken?
How does the body utilise carbs and sugars?
Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?(notice that its 450 kj not 450j)
enzyme-inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displays kinetics somehow similar to non-competitive inhibition, does this is inhibitor good to use to inhibit toxanthine oxidase in the case of hyperuricemia and gout?
Most of the enzyme reactions followed the mathematical kinetic plots suggested by the Michaelis-Menten plots:viii. Draw another Lineweaver-Burk plot and on the same plot, draw a graphto indicate un-competitive inhibition.Note: In the graphs, lable Vmax and KM clearly.
The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.

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