A. Enzyme KineticsTwo compounds were being investigated by Al Cohol, a student researcher in Biochemistry, for theirinhibitory effect on xanthine oxidase (XO). The inhibition of this enzyme is critical in the treating gouty arthritis.He uses xanthine (Xan) as substrate. He investigated two inhibitors namely kaempferol (Kmp) andchlorogenic acid (Cha). The data that he was able to acquire is given in Table 1 below.Table 1. Enzyme Kinetic DataVelocity, mM/s[S], mMХanKmpCha0.4920.06780.03510.06150.2110.05310.02610.04510.0870.02980.01570.02110.0480.01950.00910.01420.0290.01270.00670.0081A. Construct the Lineweaver-Burke plot for each reaction system in one graph using MS Excel. Copyand paste your graph with complete regression analysis.

Enzyme kinetics: Part A. [S]is the concentration of…

Answered: - Enzyme Kinetics

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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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..
Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess uses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student searcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO hich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the neweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table Table 1. Enzyme Kinetic Data Velocity, mM/s Kmp 0.0351 [S], mM Cha Хan 0.492 0.0678 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Enzyme Kinetic Parameter: Parameters Vmax |Ku | Type of Inhibition Mode of Binding Xanthine Kaempferol Chlorogenic acid NA NA Line Weaver Burk Plot:
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
The following statements refer to enzyme inhibition. Match the statement to the one of the following descriptors to which it is best associated. Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent inhibition. 9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by dialysis or drug metabolism/excretion. 9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site 9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex forming an inactive E.S.I. 9d. The inhibitor binds reversibly and independently of substrate to an allosteric site producing E.I or a ternary E.S.I complex which can't form product. 9f. The relative amount of inhibition decreases as [S] (the concentration of substrate) increases and S better competes for occupancy of the active site.
1. 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. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
Explain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. All coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement. b. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? c. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer d. Why is penicillin toxic to bacteria but not to higher organisms? e. What is the metabolic basis for the observation that many adults cannot ingest large quantities of milk without developing gastric difficulties?
Match the different names for inhibition mechanisms (1-5) with a description of their properties 7a-7d: 1. competitive inhibitor. 2. allosteric inhibitor also known as non-competitive inhibitor. 3. un-competitive inhibitor. 4. affinity label also known as active site directed covalent (irreversible) enzyme inhibitor. 5. Kcat inhibitor, also known as a mechanism-based covalent (irreversible) enzyme inhibitor. 4a. An enzyme inhibitor in which a substrate or competitive inhibitor is modified so that it contains a chemically reactive electrophile which can bind to and subsequently react with the enzyme active site: 4b. An enzyme inhibitor that contains latent reactive group that upon binding followed by catalytic turnover at the enzyme active site produces a reactive electrophile that reacts covalently with the enzyme: 4c. A reversible inhibitor that competes with the substrate for binding to the enzyme active site: 4d. A reversible inhibitor that can bind independently of substrate to its…
Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information provided
Several factors contribute to enzyme catalysis. What arethey? Briefly explain the effect of each.

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