Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine the type of inhibition shown by acetazolamide. Explain your answer. (i) (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide in Qla)(i). List down the kinetic properties of these inhibitions. Sketch a graph of I/V versus 1/[S] showing plots in the absence of an inhibitor and in the presence of the types of inhibitors mentioned in Qla)(ii). (ii)
Q: What is the relationship between a transitionstate analog and the induced-fit model of enzyme…
A: Induced-fit model : A model of enzyme catalysis in which the enzyme conformation changes in response…
Q: Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by…
A: Chymotrypsin is a protease enzyme that cleaves the proteins at the C-terminal end of phenylalanine,…
Q: HOW TO SOLVE THIS IN EXCEL? For the following aspartate reaction in the presence of inhibitor, Km =…
A: Enzymes are biocatalyst that increases the speed of reaction by lowering the activation…
Q: If isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is…
A: ATcase (Aspartate transcarbamoylase) is an allosteric enzyme. It is involved in regulation of…
Q: Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin…
A: Free energy change for a reaction, ΔG, can be solved using the standard change in Gibbs free energy,…
Q: Explain the biochemical basis of how temperature and pH affect enzyme activity. What are the changes…
A: Enzymes are the biomolecules which catalyze the biochemical reactions and increases the rate of the…
Q: B) Uncompetitive inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme…
A: An enzyme inhibitor is a molecule that will bind to an enzyme to decrease or slow down its activity.…
Q: Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal…
A: Lineweaver-Burk plot is the graphical representation of Lineweaver-Burk equation which is a double…
Q: A. What are the Vmax and Km Values for the enzyme-catalyzed reaction without inhibitor? Please give…
A: Note:- Dear student you have not mentioned with which question you need help with. So, according to…
Q: Án enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a kat value of 181s1.…
A: An enzyme is a type of biological catalyst that aids in the acceleration of chemical reactions.…
Q: Write the chemical reaction catalyzed by chymotrypsin. How is its specificity determined? How is the…
A: Chymotrypsin is a type of protease enzyme. It acts as a digestive enzyme, primarily synthesized…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…
Q: Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to…
A: Regulatory enzymes exhibit increased or decreased catalytic activity in response to specific…
Q: UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order…
A: Phase II Biotransformation reactions enable detoxification of drugs and aid in their proper removal…
Q: Lineweaver-Burk plots of enzyme kinetics for the reaction, S P, has the following features: 1/v is…
A:
Q: Compute for the AST (Aspartate Aminotransferase activity) of 0.10 mL serum sample mixed with 1mL of…
A: Step 1 AST activity: AST or Aspartate Aminotransferase activity is the measurement of AST in blood.…
Q: Calculate the turnover number for an enzyme, assuming Vmax is 0.5 M.sec-1 and the concentration of…
A: The turnover number or kcat of an enzyme can be defined as the number of molecules of substrate that…
Q: Enzyme X can be inhibited by two distinct inhibitors, only one of which is acting as a competitive…
A: Enzymes are the proteins or RNA which catalyses the rate of reaction without undergoing any change…
Q: Construct a Lineweaver-Burk plot to answer the following questions: (a) What are the apparent KM and…
A: The Lineweavwe-Burk plot is the plot between 1/[V] vs 1/[S]. Km = -1/ x-intercept Vmax= 1/y…
Q: Identify the two forms of mixed inhibition and briefly describe how the two forms differ?
A: The substance that inhibit the activity of enzymes are called enzyme inhibitors and the mechanism by…
Q: An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate)…
A: We need to draw the Lineweaver Burk (LB) plot to find out the answers. LB plot has 1/[S] as X-axis…
Q: 1966, Ferdinand showed that a random-order ternary-complex mechanism for a two-substrate…
A: Given; No. of substrates: 2 (in random-order ternary-complex mechanism which means any substrate can…
Q: Hexokinase in red blood cells has a Km of approximately 50 µM. What concentration of blood glucose…
A:
Q: Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are…
A:
Q: With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate…
A: Fluroacetate is a highly toxic susbstance. FA is present in plant species and there ingestion can…
Q: In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of…
A: In enzymology, allosteric regulation is the inhibition or activation of an enzyme by a small…
Q: Consider applying biocatalytic reduction with carrots to the following two ketones: tert-butyl…
A: Introduction :- Bio-catalysis is the process of using natural substances like- enzymes for…
Q: Calculate the standard free-energy change of the reaction catalysed by the enzyme phosphoglucomutase…
A: Reaction in the given question is proceed as Glucose-1-phosphate →→ Glucose-6-phosphate…
Q: What are the measures to inhibit the Maillard reaction in undesirable situations. please explain…
A: Maillard reaction is a type of chemical reaction in the field of Biochemistry. It occurs between a…
Q: Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme…
A: Transition state structural analogs of enzymes are chemicals with a structure that resembles the ES…
Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…
A: The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…
Q: The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried…
A: Enzymes are proteins. They are biological catalysts. Tertiary and quaternary structures are crucial…
Q: 6.3.7 Activity 6.1 2 List and briefly explain four methods of studying an E-S complex. ngenic…
A: Answer :- 1) There are various methods of studying the Enzyme-substrate complex like magnetic…
Q: Calculate the specific activity and kcat for this enzyme
A: Enzymes are catalyst that speed up the biochemical reaction by lowering the activation energy of the…
Q: The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate fructose -6-phosphate +…
A: The Gibbs free energy of a system represents the degree of randomness of the system. It is described…
Q: How to calculate the percent inhibition of xanthine oxidase enzyme inhibition with a blank…
A: To determine per cent inhibition, we first need to determine the initial velocity of the enzyme in…
Q: One treatment for hyperuricemia is administration of xanthine oxidase inhibitors like allopurinol.…
A: Allopurinol is used in the treatment of hyperuricemia and gout. The urate is the final product of…
Q: 5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105…
A: Michaelis-Menten model of enzyme kinetics is a very useful model which describe the relationship…
Q: The trypsin enzyme is able to hydrolyze a peptide substate at the carboxyl side of an Arg or Lys…
A: Enzymes are protein molecules that increase the rate of enzyme reactions by decreasing the…
Q: Write a balanced equation for cach of the following reactions or reaction sequences. (a) The…
A: Note: Since you have posted a question with multiple subparts, we will solve the first three…
Q: Explain the basis for the following statement. For efficient conver- sion of galactose to…
A: UDP : Uridine diphosphate glucose is a nucleotide sugar. It is involved in glycosyltransferase…
Q: Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM…
A: Enzymes are specialized proteins that catalyze all biochemical reactions taking place in a living…
Q: Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells..…
A: Km is the value that defines the concentration of substrate at which velocity is half of the Vmax.…
Q: Calculate the standard free energy for creatine-phosphate hydrolysis in a cell where [creatine-P]=3…
A: Creatine phosphate (CP) is the phosphorylated creatine molecule which serves as a rapidly…
Q: Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high…
A: Genetic defects in the oxidative phosphorylation are known to reduce the synthesis of ATP, which…
Q: a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of…
A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate concentration.…
Q: 1.2) If the Km of an enzyme for it's substrate remains constant as the concentration of the…
A: If Km remains unchanged even after increasing the inhibitor concentration it shows that…
Trending now
This is a popular solution!
Step by step
Solved in 2 steps with 2 images
- Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used. Eo T I S V (g/I) (°C) (mmol/ml) (mmol/ml) (mmol/ml-min) 1.6 30 0.1 2.63 1.6 30 0.033 1.92 1.6 30 0.02 1.47 1.6 30 0.01 0.96 1.6 30 0.005 0.56 1.6 49.6 0.1 5.13 1.6 49.6 0.033 3.70 1.6 49.6 0.01 1.89 1.6 49.6 0.0067 1.43 1.6 49.6 0.005 1.11 0.92 30 0.1 1.64 0.92 30 0.02 0.90 0.92 30 0.01 0.58 0.92 30 0.6 0.1 1.33 0.92 30 0.6 0.033 0.80 0.92 30 0.6 0.02 0.57Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) AAcetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
- Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graphDetermine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256Calculate the concentration of p-aminophenol control to match the 0.075 % w/w limit in 200 mg/10 ml Your Answer: 0.0015% show work
- From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. You have to plot the graph by using excel. Please include slope Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
- The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142The table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversions