f) As ATP is used, the above, at what ratio of equilibrium)? phosphocreatine stores are depleted. Using the ATP and ADP concentrations given [creatine]/[phosphocreatine] would you expect the reaction to stop (or reach G) do some research. How does the level of phosphocreatine remain high in muscle cells. Where/how is it remade from creatine? (one paragraph)
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- Question: Fumerase is an enzyme in the citric acid cycle that catalyzes the conversion of fumerate to L-malate. Given the fumerate (substrate) concentrations and initial velocities below, construct a Lineweaver-Burk plot and determine Vmax and Km values for the fumerase catalyzed reaction. Fumerate (mM) Rate (mmol l-1 min-1) 2.0 2.5 3.3 3.1 5.0 3.6 10.0 4.2 Fumerase has a molecular weight of 194,000 and is composed of four identical subunits, each with an active site. If the enzyme concentration is 1 x 10-8 M for the experiment in part (a), calculate kcat value for the reaction of fumerase with fumerate. Note: units for kcat are reciprocal seconds (s-1).Question: Theoretically, explain the factors influencing the rate of an enzyme-catalyzed reaction at the molecular level and how these factors can be manipulated to optimize the reaction rate.Matching Question: Researchers characterized a new enzyme and determined its Km=200 uM. Moreover, they found that at (Etotad10 nM this enzyme reaches maximum reaction velocity Venasa5 is 1. What is the keat of this enzyme? 2. At which concentration of the substrate this enzyme reaches initial reaction velocity (Vo) of 500 nM/s (assuming (Etotal is the same 10 nMy? 3. What is the maximum reaction velocity (Vmax) of the reaction catalyzed by this enzyme at (Etotail4 nM? Make sure to choose the correct units of measure. Note that some of the items from the answer list should NOT be used. v kcat 1. 400 uM - (S] - - Vmax 2 100 uM 500 s 450 uM 250 s1 * 501 7. so00 s 1 UM's SuMis 10 200 uM 11. 10 uMis 12 25 s 13. 500 nM/s
- Question: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM) V0 (mM/min) 0.25 0.183 0.50 0.356 1.00 0.665 2.50 1.45 5.00 2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-B Uninhibited With 1 mmol l- A 0.684 50 20 1.08 0.653 0.468 10 1.43 1.01 0.649 0.476 0.374 0.311 5 1.02 0.363 0.798 0.657 3.3 0.296 2.5 0.250 2.0 0.549 Comment on these results. 8.2 The system investigated in problem 7.1 was investigated again under identical conditions but in the presence of an inhibitor, giving the following data: 40.0 6.67 10.0 156 20.0 Substrate conc" (mmol 1-1) Initial velocity (umol 1- min-1) 5.0 100 122 222 278 Determine the type of inhibition. If K, for this system is 2.9 mmol 1-', calculate the inhibitor concenträtion present.PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-IB Uninhibited With 1 mmol I-1À 50 20 0.684 1.08 0.653 1.01 0.649 0.476 0.374 0.311 10 1.43 0.468 1.02 0.363 0.296 3.3 0.798 2.5 2.0 0.657 0.549 0.250 Comment on these results.
- ent Page Form Combine Files Protect Flatten File Ch. 7] PROBLEMS Share 390% Enzymes-2.pdf Help + < Problems 125 (142/434) Capture the ronction: Add Bookmark 7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol 1¹¹): 5.0 Initial velocity (umol l´¹ min¯¹): 147 Calculate Km and Vmax 6.67 10.0 20.0 182 233 323 125 40.0 400Enzyme Kinetics question Enzyme used is 10uL of a 10 ng/uL solution to a reaction mix in a final volume of 2.0 mL. (Enzyme used is 20kDa monomeric enzyme if matters) Based off lineweaver burk where 300 uM of inhibitor is used noninhibited formula is y= 4x + 0.1 (x axis is 1/S 1/mM) (y axis is 1/Vo sec/mM) inhibited formula is y = 4x + 1 I found Km as 1 mM for inhibited Vmax as 1mM/sec for inhibited How would I find Kcat? How would I find Ki?Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
- Problems 14 and 15: some of the exponents are unclear. Here they are: 14. Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions:(a) [S]=2x10-3 Mand[I]=2x10-3 M(b) [S]=4x10-4 Mand[I]=2x10-3 M (c) [S]=7.5x10-3 Mand[I]=10-5 MAssume that Km = 2 x 10-3 M, Ki = 1.5 x 10-4 M and Vmax = 270 nmoles x liter-1 x min-1.The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor. 15. (a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of 1.5 x 10-3 M if Km =2.9x10-4 M and Ki =2x10-5 M? (b)Towhatconcentration must the substrate be increased to reestablish the velocity at theoriginal uninhibited value?Question: What is the isoelectric point of Cysteine and Glutamate, Illustrate structures and net charges (Determine the isoelectric point based on the pka) please give clear handwritten answer!Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?