Balance the chemical equation for the oxidation of arachidonic acid to ATP, CO2, and water. (Use the lowest possible ratio of reactants and products.) ADP + Pi + 02- АТР + CO2 + H20 CH3 (CH2)4 (CH=CHCH2)4(CH2)2COOH +
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- Directions: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 × 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.U Select all of the following half reactions that require energy (work) to proceed as written. NAD+ + 2HNADH + H+ glucose + inorganic phosphate glucose-6-phosphate + H₂O › DETAILS O=d-0 OH NADH+H NAD+ + 2H OH o-p-o-C-CH3 + H2O -0-8-CH3 PREVIOUS ANSWERS ATP+ H₂O ADP + P₁ H قمر H (not balanced) (not balanced) O 0-4-OH + HO-CH₂ 0 xa) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
- calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM1 of 1 3. A sample of glucose reacts in anaerobic respiration. The right- hand box below shows a particle diagram of the moles of substances present after the reaction is complete. fe On a piece of paper draw the "Before" box as shown and draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Key = C2H5OH = CO2 = CgH1206 Sub Before After You will need to draw a diagram to answer this question. On a piece of paper, draw the "Before" box as shown, and then draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Upload an image of your drawing by clicking "Upload files" or by dragging and dropping your file into the box. Or, use your device's camera to take a photo of your work by clicking the camera icon.An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
- a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveAG" = -69.5 kJ · mol- The percent efficiency of oxidative phosphorylation is 35%. Calculate the number of ATP generated by Complex I. Use 1 significant figure. The amount of ATP generated by Complex I is mol ATP. The equation for the overall reaction that occurs in Complex I is shown as: NADH + H+ + Q = NAD+ + QH2 Please explain! Thank you so much..Vmax [S] Vo = Km+ [S] Eadie-Hofstee plot Lineweaver-Burk (L-B) plot v=Vm-Km [S] Km 1 Vm Vm [S] The equations above apply for Michaelis-Menten enzyme kinetics but are presented in three different formats. For competitive inhibition The Michaelis-Menten equation becomes Vo=Vmax[S]/(aKm+[S]) Put the Michaelis-Menten equation for competitive inhibition in the Eadie-Hofstee format. The Y-intercept of this plot will be
- Page of 6 ZOOM + name: 3. In the last reaction of the citric acid cycle, malate is dehydrogenated to regenerate the oxaloacetate necessary for the entry of acetyl-CoA into the cycle: L-Malate + NAD+ → oxaloacetate + NADH + H* AG'° = 30.0 kJ/mol (a) Calculate the equilibrium constant for this reaction at 25 °C. (b) Because AG°' assumes a standard pH of 7, the equilibrium constant calculated in (a) corresponds to [oxaloacetate][NADH] Keq [L-malate][NAD*] The measured concentration of L-malate in rat liver mitochondria is about 0.20 mM when [NAD*]/[NADH] is 10. Calculate the concentration of oxaloacetate at pH 7 in these mitochondria. (c) To appreciate the magnitude of the mitochondrial oxaloacetate concentration, calculate the number of oxaloacetate molecules in a single rat liver mitochondrion. Assume the mitochondrion is a sphere of diameter 2.0 microns.Balance the following net reaction that occurs during oxidative phosphorylation. Use the smallest whole integers possible for the reaction stoichiometry. NADH+ FADH₂ + ADP+ 0₂+H+PO, ¹ NAD+FAD+ ATP+ +H₂Och Select all statements that are correct. Note there might be more than 1 correct statement. From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis- Menten plot The Lineweaver-Burk plot assumes that products and reactants are present at equal concentrations during the entire time of the reaction The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration O 20°C D) // E