5- Draw structure of products in the following metabolic reactions and name the enzyr involved and the products. 7.1 O NH2 он 7.2 CI ZI
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- Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.Enzyme X exhibits maximum activity at pH- 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. O the enzyme uses NADH has a cofactor the enzyme uses coenzyme A has a cofactor O a Tyr residue on the enzyme is involved in the reaction. O a His residue on the enzyme is involved in the reaction1 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.
- 1. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.4.Pepsin is the proteolytic enzyme of gastric juice. The active form of this enzyme is formed from pepsinogen under HCL action.Optimum of enzyme action: pH = 1.5, t = 37°. Describe the properties of this enzyme. For this:1)Name and explain the mechanism of this enzyme activation.2)Draw the plot and explain the effects of pH and t on the reaction velocity.3) Explain how changes the velocity of this reaction in patients suffering from hypoacidie gastritis.1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
- . 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: 5.1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)HO-C-CH,-CH,~ Identify the enzyme needed in each of the following reactions as an isomerase, a decarboxylase, a dehydrogenase, a protease, or a phosphatase. о CH;-C-Č-OH → CH;-Č–H + CO, СНО CH,OH НС—ОН C=0 HO-CH — НО -СН НС—ОН НС—ОН HO-CH Но -СH CH-OPO,?- ČH-OPO,- Но -С—СН,—CH, —С—ОН — Но -С—СН—СH-С-ОН + 2Н H;N-CH-C-NH-CH-CO0 +H;O → CH; ČH3 2 H;N-CH-CO0- ČH3
- 31. The velocity of a particular enzyme-catalyzed reaction varied with pH as shown in the adjacent table: The MOST LIKELY explanation for this effect on enzyme activity is that the R-groups of: 1) His must be deprotonated 2) His must be protonated 3) Asp must be deprotonated pH Velocity (arbitrary units) 3 0.01 4) Asp must be protonated 5) Cys must be deprotonated 6) Cys must be protonated 4 3 5 10 ANSWERS A) 1,6 6 5 B) 2, 3 7 0.02 C) 3, 5 D) 4, 2 8 0.01 E) 5, 17. Complete the following reactions: ( 关关 H H H OH H H NIC 8. Compare hydrolase and lyase enzymes. ( OH I + HOWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1