Describe the reaction catalyzed by salivary amylase. To which class of enzymes does amylase belong
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1. Describe the reaction catalyzed by salivary amylase. To which class of enzymes does amylase belong? Explain thoroughly.
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- 1. What are the effects of pH and temperature to catalase? What is the optimum pH and optimum temperature for catalase? 2. Explain why the rate of reaction initially increases with increase in temperature then gradually declines as the temperature is further increased. 3. Is the rate of enzymatic reaction always directly dependent on enzyme concentration? Explain. 4. Explain the effect of substrate concentration on enzyme activity. 5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?6. In an experiment, students used liver tissuc samples to study the cthanol metabolism and the possibility of ethanol conversion into glucose. The ethanol introduction in the investigated medium didn't lead to glucose level increase. Why is it impossible to convert ethanol to glucose? For the answer: a) provide a scheme of gluconcogenesis, indicate the substrates of this process; b) write the reaction of ethanol oxidation in the liver; c) explain whether it is possible to use the metabolites of ethanol catabolism for the glucose synthesis.8. In patients with diabetes mellitus type 1, the biochemical disorders result from changes in fuel metabolism. One of these signs is acidosis, Explain why such patients have a deviation of blood pH from the norm? For this 9. b) write the reactions of synthesis and oxidation of these molecules, name the enzymes, coenzymes, reaction localization: X
- 1.Enumerate the enzymes of the alpha ketoglutarate dehydrogenase complex and write its mechanism of action1. Explain the reaction mechanism involved how glucogenic amino acids can yield either a pyruvic acid or an oxaloacetic acid. In what pathway will pyruvic or oxaloacetic acid be used and why is this pathway important? 2. Discuss the reaction mechanism involved how the -NH2 groups of amino acids are being metabolized. 3. Explain why gluconeogenesis under conditions of starvation or diabetes breaks down body proteins. Complete answer please. Thank you. |2. A 4-year-old girl was diagnosed with thiamine deficiency and the symptoms include tachycardia, vomiting, convulsions. Laboratory examinations reveal high levels of pyruvate, lactate and a-ketoglutarate. Explain which coenzyme is formed from vitamin B, and its role in oxidative decarboxylation of pyruvate. For that: a) describe the structure of pyruvate dehydrogenase complex (PDH) and the cofactors that it requires; b) discuss the symptoms which are connected with the thiamine deficiency and its effects on PDH and a-ketoglutarate dehydrogenase complex; c) explain the changes in the levels of mentioned metabolites in the blood; d) name the deseribed discase,
- 8. In patients after prolonged hepatitis, the ALT and AST activities were measured in the blood serum. What transaminase activity is inereased to a greater extent, and why? For the answer: a) explain the meaning of the enzyme diagnostics; b) draw the scheme of reactions catalyzed by ALT and AST; c) point out coenzyme of these reactions; describe vitamin from which this cocnzyme is derived; d) describe the biological importance of this type of reactions in amino acid metabolism; e) specify the demands which are claimed to enzymes been used in enzyme diagnostics.11. Write the mechanism of all three enzymatic steps of the a-ketoglutarate dehydrogenase complex, indicating which steps occur in which enzyme (E1, E2, E3) active sites.1. Write the ten reactions of the glycolytic pathway, naming all enzymes and providing the structural formulas of their substrates and products.
- 1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial 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. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:3. Palmitate is radiolabeled at the ¹¹ position using ¹4C. This is added to a liver homogenate. Trace the flow of the radiolabeled carbon as the palmitate is catabolized and then used for ketone body production. If a molecule can have the radiolabel in two different positions, make sure to show both possibilities. Present your work as a progression through the catabolic pathway, showing the product(s) from every round of B-oxidation and the subsequent steps to ketone body production that contain the radiolabel. Make sure each step also shows any needed cofactors and/or enzymes.1. Select the INCORRECT statement about Glutamate dehydrogenase : a. Catalyzes the removal of NH4+ into glutamate b.Catalyzes the incorporation of NH*4 into a-ketoglutarate c. Catalyzes the removal of NH*4 from glutamate C d. Catalyzes the incorporation of NH'4 into a-keto acid