Propose a reasonable pathway to degrade the following amino acid to core metabolic intermediates. Mechanisms are not required, but be sure to include relevant cofactors. Based on your pathway, would this amino acid be glucogenic, ketogenic, or both? *H3N. NH3*
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- 6. Reciprocal regulation of opposing pathways is necessary to avoid the wasteful synthesis anddegradation of metabolic intermediates. Provide two distinct examples of reciprocal regulation. Bespecific, and be sure to explain the conditions that signal enzyme activation and/or inhibition.5. Gout can be caused by superactivation of PRPP synthase, or partial deficiency of hypoxanthine-guanine phosphoribosyl transferase. Why the change in these enzyme activities can induce the development of this disorder? For the answer: a) write down the scheme of the reactions catalyzed by these enzymes;b) specify metabolic pathways these reactions take part in; c) answer the main question of the problem.9. The transamination of the amino acid aspartate is catalyzed by aspartate aminotransferase. A) Draw out the mechanism for aspartate aminotransferase - you don’t need to show the subsequent formation of glutamate by the transaminase. B) After transamination, write out the subsequent steps (no mechanisms) to generate a molecule of glucose from two aspartates. How many ATP equivalents would this consume? C) After the transamination, write out the subsequent steps (no mechanisms) to fully oxidize aspartate into CO2 through malate (see above). How many ATP equivalents would this produce?
- 1. Describe the glucose oxidase's general enzymatic class (oxidoreductase, transferase, isomerase, hydrolase, ligase, or lyase), which types of cells express this enzyme, and what its role is within those cells and/or their surrounding tissues. 2. Describe glucose oxidase's substrate, the substrate’s biological relevance, and identify the main interaction that governs how the substrate binds (e.g. specific salt bridges, negative/positive patches, hydrophobic pockets) 3. Describe two different ways in which glucose oxidase is regulated. These mechanisms of regulation do not need tobe allosteric in nature, but they often are—for any allosteric regulatory mechanisms, indicate whether they arepositive/negative, homotropic/heterotropic, and whether they constitute an example of feedback inhibition19. From the various reactions you have learned in catabolism of amino acids; list three reactions in which NH4 is used as substrate to yield different products, in other words, reactions that will reduce NH4 concentration in the cell.#1)What are the main roles of the following amino acids; (within the crystal structure and/or active site. be specific, with pictures and mechanistic arrows as needed) -Glu305 from pyruvate carboxylase -Gln23 from Penecilin Acylase -Ser203 from Acetylcholinesterase #2) Why is L-tetrahydro-2-furoic acid would be a suitable inhibitor for Proline oxidase?
- 3. (Part A) The intermediates of a pathway are shown in the following scheme. Using curved arrows, show the mechanism of each step labeled with a blue letter. Draw out the structures of all coenzymes, so that you can effectively show all arrow pushing. You may abbreviate the coenzymes by putting R groups on the molecule, but do draw out the parts of the structure that are involved in the arrow pushing. Please note that some of the transformations will require you to show multiple structures to show all of the arrow pushing (particularly some of the coenzyme-mediated steps). You do not need to show specific amino acid residues that perform the catalysis. You can abbreviate acidic amino acid residues "Enz-B-H" and basic residues "B-Enz". HO O O HO NH₂ OH ATP ADP (A) H₂O3PO H₂O (D) O NH₂ O HO. O OH NADPH (B) NADP+ OH ILI I Igr OH HO OH O OH NH₂ O NH₂ H₂O OH (E) (C) OH OH1. 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?8. The enzyme thiolase catalyzes one step in the ß-oxidation of saturated fats. One portion of the mechanism for this reaction is shown below. Describe the catalytic mechanism at work. (Note: "SCOA" is shorthand for the compound Acetyl-CoA) RCOCH₂COSCoA + HSCOA → H3C₂OSC0A + RCOSCOA HN NH CH₂ NH CH₂ CH₂ FS Grease NH3 H-SCO A NH CH2 CH₂ NH3 S Co A CH₂ NH 1 3 H-SCO A H3C SCO A NH3 a h-SCOA R-C S Co A CH₂ CH₂ C H₂ 0=0 HN NH + NH3 H₂C HN CH₂ NH CH₂ CH₂ 2 S Co A CH₂ NH NH
- 3) Read the situations below and indicate which of the four methods of enzyme regulation is occurring for each. a) The energy-carrying molecule ATP is made by the enzyme ATP synthase. Muscle cells use a lot of energy and also have higher amounts of the ATP synthase enzyme than many other cell types. General mechanism of enzyme regulation: S b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as the perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzym called cyclo-oxygenase. "Ibuprofen" is the active ingredient in a variety of anti-inflammatory medications such as Motrin® and Advil®. It reduces pain and swelling by binding to a hydrophobic channel in the active site of cyclo-oxygenase, blocking the polyunsaturated fatty acids from binding to the enzyme, and therefore stopping production of prostaglandins. General mechanism of enzyme regulation: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: X1. A metabolic pathway proceeds according to the scheme, R → S →T→U→ V→ W. A regulatory enzyme, X, catalyzes the first reaction in the pathway. Which of the following is most likely correct for this pathway? A) Either metabolite U or V is likely to be a positive modulator, increasing the activity of X. B) The first product S, is probably the primary negative modulator of X, leading to feedback inhibition. C) The last product, W, is likely to be a negative modulator of X, leading to feedback inhibition. D) The last product, W, is likely to be a positive modulator, increasing the activity of Х. E) The last reaction will be catalyzed by a second regulatory enzyme.