Using the list of enzymes given below, provide all chemical structures and reactions for complete metabolism of the fatty acids 8:0, 18:145 and 12:247,10. It is unnecessary to repeat a reaction once it has been drawn out previously. Refer to the repeated reaction by group and number. Use the next pages if necessary and clearly identify which fatty acid is being metabolized.
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- Briefly describe the function of uridine triphosphate (UTP) in carbohydratemetabolism.Complete the following table by providing the reactants/substrates, enzymes and their functions as well as the products in each step of the Fatty Acid Degradation. Please provide the structure of the reactants and productsThe biosynthesis of vitamin D₂ is a two-step reaction, requiring two types of concerted pericyclic reactions. Draw in the arrows for each step and identify the structure of precalciferol. If an electrocyclic reaction is required, identify if it occurs through a conrotatory or disrotatory reaction. HO H H ergosterol hv precalciferol Cast HO ergocalciferol
- Suggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer.Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*Determine the sequence of a pentadecapeptide using the information below. carboxypeptidase: G aminopeptidase: R enzymatic hydrolysis fragments: TG, CT, SC, CH, CHP, FCT, RP, PIS, QKF, SCH, PME, EQK, KFC all fragments must be visible in the original sequence. Use one-letter abbreviations only. Write the complete answer in 3-aa length fragments
- List the systematic classification of enzymes according to the Enzyme Commission indication the class, subclass and sub-sub-class and give the description of each reaction.33333333333333333333333 Using the table below, differentiate the effect of two varying pH levels (as indicated by by the color) to the amylase enzyme. How does pH level affects the enzymatic reaction (enzyme-substrate complex)? Tube 1 Tube 2 Tube 3 Tube 4 Ingredients StarchAmylaseBuffer pH 7 StarchAmylaseBuffer pH 2 MaltoseWaterBuffer pH 7 StarchWaterBuffer pH 7 Color (1) (2) Orange BlueComplete the following tables by providing the reactants/substrates, enzymes and their functions as well as the products in each step of thefatty acid pathways.
- With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate poisoning? Example: Step 1: Fluoroacetate is converted to Product “A”. This reaction is catalyzed by Enzyme __________________________ Structures of fluoroacetate and the product “A”. Name of Enzyme. Step 2: Product “A” from Step 1 is converted to Product “B.” Catalyzed by enzyme 2. Structure of Product B and name of Enzyme 2. etc.Consider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.Describe the characteristics of allosteric enzymes and explain how the kinetic curves of such enzymes differ from Michaelis– Menten enzymes.