HCO3 + Glutamine + ATP Carbamoyl phosphate + Aspartate AT Case N-carbamoylaspartate -UMP UTP CTP
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- Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.b) Following this experiment, you would like to elucidate the mechanism of action of pyruvate kinase. Unfortunately, the crystal structure of pyruvate kinase is not available, which requires the enzyme to be modelled based on the available three-dimensional structures of related enzymes. Suggest a bioinformatics approach that can be conducted to perform this study.
- In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complexBecause it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATE
- Identify the type of regulation of enzyme activity seen in the following situations - for example, competitive inhibition, allosterism, phosphorylation, zymogen conversion, association-dissociation, feedback inhibition, etc. a. Trypinsogen, which is not catalytically active, is converted to the active enzyme trypsin by removal of a hexapeptide from the N-terminal end. b. The dimer protein kinases is catalytically inactive. Binding of cAMP causes protein kinase dimer to split into its monomer which are active catalysts.create a detailed flow chart or diagram that will illustrate all the important features of the glycolytic pathway. I want you to place in your flow chart or diagram the following important information like: 1. the reactants and products of each step, 2. enzymes involved in each step, 3. important by-products generated in some steps, 4. type of the reaction of each step, 5. and the outline of the two stages of the pathway. Also, discuss briefly (4 sentences) how Galactose and Fructose enter the glycolytic pathway.During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.
- In step 4 of glycolysis, F16BP is converted to GAP and DHAP. In the mechanism carried out by the aldolase (the enzyme the carries out this reaction) an active site lysine residue reacts with the substrates' carbonyl group to form a Schiff base. Briefly, what is the logic behind the formation of the Schiff base (i.e. why is it beneficial that the enzyme forms this Schiff base)?ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction? uncompetitive inhibitors heterotropic modulators homotropic modulators mixed inhibitorsAMP- PNP is a non-hydrolyzable ATP analog that cannot be metabolized by cells. Taurocholate is a bile acid that helps emulsify fats. When taurocholate is added to hepatocyte cell culture, it accumulates in those cells. The graph below shows the rate of cellular accumulation of the drug taurocholate in the presence of either ATP, ATP, or AMP-PNP. Based on this date, describe the mechanism by which taurocholate enters the cell. Justify the answer.