Briefly explain chymotrypsin with reference to the following: a) Catalytic triad (not the mechanism just what it does): b) Oxyanion hole: c) Specificity (compared with trypsin, elastase):
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![2. Briefly explain chymotrypsin with reference to the following:
a) Catalytic triad (not the mechanism just what it does):
b) Oxyanion hole:
c) Specificity (compared with trypsin, elastase):
d) Induced Fit](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F424482ac-ef50-4214-a1e3-aaaeb325792a%2F0fd54f9c-1dfc-43b2-992f-7f0ed2b87035%2Fs6pg3e_processed.png&w=3840&q=75)
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- (a) Fill in the blank regarding the mechanism of chymotrypsin below. (1) Polypeptide substrate binds non covalently in the enzyme active site. The catalytic Triad includes a reactive Nucleophile that attacks the electrophilic amide C atom. (2) The resulting tetrahedral - Is stabilized by H-bonding interactions with the hole.(Note: this is the same word repeated) (3) Collapse of the tetrahedral intermediate and H * Transfer from- Lead to the Cleavage of the C-N bond. The N-terminal peptide is bound through acyl linkage to serine. (4) A Molecule then binds to the active site and attacks the acyl ester car- bonyl. (5) The resulting tetrahedral Tions with the Same word repeated). (6) The second peptide fragment is released, and the enzyme returns to its initial state. Intermediate is stabilized via enthalpic interac- hole. (Note: this is the same answer as (2), and is again the (b) Trypsin and chymotrypsin are two closely related proteases; however, trypsin cleaves after positively charged…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.16. This figure from Foundations should look familiar. Which protein is shown here? A) Aglycosidase B) A G-protein C) Chymotrypsin D) Hexokinase E) Trypsin catalytic triad Ser 195 His 57 H Gly 193 N-H R Ņ Ca CB Asp 102 R' 17. What kind of enzymatic mechanism is shown in this figure from Foundations? A) Specific acid-base catalysis with His57 as the base B) Specific acid-base catalysis with Ser195 as the base C) General acid-base catalysis with Ser195 as the base D) General acid-base catalysis with His57 as the base E) Metal ion catalysis N-H
- 5. Treatment of the patients with familial hypercholesterolemia by statins (pravastatin, for instants) allows to decrease cholesterol levels in blood up to the normal range. Explain the statin action on the cholesterol metabolism. For that: a) draw the scheme of the cholesterol synthesis, indicate the key enzyme of the pathway; b) name all mechanisms of the key enzyme regulation and statin's action; c) describe the structure of LDL receptor and its function in cholesterol metabolism; d) explain the cause of familial hypercholesterolemia and the symptoms of the disease.5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each optionIn what way(s) are Trypsin, Chymotrypsin, and Elastase different? (choose 1) a) They target different amino acid residues in proteins. b) They use different reaction mechanisms c) Both of the above d) Neither of the above
- 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: X8. In patients with diabetes mellitus type I, 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: b) write the reactions of synthesis and oxidation of these molecules, name the enzymes, coenzymes, reaction localization;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.
- 1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X 0 J mol-¹ and AG' is <0 J mol-¹ for this reaction. a) At standard states, is this reaction favorable? b) Is the reaction favorable or unfavorable at cellular condition? c) Is this an endergonic or exergonic reaction in the cell? d) Would you describe this as a thermodynamically downhill or uphill reaction in the cell?12. Nirogenase is an enzyme that converts the remarkably stable triple bond in N2 into a usable form. It uses an iron sulfur cluster comprised of iron and the sulfur atoms of several active site cysteine residues. Based on your knowledge of Biochemistry what is the enzyme doing to effectively carry out this reaction? a) stabilizing the transition state for the reaction by hydrophobic effects b) stabilizing the ground state for the reaction by hydrophobic effects c) stabilizing the transition state for the reaction by metal ion catalysis d) stabilizing the ground state for the reaction by metal ion catalysis e) all of the above6. Suggest a name for an enzyme that catalyzes each of the following reactions. a.) Oxidation of nitrite b.) Decarboxylation of citrate c.) Reduction of oxalateT
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