i need the answer quickly 10. Isoniazid (MAO inhibitor) is prescribed to the patient with Parkinson disease.What does cause this disorder? What is the mechanism of prescribed drag? Forthe answer:a) specify the neurotransmitter the disturbed formation of which causes this disorder;b) present the scheme of its synthesis and point out the most probableenzymatic block;c) write down the reaction catalyzed by MAO, give the full name of the enzyme,specify coenzyme and explain the mechanism of isoniazid action.

Parkinson's disease is the second most common movement illness, affecting one million people in…

Answered: 10. Isoniazid (MAO inhibitor) is…

Phlebotomy Essentials

6th Edition

ISBN:9781451194524

Author:Ruth McCall, Cathee M. Tankersley MT(ASCP)

Publisher:Ruth McCall, Cathee M. Tankersley MT(ASCP)

Chapter1: Phlebotomy: Past And Present And The Healthcare Setting

Section: Chapter Questions

Problem 1SRQ

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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.
. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.
8. 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;
5.Aspirin isthedrug,used for the decreasing ofinflammatory reaction and temperature. 1)Describe the mechanism of aspirin action. 2) What types of reversible inhibition do you know.3)Give the examples of drugs acting as such inhibitors.
13.) An unchanged apparent Km results from the action of an uncompetitive inhibitor because A) the presence of the inhibitor can shift the binding equilibrium toward the ES complex. B) the presence of the inhibitor can shift the binding equilibrium toward the E + S state. C) the presence of excess substrate shifts the binding equilibrium toward the ES complex. D) uncompetitive inhibitors do not alter the binding equilibrium between substrate and enzyme. E) Uncompetitive inhibitors always result in a lower apparent Km, not an unchanged apparent Km.
Identify the following statements as true or false. If a statement is false, explain what is wrong with that statement a) Transition state analogs bind very tightly with the enzyme active site as they form covalent bonds with the active site b) Receptor desensitization happens upon prolonged exposure of receptors to both agonists and antagonists c) Dactinomycin and Doxorubicin are examples of drugs that bind with the major groove of DNA d) Mitomycin C forms interstrand crosslinking while cisplatin forms intrastrand crosslinking of DNA
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.
8. Hypercholesterolemia is a frequent complication of diabetes mellitus in patients with prolonged hyperglycemia. Why a high level of glucose in blood causes hypercholesterolemia and atherosclerosis? For the answer explain: a) how glucose can interact with the proteins and the consequences of this reaction for the proteins; b) glycation of which proteins results in hypercholesterolemia; c) possible causes and complications of hypercholesterolemia.
2. a) Outline the general mechanism of a coenzyme B12-dependent enzyme which catalyzes the following reaction. HO H R-C-C-H ĤIÓN - H₂O HIC-H R-C-C O= H b) When R is CH3, what would the name of the enzyme be, and what would be the full EC number? Justify the first number of the EC number.
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.
7. Identify the type of inhibition in each description. A) competitive B) noncompetitive C) Irreversible 1) an inhibitor that resembles the structure of the substrate 2) an inhibitor that forms a covalent bond with a side chain in the active site 3) Adding more substrate does not reverse the effect of this inhibitor. 4) The inhibition can be reversed by increasing the concentration of substrate. 5) The inhibitor does not resemble the substrate.
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?

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