C. What types of inhibitors of this enzyme is shown below? (1). D. What effect (increase, decrease, stay the same) does the inhibitor have on Vmax? E. What effect (increase, decrease, stay the same) does the inhibitor have on Km?
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![C. What types of inhibitors of this enzyme is shown below?
[1].
D. What effect (increase, decrease, stay the same) does the inhibitor have on Vmax?
E. What effect (increase, decrease, stay the same) does the inhibitor have on Km?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F1477abb9-d688-4e57-8562-687cc6a266e8%2F6f70b2a2-22a5-456f-80f1-4f44674a84a2%2F2xg2bji_processed.jpeg&w=3840&q=75)
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- What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?Under what conditions, a higher rate in the presence of the inhibitor observed? (how could the effect of inhibitor be compensated) explain1, For EACH of the following enzyme categories, (1) describe what the general function of the enzyme is; (2) identify a SPECIFIC enzyme in glycolysis that performs this function; and (3) identify the names of the organic substrate and product for the specific enzyme identified. Remember that the name of the category need not appear in the actual name of the enzyme. A. First enzyme category: kinase (answer (1), (2), and (3) B. Second enzyme category: dehydrogenase (answer (1), (2), and (3) C. Third enzyme category: isomerase (answer (1), (2), and (3)
- A. Elastase is activated by trypsinB. Trypsinisactivatedbyelastase Which statement is correct? Proteolytic activation of chymotrypsin from chymotrypsinogen requires cleavage of four peptide bonds. Assume that any proteases can convert 100 substrates to 100 products. Activation of one enteropeptidase can eventually lead to formation of how many chymotrypsin proteins?B) 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 ouier cem types. General mechanism of enzyme regulation: /1 b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as th perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzyn 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: a) In point form, describe the steps by which ATP is produced…In pure noncompetitive inhibition: a. Where on the enzyme does the inhibitor bind? b. Does the inhibitor bind to E, ES or both? c. What is the effect of I on Vmax? d. What is the effect of I on Km?
- A. Provide a reasonable mechanism for the production of geranyl pyrophosphate from IPP andDMAPPB. How many molecules of IPP and how many molecules of DMAPP would you need to makefarnesyl pyrophosphateInhibitors of acetylcholinesterase, such as edrophonium, are used to treat Alzheimer’s disease. The substrate for acetylcholinesterase is acetylcholine. Structures are attached. What kind of inhibitor is edrophonium? Explain. Can inhibition by edrophonium be overcome in vitro by increasing the substrate concentration? Explain. Does this inhibitor bind reversibly or irreversibly to the enzyme? Explain.A.What is the Result of the sodium potassium ATPase activity in the cell? B.What mechanism does the sodium potassium ATPase use to achieve this result? C. Why is the above-mentioned change in affinity critical for the sodium potassium ATPase to perform its function?
- a. How to distinguish fresh fish? Do you think this has anything to do with the biochemical changes that occur when a fish is caught or harvested? Explain briefly b.What are the signs of cooked fish and shellfish. Explain(c) Discuss the mechanism of action of the enzyme chymotrypsin.What are the measures to inhibit the Maillard reaction in undesirable situations. please explain detailed
