please answer it Which of the following statements about enzyme regulation is incorrect?Feedback inhibition is a mode of enzyme regulation employing negative allostery, where thefinal product of a pathway inhibits the first step of the same pathwayThe differential KM and Vmax of hexokinase isoforms between the liver and muscle allows thetuning of enzyme activity to different substrate concentrations and overall tissue functionThe covalent modification of enzymes is a mechanism of regulation requiring kinase activity toinstall the phosphate, but where dephosphorylation can't occur spontaneouslyProteolytic activation of enzymes converts a zymogen to an active enzyme by removal ofpeptide components and/or rearrangement of the protein backbone.O All answers are correctLL

Enzyme regulation is the process by which enzyme activity is regulated either by allosteric…

Answered: Which of the following statements about…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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…
n a particular enzyme, an alanine residue is located in a cleft where the substrate binds. A mutation that changes this residue to glycine has little effect on activity; however, another mutation, which changes the alanine to a glutamate residue, leads to a complete loss of activity. Provide a brief explanation for these observation
In the rete mirabile serving the red swimming muscles oftunas, some key enzymes of catabolism show gradients ofconcentration: They are more concentrated at the cold end of therete, and less concentrated at the warm end. These variationsparallel variations that are often seen in the thermal acclimationof poikilotherms, when enzyme concentrations rise duringacclimation to cold and fall during acclimation to heat. Whatdo you think could be some of the reasons for these spatial andtemporal variations in enzyme concentration? Why not havethe highest observed enzyme concentrations everywhere at alltimes?
What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require light
Which statement is false for transition-state analog enzyme inhibitors? They fit the active site better than the substrate. Although they cannot perfectly mimic a transition state, they are important to the design of new pharmaceutical agents. Phosphoglycolohydroxamate inhibits the glycolytic enzyme aldolase nearly 10,000 times better than dihydroxyacetone phosphate. Due to noncovalent interactions with the active site, this type of inhibitor is reversible.
Which of the following statements are true about enzyme regulation via noncovalent interactions? Select all that apply. Molecules can cause a change in enzyme shape because they're able to bind to the enzyme somewhere other than the active site The function of an enzyme is altered by a chemical change in its primary structure, which is called phosphorylation Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to the enzyme's active site Molecules that are similar to the substrate in both size and shape can compete with the substrate for access to a location other than the active site
Because 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?
If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:
In a particular enzyme,an alanine residue is located in a cleft where the substrate bonds.A mutation that changes this residue to glycine has little effect on activity,however another mutation ,which changes the alanine to a glutamate residue,leads to loss of activity.Provide a brief explanation for those observation
The catalytic mechanism of bovine pancreatic RNase A relies upon acid-base catalysis involving the amino acid O imidazole lysine K histidine Oaspartic acid glutamic acid
Which of these statements about enzyme-catalyzed reactions is false? The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 V, max: At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. If enough substrate is added, the normal V, of max a reaction can be attained even in the presence of a competitive inhibitor.
Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above

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