answer these Both tertiary structure and quaternary structure have? *Both structures have specific shapes that depend upon the amino acid sequence ofthe protein.Both structures are stabilized by numerous covalent hydrophobic and hydrophilicinteractions.Both structures must contain multiple a-helices and b-pleated sheets connected byturns. Enzyme A is an allosteric enzyme inhibited by galactose while Enzyme B is a covalentlymodified enzyme inhibited by phosphate. Which will occur during their regulation? *Enzyme A will become more inhibited as the concentration of galactose increases.Both enzymes will bind their regulating molecule to a specific active site on a catalyticsubunit.Enzyme B will become more inhibited as the concentration of phosphate increases.

Answered: Image /qna-images/answer/80550136-ee89-415b-87fb-6ba0888f3f82.jpg

Answered: soth tertiary structure and quaternary…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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Allosteric enzymes have two different binding sites why do they have two different binding sites and how does they influence enzyme function. Also tell is allosteric regulation competitive or non competitive inhibition Please help???? ASAP with complete answer
In a metabolic pathway, succinate dehydrogenase catalyzes the conversion of succinate to fumarate. The reaction is inhibited by malonic acid, a substance that resembles succinate and can bind at the active site but cannot be acted upon by succinate dehydrogenase. Is Malonate a competitive or non -competitive inhibitor. What is the difference between the two types of inhibition? Can you overcome inhibition caused by Malonic acid?
Select the graph that correctly illustrates the effect of a positive modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector. R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that this is a positively cooperative enzyme, meaning that the affinity for substrate increases with increasing substrate concentration.
Students conducting research observe the rate of an enzyme-catalyzed reaction under various conditions with a fixed amount of enzyme in each sample. When will increasing the substrate concentration likely result in the greatest increase in the reaction rate?
What is the effect of each of the 4 types of inhibitors on the initial rate of an enzyme catalyzed reaction?
The synthesis of compound 6 proceeds via the metabolic pathway given below. Which enzyme is most suitable for controlling the synthesis of compound 6 by feedback inhibition? Which compound is most likely to be a negative modulator of this enzyme? Which compound is most likely to be a positive modulator of this enzyme?
Enzymes are able to reduce the activation energy barrier in a number of ways. List at least three ways that enzymes help lower the energy activation barrier?
Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weight
a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?
When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.
Would you expect an “enzyme” designed to bind to its target substrate astightly as it binds the reaction transition state to show a rate enhancementover the uncatalyzed reaction? In other words, would such a protein actuallybe a catalyst? Explain why or why not.
A group of young researchers was working on a biochemical pathway. At that time, they produced an enzyme having altered active site. Do you think, the activity of the new enzyme would differ from the original one? Why? On a different reaction they found, an enzyme works best at a temperature near about 30 degree Celsius. At 60 degree Celsius, the enzyme becomes inactivated. Briefly explain, why that enzyme is not working at elevated temperature?

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