which of the following describes an enzyme ALLOSTERIC site? It is where catalysis occurs.It is where the substrate binds.It is where an inhibitor may bind.It covers a large portion of the enzymestructure.

Proteins that operate as biological catalysts are known as enzymes. They work by assisting in the…

Answered: which of the following describes an…

Science

Biochemistry

which of the following describes an enzyme ALLOSTERIC site?

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter3: Cells And How They Work

Section: Chapter Questions

Problem 8SQ: Enzymes _______. a. enhance reaction rates b. are affected by pH c. act on specific substrates d....

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An inhibitor was added to an enzyme and the expected rate of the reaction was not detected and the substrate was not utilized at all. This inhibitor is (choose one answer only): Is un-competitive, meaning the inhibitor binds to a site near the active site. Is competitive, meaning the inhibitor binds directly to the same active site as the subtrate. Is non-competitive, meaning the inhibitor binds to site other than the active site as the subtrate. Is irreversible, meaning the inhibitor binds covalently to the enzyme keeping the enzyme inactive permanently.
Please select all of the following statements that are true. Cofactors involve the use of vitamins to assist enzymes Competitive inhibitors bind to the same active site as the substrate. When the substrate binds to the enzyme the reaction rate increases. Non-competitive inhibitors can act as both inhibitors and activators.
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
Which of the following is characteristic of competitive inhibitors? the inhibitor could bind to the active site or to an allosteric site on the enzyme. the enzyme will mistake the inhibitor for its substrate, so that the inhibitor will end up covalently bound to the enzyme. the inhibitor can bind only AFTER the substrate has bound (i.e. it binds only to the ES complex). the inhibitor can bind reversibly at the substrate-binding site (the active site). the inhibitor will lower the characteristic Vmax of the enzyme.
Which of the following are characteristics of catabolic metabolic pathways? (Choose all correct answers). Overall oxidation of initial substrates so redox reactions involve use of NAD+ as oxidizing agent, converted to NADH. Large initial substrates are broken down to smaller final products. Overall reduction of intial substrates so redox reactions involve use of NADPH as reducing agent, converted to NADP+. The pathways are overall exergonic (negative delta G). Net production of ATP as a result of the pathway. Essentially irreversible
Classify the inhibitor characteristics according to one of three types of inhibition: reversible competitive, reversible noncompetitive, or irreversible. Reversible competitive inhibitor binds noncovalently at site other than active site 0° Reversible noncompetitive inhibitor structure resembles substrate structure inhibitor does not alter the maximum reaction rate Irreversible inhibitor binds.covalently and permanently at site other than active site
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
Classify each specific inhibitor or inhibitor characteristic according to one of two types of inhibition: competitive or noncompetitive.
When the enzyme hexokinase binds to glucose and ATP it undergoes a conformational change. All of the following are true about this enzyme-substrate binding EXCEPT: The active site changes shape so that it binds more tightly to the substrates The substrates are optimally positioned for the reaction to occur The substrates become contorted or strained, which increases their reactivity The activation energy of the reaction increases
hich of the following are advantages of quaternary structure? Choose all correct nswers 1) The genes may be for single subunits, rather than requirement for transcription and translation of giant sequences 2) Subunit construction may provide the structural basis for protein regulation 3) Multi-subunit proteins are more water soluble than single subunit proteins of the same size 4) Defects in protein synthesis may be fixed at the subunit level, rather than giant polypeptide level 5) May have multiple active sites - one on each subunit
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:
Classify the items as competitive or noncompetitive inhibitors for control of enzyme action. Bind to the allosteric site on the enzyme Not influenced by the concentration of substrate Resemble the substrate Do not resemble thhe substrate Bind to active site of the enzyme