rearrangement of molecules O formation of an enzyme-substrate complex O catalysis of the reaction O.formation of the transition state
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- In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.Allosteric regulation O The product of a series of reactions acts as an inhibitor for an earlier reaction. O Hormones control the synthesis of enzymes. A regulator binds to the enzyme at a site other than the active site. This binding changes the shape of the enzyme and alters the catalytic ability of the enzyme. An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of the second substrate to the active site. The activity of an enzyme is influenced by the addition or removal of a group that is covalently bonded to the enzyme. O An inhibitor forms covalent bonds to the active site. permanently blocking it.Allosteric regulation of an enzyme is accomplished when the enzyme pathway's product accumulates and then binds to the active (catalytic) site of the enzyme O True False
- Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme U the active site of the enzyme must be flexible O only one substrate could be converted to product by the enzyme the entire enzyme must be rigid the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures O the active site of the enzyme must be rigid Submit Answer Retry Entire Group 5 more group attempts remainingWhich 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
- Enzyme inhibition (compare and contrast reversible and irreversible inhibitors)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 siteOnly a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.