BBMB 301 Chapter Notes - Chapter 8: Uncompetitive Inhibitor, Enzyme Inhibitor, Nucleophile

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jadeox319

1 Oct 2017

School

Iowa State University

Department

Biochemistry, Biophysics, and Molecular Biology

Course

BBMB 301

Professor

Thornburg Robert

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Study graphs in chapter 8: chymotrypsin an enzyme that temporarily undergoes covalent catalysis as part of its mechanism. In conducting an experiment with a new drug, you find that regardless of the concentration of substrate, the drug is able to inhibit the enzyme activity. The enzyme inhibition that can be overcome by increasing the concentration of substrate. A(n) ________________ inhibitor has a structure similar to the substrate and reversibly binds to the active site of the enzyme. Which type(s) of inhibition can be reversed: competitive, noncompetitive, uncompetitive, all of the above, none of the above. In this type of inhibition, the inhibitor can only bind to the es complex to form an esi complex: competitive, noncompetitive, irreversible, uncompetitive, none of the above. The metal most commonly found at the active site of metalloproteases is: zinc, calcium, selenium, magnesium, sodium. The type of catalysis in which two substrates are brought into close proximity.

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B. C. Mixed tive 8. The panereas is protected from digestion by trypsin (a proteolytic enzyme that it produces) because: A. B. C. D. Trypsin works only on denatured proteins Trypsin is specific for plant proteins Trypsin works only at the surface of membranes Trypsin is not activated until it is proteolytically modified 9. The active site of an enzyme is the region that A. binds allosteric regulators of the enzyme. B. is involved in the catalytic reaction of the enzyme C. binds noncompetitive inhibitors of the enzyme D. is inhibited by the presence of a coenzyme or a cofactor 10. According to the induced fit hypochesis of enzyme catalysis,which of the following is corect? A. The binding of the substrate depends on the shape of the active site B. Some enzymes change their structure when activators bind to the enzyme C. A competitive inhibitor can outcompete the substrate for the active site D. The binding of the substrate changes the shape of the enzyme's active site 11. Increasing the substrate concentration in an enzymatic reaction could overcome which of the following? A. denaturization of the enzyme B. allosteric inhibition C competitive inhibition D. saturation of the enzyme activity 12. Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as a(n) A. competitive inhibitor of the enzyme B. noncompetitive inhibitor of the enzyme C. allosteric activator of the enzyme. D cofactor necessary for enzyme activity 13. Some of the drugs used to treat HIV patients are competitive inhibitors of the HIV reverse transcriptase enzyme. Unfortunately, the high mutation rate of HIV means that the virus rapidly acquires mutations with amino acid changes that make them resistant to these competitive inhibitors. Where in the reverse transcriptase enzyme would such amino acid changes most likely occur in drug-resistant viruses? A. in or near the active site B. at an allosteric site Cat a cofactor binding site D. in regions of the protein that determine packaging into the virus capsid the fever is not controlled? When you have a severe fever, what grave consequence may occur if A. destruction of your enzymes' primary structure B. removal of amine groups from your proteins C. change in the tertiary structure of your enzymes D removal of the amino acids in active sites of your enzymes 14.

An allosteric interaction between a ligand and a protein is one in which: 74. changes in Km are negligible, so Km can be treated as a constant. C. binding of a molecule to a binding site affects binding of additional molecules to the same site. binding of a molecule to a binding site affects binding properties of another site on the protein. binding of the ligand to the protein is covalent. multiple molecules of the same ligand can bind to the same binding site. A. D. VO Vmax. E. varying [S] has no effect on Vo. 78. The steady state assumption, as applied to B. enzyme kinetics, implies: Km = Ks. the enzyme is regulated the ES complex is formed and broken down at equivalent rates. the Km is equivalent to the cellular substrate concentration A. B. C. C. D. D. E. the mximum velocity occurs when two different ligands can bind to the same binding site. E. the enzyme is saturated. The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: 79. 75. One of the enzymes involved in glycolysis aldolase, requires Zn2+ for catalysis. Under conditions of zinc deficiency, when the enzyme may lack zinc, it would be referred to as the: Substrate added vo COmol/min) (mmol/L) A. apoenzyme. B. coenzyme. C. holoenzyme. D. prosthetic group. E. substrate 0.8 217 325 488 647 76. 1,000 The role of an enzyme in an enzyme- catalyzed reaction is to: bind a transition state intermediate, such that it cannot be converted back to substrate. ensure that all of the substrate is converted to product ensure that the product is more stable than the substrate. increase the rate at which substrate is converted into product. make the free-energy change for the reaction more favorable. A. The Km for this enzyme is approximately: B. C. D. E. A. 1 mM B. 1,000 mM. C. 2 mM D. 4 mM E. 6 mM 80. In competitive inhibition, an inhibitor: binds at several different sites on an enzyme. binds covalently to the enzyme. binds only to the ES complex. binds reversibly at the active site. lowers the characteristic Vmax of the enzyme A. B. C. D. E. 77. The benefit of measuring the initial rate of a reaction VO is that at the beginning of a reaction: A. [ES] can be measured accurately. B. changes in [S] are negligible, so [S can be treated as a constant

BBMB 301 Chapter Notes - Chapter 8: Uncompetitive Inhibitor, Enzyme Inhibitor, Nucleophile

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