48- Which of the following statements most accurately describes the ! conclusions of the experiment with ribonuclease A? & 4. Enzyme activity is preserved evenwhen the pratein is denatured. = TNO RHREY oid Zann Dr epn Leas NR: Se NSAERP ERT dimensional structure. ¢. Denaturants, such as urea, are'sufficient to completely denature ribonuclease d. Protein denaturation is rarely reversible. 49- Which one is an attribute of enzyme? @. Increases rate of reaction. b. Most efficient catalyz*. €, Specific in nature. d. All the above 50- Which of the following statements about enzymes is INCORRECT? a. Enzymes increase the rate o¥ reactions by lowering the free energy of activation. b. Enzymes alter the equilibrium constant of the reaction they catalyze. ¢. Mast enzymes are proteins, & d. Enzymes are biological catalysts. 51° Which of the following statements is NOT CORRECT for an enzyme- catalyzed reaction? @: both the substrate and product molecules are bound to the enzyme tibleGule: | b, the substrate binds to the enzyine. ¢. product-enzyme complex is formed during the reaction d. the product is Formed at the enzyme molecule then re leased.| Chapter 7 behavior 6 . we main distinguishing feature of the concerted model for the allosteric enzymes is that: ‘A. it applies only to dimeric enzymes B.it involves three possible conformations far all subunits € the conformation of all subunits changes simultaneously D. the T ond R conformations exist in roughly equal amounts ANS: ¢ 53- Feedback inhibition refers to: A. Effect of substrate on rate of enzymatic reaction. 8. Effect of end product on rate of enzymatic reaction C Effect of enzyme concentration on rate. of enzymatic reaction. D. Effect of external compound on rate of enzymatic reaction ANS: B 54- How do each of these compounds affect the function of ATCase? A. ATP is.aK effector and CTP is a V effector B. ATP isa V effector and CTP is ak effector. €. Both ATP and CTP are K effectors D. Both ATP and CTP are V effectors ANS: ¢ 55- The catalytic triad of chymotrypsin and other serine proteases consists of: A. three subunits of the enzyme. B. three amino acid residues adjacent in the primary structure which act to make serine a strong nucleophile ¢. three enzymes with very similar structural features D. three amino acid residues close enough in space to make serine a strong nucleophile ANS: D57- The role of serine at the active site of chymotrypsin is to act as a__ catalyst, while the histidine residue acts as a__ catalyst. A- weak, strong. 8 nucleophilic, acid-base. acid-base, covalent, D- strong, weak 58- Glycogen phosphorylase a (R-state) is inactivated by AMP: True False. 59- Glycogen phosphorylase b (T-state) is activated by: A- glucose. B- ATP. CAMP, D- Caffeine. 60- Allosteric inhibition A- Makes active site unfit for substrate. 8- Controls excess formation and end product, C- Both of the above. D- None of the above,|| C- shows that cooperative kinetics are observed 61- Tf on enzyme is irreversibly inhibited by N-tosylamida L-phenylethy! chloromethyl ketone (TPCK) What does this show? A- The enzyme has been denatured by TPCK. B- Histidine is likely an ‘important residue in the active site. ‘© TPCK is an allosteric modulator af the enzyme. D-TPCK is an analog of the enzyme's substrate. 62- Which of the following coenzymes is involved in aldehyde transfer reaction? A> Biotin 8- Thiamine Pyrophosphate C- Riboflavin: D- Coenzyme A 63- Which of the following statements is NOT TRUE? “ Conformational change of the sodium-potassium pump protein is necessary for sodium ion movement outside the cell, | B- ATP is required for sodium-patassium exchange. | & Movement of sodium ions outside the cell occurs against its concentration gradient. D- Movement of sodium ions outside the cell occurs in the direction of its concentration gradient. ANS: D, 64- In the reaction catalyzed by chymotrypsin, a graph in which the rate is plotted against the concentration of substrate. |) - is sigmoidal, characteristic of an allosteric enzyme. | B- shows that the reaction is zero order, D- is hyperbolic, characteristic of a non-allosteric enzyme.65- Which of the following coenzymes is invalved in transfer of one! units? 8. Niacin, ‘D- Biotin. ANS: A 66- CTP is a known inhibitor of ATCase, which is the enzyme that catalyzes The first reaction in the pathway for the synthesis of this compound, This is an example of A- negative cooperativity B- irreversible inhibition © feedback inhibition D- zymogenic inhibition 67- Which of the following statements is correct about chymotrypsinogen? A- Synthesized and stored in the liver. lypeptide chain of 254 amino acid residues cross-linked by two B- Consists of a single poh disulfide (-S-S-) bonds. © When secreted into the small intestine, the digestive enzyme trypsin cleaves 6 Polypeptide bond from the N-terminal end to give active p-chymatrypsin. D- All af the above. ANS: C 68- In the concerted model the binding of the first substrate malecule will achieve all except: ‘A- facilitation of the binding of other substrate molecules. B- facilitation of the conversion of other subunits to the active state, € facilitation of the binding of inhibitors to the enzyme, D- all of these answers are correct.Ssh $4@ 8:46 lS Pa ae Biochemisrty station F Bye Pal 4 Lette ala smelt) yA) FOUL Ene ea ner Seo 1D) A ares ies] peer) La © 136 ¢ 6:26 a Biochemisrty station 2023 cA AO erence lees aaa a eeu icc shows that the reaction is zero order. & shows that cooperative kinetics are observed. | >> is sigmoidal, cheracteristic of an allosteric enzyme. Ans: B jeaver ~ Burk plot is useful in the analysis of enzymatic reactions ibitors. ‘enzyme displays Michaelis - Menten kinetics, ¢- it can be used whether or not the | D- all of the above. ae 20 ae a 10- Given the rate law, rate= k [A] (B], the overall reaction erderts A- zero. Ars: A C-one, | - cannot be determined, 7 stitgnamie’ Noa sented tala Sk on-set beth his ote ; il Eh ‘Wis deine sgmteer11- According to the steady ~ state assumption: ‘A- the substrate concentration is large and does not change significantly B- the free enzyme concentration is always in great excess ta the concentration of enzyme Substrate complex: -the product concentration does not change significantly. 12- First order kinetics means: 8- More information is needed to answer this question. | & The rate of the reaction varies with the squore of the amount of the reoctant measured. D- The rate of a reaction is independent of the amount of reactant measured. Ane: & | 13- According to the Michaelis - Menton approach{ ke jeasures the: A- enzyme-substrate catalytic mechanism, B- enzyme-substrate complex dissociation & steady-state level. 14 What is the function of chymotrypsin? A-Breck peptide bond of acidic amino acid. 8- Break peptide bond of aliphatic amino acid. & Break peptide bond of basic amino acid, ANS: D | 15- Which of the following/accurately describes ‘the Michaelis - Menter model for inhibitor effects on enzyme kinetic behavior? ao ‘A- The difference between an {uncompetitive and| ce ncompetitivd rt 8- The rate of product formation distinguishes competitive, non~ competitive, and. uncompetitive inhibi } €- Vmax is unaltered in the presence of an uncompetitive inhibitor, b= A competitive inhibitor and substrate both bind free enzyme with the same affinity.from the substrate, ‘the reaction, A- is activated by one 8- is competitive with D- is reversible. | 19- + D+ none of the above. ‘A- binds covalently to th 16: The concept of " induced fit refers ‘to the fact that: A-when a substrate binds to D- none of the above. 18- A suicide inhibi a 8- A suicide inhibitor of an enzyme is one that: 20- In competitive inhibition an ai | © binds reversibly at the active site. ©- binds at several different sites on an enzyme. an-enzyme, the enzyme induces «loss of water (de - solvatian) ANS: B 17. The rate - determining Step of Michaelis Menten kinetics is A- the complex ion eteps.”) B tombe fo produce product. & the product formation step. type of enzyme for the purpose of inhibiting a second type of enzyme. Substrate. The active site of an enzyme mains =) A- at the center of globular(proteins, B- rigid and does not change/shc 1e enzyme.21- If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec/millimole) and tr. slope 75.3 L/sec, Vmax equals: A- 39.4 millimoles per second, B- 5.23 millimoles per second, © 0.0254 millimoles per second, se hich of the following statements is true for(enaymaticallylcatalyzed reaction? =a 8 he octWation energy ofthe reactions lowered so that fewer substrate molecules ean ‘overcome it. C- The activation energy of the reaction is increased, thus decreasing the likelihood that any Substrate molecules will overcome it. D- Additional substrate molecules are ‘energized to overcome the activation energy of the reaction ANS: A gy 23- The{nucleophile)in chymotrypsin mechanism is A- Serine —— } 8- water —~ © both (A) and (B) D- Asparagine ANS: € a 24- Which of the following is not true? & Tf areaction is spontaneous then it has a negative AG. B- Speed of a reaction is.a kinetic parameter, not a thermodynamic one. | &In thermodynamics, spontaneous dees not mean instantaneous or even fast. B- A reaction with a positive AGO ton never happen.25- Given an enzyme witha Key = 10 m mol and Vex = 100 m mal/min. Tf [S] - m mol, which of the following ¥ will be true? A-A10 - fold increase in Vnecwould increase velocity 10 - fold. i x B-A10- fold decrease inky would increase velacity. Ess C- Both (a) and (b). D- A 10 - fald increase in Vmex would decrease velocity 20 - fold ANS: ¢ 26- When on enzyme - catalyzed reaction had two substrates and substrate A must bind before substratd B, the mechanism is is called: ‘A~ a ping — pong mechanism. 8- 4 random mechanism, (© an ordered mechanism. D- a suicide mechanism. 27- The(rate\of a reactiondepends on: A- the activation eneray. B- the entropy change. C- the free energy change D- the enthalpy change. 26-| (A mixed “mixed noncompetitive inhibitor of an enzyme - scotalyzed reaction: Pee a, B- reduces Ku and increases Venax. | c- increases ku and reduces Vu, D- reduces Ku and reduces Vnas 29- Enzymatic activity has an gptimum temperature because: | 4 the rate of reactions is thermodynamically controlled B- raising the temperature speeds(iip'}he reaction until protein denaturation sets in. ¢- the component amino acids have varying melting points. | D- the side chains of essential residues are chemically degraded at higher temperatures" | 30- Ina Lineweaver - Burk Plot, competitive inhibitor shows which of the following effect? A- Tt changes the(x = Intercept. 8. Tt moves the entire curve to right. C- Tt moves the entire curve to left. D- Tt has no effect on the slope. a, 31- As catalysts, enzymes are: A- slightly more ef fective than nonenzymatic catalysts. B- slightly less effective thon nonenzymatic catalysts. C- significantly less effective than nonenzymatic catalysts. D- significantly driore ef fective than nonenzymatic catalysts. > ANS: D 32- Which of the following statements is NOT CORRECT for an enzyme- catalyzed reaction? “@ both the’ substrate and product molecules are bound'to the enzyme molecule b. the substrate binds to the enzyme. & product- enzyme complex is formed during the reaction. > d, the product is formed at the enzyme molecule then released. ANS: © | 33- The reason to rewrite the!Michaelis-Menten equation (such as the | Lineweaver-Burk plot) is to a. calculates catalytic proficiency | b form enzyme kinetic data as a hyperbolic curve. c. visualizes reactions better 4. calculates Vmax and Km. ANS:D 34- In the induced-fit model of substrate binding to enzymes: ! a, there is aggregation of several enzyme molecules when the substrate binds b. the substrate changes its conformation to fit the active site | || & the active site changes its conformation to fit the substrate | there isa conformational change in the enzyme when the substrate binds35- Which of the following statements about enzymes is INCORRECT? a, Enzymes increase the rate of reactions by lowering the free energy of activation _b. Enzymes alter the equilibrium constant of the reaction they catalyze. c. Most enzymes are proteins d. Enzymes are biological catalysts. nae 36- Which statement is true about enzyme inhibition? a. In competitive inhibition, the inhibitor binds to the active site of the enzyme. b. In irreversible inhibitign, a poison binds to the enzyme so: that it can never work again. © In noncompetitive inhibition, the inhibitor binds to the allosteric site of the substrate. | d. All the above. ANS:D 37- Which of the fallawing statements most accurately describes the Conclusions of the experiment with ribonuclease A? a. Enzyme activity is preserved even when the protein is denatured. b. The primary amino acid sequence of ribonuclease is the. primary determinant of its three dimensional structure; ¢. Denaturants, such as urea, are sufficient to completely denature ribonuclease. d, Protein denaturation is rarely reversible. ANS: D 38- In a Lineweaver-Burk plot, the y intercept equals @i/Vmax - b. i¢vkm Ckm d.[S} ANS: A 39- Which one is an attribute of enzyme? a, Increases rate of reaction | b( Most efficient catalyst € Specific in nature ANS:D d. All the above40- To catalyze a reaction anénzyme must: | a. increases the activation energy of the reaction. b. not binds to its substrate. Calter the equilibrium constant of the reaction, 1. increases the rate « P reacti 4. of the reaction. ansiD 41- The rate constant for the(dissociation of the ES complex to free enzyme and substrate is: @. keat baked Peo kd ke ANS: B 42- Which statement isitrue about enzyme inhibiti . Incompetitive inhibition, the inhibitor binds to the active site of the enzyme. b. In irreversible inhibition, a poison binds to the enzyme so that it can never work again. ¢. Innoncompetitive inhibition, the inhibitor binds to the allosteric site af the substrate. d. All the above. > ANS: D. 43- Ina Lineweaver-Burk plot, the y intercept equals: a: 1/Vmax. b. 1/Km. cc. km 4. [S$] ANS: A44- In the induced-fit model of substrate binding to enzymes «. there is aggregation of Sevendl enzyme molecules when the substrate binds. b. the substrate changes its conformation to fit the active site. © The active site changes its tonfarmation to fit the substrate. “d. there is a.conformational change in the enzyme when the substrate binds. 45- The reason to rewrite the Michaelis-Menten equation (such os the Lineweaver-Burk plot) is to 2. calculate catalytic proficiency 6. form enzyme kinetic data as a hyperbolic curve. c visualize 1 s better, ‘@ calculate Vmax and Kin, 7 46- To catalyze a reaction an enzyme must: @. increase the activatign energy of the reaction . b. not bind to its substrate. €. not alter the equilibrium-constant of the reaction. d. increase the rate’of the reaction, ‘and substrate is: a. keat ANS: D ANS: € ANS: D | 47- The rate constant for the dissociation of the ES complex to free enzyme ANS: B