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4/3/2015

TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

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M O NDA Y ,

DEC EM B ER 7,

2009

Q:1:Thecatalyticactivityofanenzymeisrestrictedtoits

smallportioncalled

(A)Activesite

(B)Passivesite

(C)Allostericsite

(D)AllChoicesarecorrect

Q:2:Anactivatedenzymemadeofpolypeptidechainandaco­

factoris

(A)Coenzyme

(B)Substrate

(C)Apoenzyme

(D)Holoenzyme

Q:3:Koshlandin1959proposed

(A)Fluidmosaicmodel

(B)Inducefitmodel

(C)Lockandkeymodel

(D)Reflectiveindexmodel

Q:4:Enzymesarelargely

theirchemicalnature.

(A)Lipids

(B)Steroids

(C)Proteinaceous

(D)AllA,BandC

in

A B O U T

M E

(B)Steroids (C)Proteinaceous (D)AllA,BandC in A B O U T M E PROFILE MANSOOR AHMED Assistantprofessorin Biologycell#

Assistantprofessorin

Biologycell#

03337544304

L A B EL S

MCQTESTChapter=3(ENZYMES)(1)

4/3/2015

TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

Q:5:Whoproposed“lockandkey”modeltostudyenzyme–

substrateinteraction?

(A)Koshland(1959)

(B)WilhelmKuhne(1878)

(C)Fischer(1898)

(D)Noneofthese

Q:6:Inhumanbodytheoptimumtemperatureforenzymatic

activitiesis

(A)37oC

(B)40oC

(C)25oC

(D)30oC

Q:7:OptimumpHvalueforpepsinis

(A)5.5

(B)7.4

(C)4.1

(D)1.4

Q:8:Competitiveinhibitorsstopanenzymefromworkingby

(A)Changingtheshapeoftheenzyme

(B)mergingwiththesubstrateinstead

(C)blockingtheactivesiteoftheenzyme

(D)combiningwiththeproductofthereaction

Q:9:Theenzymesaresensitiveto

(A)ChangesinpH

(B)Changesintemperature

(C)BothAandB

(D)Noneofthese

Q:10:EnzymeBrequiresZn2+inordertocatalyzethe

conversionofsubstrateX.Thezincisbestidentifiedasa(n):

(A)Coenzyme

(B)Activator

(C)Substrate

(D)Product

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

Q:11:Theenzymeminusitscoenzymeisreferredtoasthe

(A)Iso­enzyme

(B)Metalloenzyme

(C)Apoenzyme

(D)Allofthese

Q:12:The“lockandkey”modelofenzymeactionillustrates

thataparticularenzymemolecule

(A)formsapermanentenzyme­substratecomplex

(B)maybedestroyedandresynthesizedseveraltimes

(C)interactswithaspecifictypeofsubstratemolecule

(D)reactsatidenticalratesunderallconditions

Q:13:Considerthisreaction.A+B­­>C+D+energy.

(A)Thisreactionisexergonic

(B)Anenzymecouldstillspeedthereaction

(C)AandBarereactants;CandDareproducts

(D)Allofthesearecorrect

Q:14:Aninhibitorthatchangestheoverallshapeand

chemistryofanenzymeisknownasa(n)

(A)Auto­stericinhibitor

(B)Competitiveinhibitor

(C)Stericinhibitor

(D)Noncompetitiveinhibitor

Q:15:Non­proteincomponentsofenzymesareknownas

(A)Coenzymes

(B)Activators

(C)Cofactors

(D)AllA,B,andC

Q:16:Thereactionbelowoccurswithinthecellstopreventthe

accumulationofhydrogenperoxide.Inthisreaction,catalase

functionsasan

4/3/2015

TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

4/3/2015 TalentCoachingCentre:MCQTESTChapter=3(ENZYMES) (A)Enzymeinthebreakdownofhydrogenperoxide

(A)Enzymeinthebreakdownofhydrogenperoxide

(B)Enzymeinthesynthesisofhydrogenperoxide

(C)Emulsifierinthedigestionofhydrogenperoxide

(D)Indicatorinthedetectionofhydrogenperoxide

Q:17:Anenzymeisgenerallynamedbyadding

theendofthenameofthe

to

(A)"­ase".coenzyme

(B)"­ase".cellinwhichitisfound

(C)"­ose".substrate.

(D)"­ase".substrate

Q:18:Theminimumamountofenergyneededforaprocessto

occuriscalledthe

(A)Minimalenergytheory

(B)Processenergy

(C)Kineticenergy

(D)Activationenergy

Q:19:Astudentconductsanexperimenttotesttheefficiency

ofacertainenzyme.Whichwouldprobablynotresultina

changeintheenzyme'sefficiency?

(A)Addinganacidicsolutiontothesetup

(B)Addingmoresubstratebutnotenzyme

(C)Increasingtemperatureofsolution

(D)Alla,b,&cchangeenzyme'sefficiency

Q:20:Enzymesfunctionas

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(A)Organiccatalysts

(B)Inorganiccatalysts

(C)Inhibitors

(D)Allofthese

Q:21:Acatalystisachemicalinvolvedin,butnot

by,achemicalreaction.

(A)Supported

(B)Changed

(C)Controlled

(D)Allofthese

Q:22:Manyenzymesfunctionby

activationenergyofreactions.

(A)Increasing

(B)Promoting

(C)Lowering

(D)BothAandB

the

Q:23:Anuncatalysedreactionrequiresa

(A)Higheractivationenergy

(B)Loweractivationenergy

(C)Balancedactivationenergy

(D)Allofthese

Q:24:Itsuggeststhatthebindingofthesubstratetothe

enzymealtersthestructureoftheenzyme,placingsome

strainonthesubstrateandfurtherfacilitatingthereaction.

(A)LockandKeyhypothesis

(B)Inducedfithypothesis

(C)Fischer’shypothesis

(D)D.D.Wood’shypothesis

Q:25:Theyarenon­proteinorganicmoleculesboundto

enzymesneartheactivesite.

(A)Activators

(B)Coenzymes

(C)Holoenzymes

(D)Allofthese

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

Q:26:Thefirststepinanyreactioncatalysedbyanenzymeis

theformationofaspecificassociationbetweenthemolecules

calledan

(A)Enzyme­productcomplex

(B)Enzyme­intermediatecomplex

(C)Enzyme­substratecomplex

(D)Noneofthese

Q:27:Thefunctionofcompetitiveinhibitorsisdefinedby

theirabilitytointeractorbindto

(A)Theactivesiteofanenzyme

(B)Regulatorysub­unitsofanenzyme

(C)Non­competitiveinhibitor

(D)Enzymecofactors

Q:28:Ifanenzymesolutionissaturatedwithsubstrate,the

mosteffectivewaytoobtainanevenfasteryieldofproducts

wouldbe

(A)Addmoreoftheenzymes

(B)Addmoresubstrate

(C)Addanallostericinhibitor

(D)Addanon­competitiveinhibitor

thefinalproductofa

metabolicpathwayturnoffthefirststepofmetabolic

Q:29:During

pathway.

(A)Positivefeedback

(B)Negativefeedback

(C)Competitivefeedback

(D)BothAandC

Q:30:

whichdoesnothavetoresemblethesubstrate,bindstothe

enzymeotherthanattheactivesite.

occurswhentheinhibitorychemical,

(A)NoncompetitiveInhibition

(B)CompetitiveInhibition

(C)Uncatalysedreaction

(D)AllA,BandC

Q:31:Whichoneisnotattributeofenzyme

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

(A)Specificinnature

(B)Proteininchemistry

(C)Consumedinreaction

(D)Increasesrateofreaction

Q:32:Whichoneinactivatesanenzymebyindirectly

changingtheshapeoftheactivesiteofanenzyme

(A)Non­competitiveinhibitor

(B)Competitiveinhibitor

(C)Coenzyme

(D)Activator

Q:33:Theenzymesareclassifiedinto

(A)Fivegroups

(B)Threegroups

(C)Sixgroups

(D)Fourgroups

Q:34:Non­proteinaceouspartofholoenzymeis

(A)Prostheticgroup

(B)Apoenzyme

(C)Tubulin

(D)Noneofthese

Q:35:Enymesarehighlyspecificforagivensubstratewhich

isduetotheshapeoftheir

(A)Activesite

(B)Allostericsite

(C)Non­competitivesite

(D)Noneofthese

Q:36:Thenameenzymewassuggestedin1878bytheGerman

physiologist

(A)WilhelmKuhne

(B)Koshland

(C)Fischer

(D)PaulFilder

Q:37:Proteinaceouspartofholoenzymeis

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(A)Prostheticgroup

(B)Apoenzyme

(C)Lecithin

(D)Noneofthese

Q:38:The"lockandkeyhypothesis"attemptstoexplainthe

mechanismof

(A)vacuoleformation

(B)pinocytosis

(C)sharingofelectrons

(D)enzymespecificity

Q:39:Anenzymethathydrolyzesproteinwillnotactupon

starch.Thisfactisanindicationthatenzymesare

(A)hydrolytic

(B)specific

(C)catalytic

(D)synthetic

Q:40:Thesitewhereenzymecatalyzedreactiontakesplaceis

called?

(A)Activesite

(B)Allostericsite

(C)Denaturessite

(D)DeadSite

Q:41:Whatisacofactor?

(A)Inorganicions

(B)Organicmolecules

(C)Bothaandb

(D)Noneoftheabove

Q:42:Mg+2isaninorganicactivatorfortheenzyme

(A)Phosophatase

(B)Carbonicanhydrase

(C)Enterokinase

(D)Amylase

Q:43:Zn+2isaninorganicactivatorforenzyme.

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

(A)Carbonicanhydrase

(B)Phosophatase

(C)Chymotrypsin

(D)Maltase

Q:44:Whichantibioticblockstheactivesiteofanenzymethat

manybacteriausedtomakecell­walls.

(A)Amphotericin

(B)Gentamicin

(C)Penicillin

(D)Cephalosporin

Q:45:DDTandParathionareinhibitorsofkeyenzymesin

(A)Nervoussystem

(B)Respiratorysystem

(C)Digestivesystem

(D)Circulatorysystem

Q:46:Athightemperaturetherateofenzymeaction

decreasesbecausetheincreasedheat

(A)ChangesthepHofthesystem

(B)Alterstheactivesiteoftheenzyme

(C)Neutralizeacidsandbasesinthesystem

(D)Increasestheconcentrationofenzymes

Q:47:Whichofthefollowingenzymeswoulddigestafat?

(A)sucrase

(B)protease

(C)Ligase

(D)lipase

Q:48:IntheLockandKeymodelofenzymeaction,thepartof

theenzymethatrecognizesthesubstrateisknownasthe

(A)Enzyme­substratecomplex

(B)Product

(C)Enzyme­productcomplex

(D)Activesite

Q:49:Whichmodelofenzymeactionisrepresentedinthis

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

diagram.

TalentCoachingCentre:MCQTESTChapter=3(ENZYMES) diagram. (A)Fluidmosaicmodel (B)Inducefitmodel (C)Lockandkeymodel

(A)Fluidmosaicmodel

(B)Inducefitmodel

(C)Lockandkeymodel

(D)Reflectiveindexmodel

Q:50:Acertainenzymewillhydrolyzeeggwhitebutnot

starch.Whichstatementbestexplainsthisobservation?

(A)Starchmoleculesaretoolargetobehydrolyzed

(B)Enzymemoleculesarespecificintheiractions

(C)Eggwhiteactsasacoenzymeforhydrolysis

(D)Starchiscomposedofaminoacids.

Q:51:Atabout0C,mostenzymesare

(A)Inactive

(B)Active

(C)Destroyed

(D)Replicated

Q:52:Vitaminsareessentialtothesurvivaloforganisms

becausevitaminsusuallyfunctionas

(A)Substrates

(B)Nucleicacids

(C)Co­enzymes

(D)Nucleosides

Q:53:Whenamoleculebindstoanareaofanenzymethatis

nottheactivesite,andchangestheshapeoftheenzymeso

thatitnolongercanwork,thisiscalled

(A)denaturation

(B)competitiveinhibition

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(C)noncompetitiveinhibition

(D)substratedelocation

Q:54:Whatisacoenzyme?

(A)Inorganicion

(B)Organicmolecule

(C)BothAandB

(D)Noneofthese

Q:55:Whichstatementbestexpressestheinformation

representedinthegraphshown?

representedinthegraphshown? (A)TheactionofenzymesvarieswithpH

(A)TheactionofenzymesvarieswithpH

(B)ApHof7providestheoptimumenvironmentfordigestive

enzymes

(C)GastricjuiceisactiveatapHextendingfrom0to12

(D)AcidshaveapHgreaterthan7

Q:56:Whichtypeofinhibitorisshowninthisdiagram?

Q:56:Whichtypeofinhibitorisshowninthisdiagram? Competitive (B)Non­competitive (C)Allosteric (D)BothBandC

Competitive

(B)Non­competitive

(C)Allosteric

(D)BothBandC

(A)

Q:57:Whichenzymerepresentsanenzymefunctioningin

thisreaction?

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

4/3/2015 TalentCoachingCentre:MCQTESTChapter=3(ENZYMES) (A)E (B)C (C)B (D)A AnswerKey 1.A 2.D 3.B 4.C 5.C 6.A 7.D 8.C

(A)E

(B)C

(C)B

(D)A

AnswerKey

1.A

2.D

3.B

4.C

5.C

6.A

7.D

8.C

9.C

10.B

11.C

12.C

13.D

14.D

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

15.D

16.A

17.D

18.D

19.D

20.A

21.B

22.C

23.A

24.B

25.B

26.C

27.A

28.A

29.B

30.A

31.C

32.A

33.C

34.A

35.A

36.A

37.B

38.D

39.B

40.A

41.C

42.A

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TalentCoachingCentre:MCQTESTChapter=3(ENZYMES)

43.A

44.C

45.A

46.B

47.D

48.D

49.C

50.B

51.A

52.C

53.C

54.B

55.A

65.D

57.C

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