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Home > Sciences > BiochemistryI > SixTypesofEnzymeCatalysts

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TheScopeof
Biochemistry
TheImportanceofWeak
Interactions
Introductionto
BiologicalEnergyFlow
OverviewofBiological
InformationFlow
ProteinStructure

24

26

SixTypesofEnzymeCatalysts
Althoughahugenumberofreactionsoccurin
livingsystems,thesereactionsfallintoonlyhalfa
dozentypes.Thereactionsare:

OxygenBindingby
Myoglobinand
Hemoglobin
Enzymes

1. Oxidationandreduction.Enzymesthatcarryoutthesereactionsarecalled
oxidoreductases.Forexample,alcoholdehydrogenaseconvertsprimary
alcoholstoaldehydes.

Chemical
Mechanismsof
EnzymeCatalysis
Chymotrypsin:An
EnzymeatWork

EnzymeRegulation
CovalentModification
EnzymesAre
Catalysts
SixTypesof
EnzymeCatalysts
Organizationof
Metabolism
Glycolysis
TheTricarboxylicAcid
TCACycle
Oxidative
Phosphorylation
Carbohydrate
MetabolismII

Inthisreaction,ethanolisconvertedtoacetaldehyde,andthecofactor,NAD,is
convertedtoNADH.Inotherwords,ethanolisoxidized,andNADisreduced.(The
chargesdon'tbalance,becauseNADhassomeotherchargedgroups.)Remember
thatinredoxreactions,onesubstrateisoxidizedandoneisreduced.
2.Grouptransferreactions.Theseenzymes,calledtransferases,move
functionalgroupsfromonemoleculetoanother.Forexample,alanine
aminotransferaseshufflesthealphaaminogroupbetweenalanineandaspartate:

RelatedTopics:
BiochemistryII
Chemistry

OthertransferasesmovephosphategroupsbetweenATPandothercompounds,
sugarresiduestoformdisaccharides,andsoon.
3.Hydrolysis.Theseenzymes,termedhydrolases,breaksinglebondsby
addingtheelementsofwater.Forexample,phosphatasesbreaktheoxygen
phosphorusbondofphosphateesters:

CliffsNotes


Otherhydrolasesfunctionasdigestiveenzymes,forexample,bybreakingthe
peptidebondsinproteins.
4.Formationorremovalofadoublebondwithgrouptransfer.The
functionalgroupstransferredbytheselyaseenzymesincludeaminogroups,water,
andammonia.Forexample,decarboxylasesremoveCO2fromalphaorbetaketo
acids:
Dehydratasesremovewater,asinfumarase(fumaratehydratase):

Deaminasesremoveammonia,forexample,intheremovalofaminogroupsfrom
aminoacids:

5.Isomerizationoffunctionalgroups.Inmanybiochemicalreactions,the
positionofafunctionalgroupischangedwithinamolecule,butthemoleculeitself
containsthesamenumberandkindofatomsthatitdidinthebeginning.Inother
words,thesubstrateandproductofthereactionareisomers.Theisomerases(for
example,triosephosphateisomerase,shownfollowing),carryoutthese
rearrangements.

6.Singlebondformationbyeliminatingtheelementsofwater.Hydrolases
breakbondsbyaddingtheelementsofwaterligasescarryouttheconverse
reaction,removingtheelementsofwaterfromtwofunctionalgroupstoforma
singlebond.SynthetasesareasubclassofligasesthatusethehydrolysisofATPto

drivethisformation.Forexample,aminoacyltransferRNAsynthetasesjoinamino
acidstotheirrespectivetransferRNAsinpreparationforproteinsynthesisthe
actionofglycyltRNAsynthetaseisillustratedinthisfigure:

TheMichaelisMentenequation
Ifanenzymeisaddedtoasolutioncontainingsubstrate,thesubstrateisconverted
toproduct,rapidlyatfirst,andthenmoreslowly,astheconcentrationofsubstrate
decreasesandtheconcentrationofproductincreases.Plotsofsubstrate(S)or
product(P)againsttime,calledprogresscurves,havetheformsshowninFigure.
Notethatthetwoprogresscurvesaresimplyinversesofeachother.Attheendof
thereaction,equilibriumisreached,nonetconversionofsubstratetoproduct
occurs,andeithercurveapproachesthehorizontal.

Figure1

Anotherwaytolookatenzymesiswithaninitialvelocityplot.Therateofreaction
isdeterminedearlyintheprogresscurveverylittleproductispresent,butthe
enzymehasgonethroughalimitednumberofcatalyticcycles.Inotherwords,the
enzymeisgoingthroughthesequenceofproductbinding,chemicalcatalysis,and
productreleasecontinually.Thisconditioniscalledthesteadystate.Forexample,

thethreecurvesinFigurerepresentprogresscurvesforanenzymeunderthree
differentreactionconditions.Inallthreecurves,theamountofenzymeisthesame
however,theconcentrationofsubstrateisleastincurve(a),greaterincurve(b),
andgreatestincurve(c).Theprogresscurvesshowthatmoreproductformsas
moresubstrateisadded.Theslopesoftheprogresscurvesatearlytime,thatis,
therateofproductformationwithtimealsoincreasewithincreasingsubstrate
concentration.Theseslopes,calledtheinitialratesorinitialvelocities,ofthe
reactionalsoincreaseasmoresubstrateispresentsothat:

Themoresubstrateispresent,thegreatertheinitialvelocity,becauseenzymesact
tobindtotheirsubstrates.Justasanyotherchemicalreactioncanbefavoredby
increasingtheconcentrationofareactant,theformationofanenzymesubstrate
complexcanbefavoredbyahigherconcentrationofsubstrate.

Figure2

Aplotoftheinitialvelocitiesversussubstrateconcentrationisahyperbola(Figure).
WhydoesthecurveinFigureflattenout?Becauseifthesubstrateconcentration
getshighenough,theenzymespendsallitstimecarryingoutcatalysisandnotime
waitingtobindsubstrate.Inotherwords,theamountofsubstrateishighenough
sothattheenzymeissaturated,andthereactionratehasreachedmaximal
velocity,orVmax.NotethattheconditionofmaximalvelocityinFigureisnotthe
sameasthestateofthermodynamicequilibuiuminFigures1and2.

Figure3

Althoughitisavelocitycurveandnotabindingcurve,Figureisahyperbola.Just
asmyoglobinissaturatedwithoxygenathighenoughpO2,soanenzymeis
saturatedwithsubstrateathighenoughsubstrateconcentration,designated[S].
TheequationdescribingtheplotinFigureissimilarinformtotheequationusedfor
O2bindingtomyoglobin:

KmistheMichaelisconstantfortheenzymebindingsubstrate.TheMichaelis
constantisanalogousto,butnotidenticalto,thebindingconstantforthesubstrate
totheenzyme.Vmaxisthemaximalvelocityavailablefromtheamountof
enzymeinthereactionmixture.Ifyouaddmoreenzymetoagivenamountof
substrate,thevelocityofthereaction(measuredinmolesofsubstrateconverted
pertime)increases,becausetheincreasedamountofenzymeusesmoresubstrate.
ThisisaccountedforbytherealizationthatVmaxdependsonthetotalamountof
enzymeinthereactionmixture:

whereEtisthetotalconcentrationoftheenzymeandkcatistherateconstantfor
thesloweststepinthereaction.
OtherconceptsfollowfromtheMichaelisMentenequation.Whenthevelocityofan
enzymaticreactionisonehalfthemaximalvelocity:
then:

because:

Inotherwords,theKmisnumericallyequaltotheamountofsubstraterequiredso
thatthevelocityofthereactionishalfofthemaximalvelocity.
Alternatively,whentheconcentrationofsubstrateinthereactionisveryhigh(V
maxconditions),then[S]>>Km,andtheKmterminthedenominatorcanbe
ignoredintheequation,giving:

Ontheotherhand,when[S]<<Km,theterm[S]inthedenominatorofthe
MichaelisMentenequationcanbeignored,andtheequationreducesto:

Inthelastcase,theenzymeissaidtobeunderfirstorderconditions,becausethe
velocitydependsdirectlyontheconcentrationofsubstrate.

Inhibitorsofenzymecatalyzedreactions
InthetermsoftheMichaelisMentenequation,inhibitorscanraiseKm,lowerV
max,orboth.Inhibitorsformthebasisofmanydrugsusedinmedicine.For

example,therapyforhighbloodpressureoftenincludesaninhibitorofthe
angiotensinconvertingenzyme,orACE.Thisenzymecleaves(hydrolyzes)
angiotensinItomakeangiotensinII.AngiotensinIIraisesbloodpressure,soACE
inhibitorsareusedtotreathighbloodpressure.Anothercaseisacetylsalicylicacid,
oraspirin.Aspirinsuccessfullytreatsinflammationbecauseitcovalentlymodifies,
andthereforeinactivates,aproteinneededtomakethesignalingmoleculethat
causesinflammation.
Theprinciplesbehindenzymeinhibitionareillustratedinthefollowingexamples.
Alkalinephosphatasecatalyzesasimplehydrolysisreaction:

Phosphateion,aproductofthereaction,alsoinhibitsitbybindingtothesame
phosphatesiteusedforbindingsubstrate.Whenphosphateisbound,theenzyme
cannotbindsubstrate,soitisinhibitedbythephosphate.Howtoovercomethe
inhibitor?Addmoresubstrate:ROPO32.Becausethesubstrateandthe
inhibitorbindtothesamesiteontheenzyme,themoresubstratethatbinds,the
lessinhibitorbinds.Whenisthemostsubstrateboundtotheenzyme?UnderVmax
conditions.Phosphateionreducesthevelocityofthealkalinephosphatereaction
withoutreducingVmax.Ifvelocitydecreases,butVmaxdoesn't,theonlyother
thingthatcanchangeisKm.RememberthatKmistheconcentrationwherev=V
max/2.BecausemoresubstrateisrequiredtoachieveVmax,Kmmustnecessarily

increase.Thistypeofinhibition,whereKmincreasesbutVmaxisunchanged,is
calledcompetitivebecausetheinhibitorandsubstratecompeteforthesamesite
ontheenzyme(theactivesite).
Othercasesofinhibitioninvolvethebindingoftheinhibitortoasiteotherthanthe
sitewheresubstratebinds.Forexample,theinhibitorcanbindtotheenzymeon
theoutsideoftheproteinandtherebyalterthetertiarystructureoftheenzymeso
thatitssubstratebindingsiteisunabletofunction.Becausesomeoftheenzymeis
madenonfunctional,addingmoresubstratecan'treversetheinhibition.Vmax,the
kineticparameterthatincludestheEtterm,isreduced.Thebindingofthe
inhibitorcanalsoaffectKmiftheenzymeinhibitorcomplexispartiallyactive.
InhibitorsthatalterbothVmaxandKmarecallednoncompetitivetherare
inhibitorsthatalterVmaxonlyaretermeduncompetitive.
Youcanvisualizetheeffectsofinhibitorsusingreciprocalplots.IftheMichaelis
Mentenequationisinverted:

Thisequationislinearandhasthesameformas:

sothataplotof1/vversus1/[S](aLineweaverBurkplot,showninFigure)has
aslopeequaltoKm/Vmaxandayinterceptequalto1/Vmax.Thexinterceptofa
LineweaverBurkplotisequalto1/Km.

Figure4

Competitiveinhibitorsdecreasethevelocityofanenzymaticreactionby
increasingtheamountofsubstraterequiredtosaturatetheenzymetherefore,they
increasetheapparentKmbutdonotaffectVmax.ALineweaverBurkplotofa

competitivelyinhibitedenzymereactionhasanincreasedslope,butitsinterceptis
unchanged.
NoncompetitiveinhibitorsbothincreasetheapparentKmandreducethe
apparentVmaxofanenzymecatalyzedreaction.Therefore,theyaffectboththe
slopeandtheyinterceptofaLineweaverBurkplot,asFiguresandshow.
Uncompetitiveinhibitors,becausetheyreduceVmaxonly,increasethereciprocalof
Vmax.Thelinesofthereciprocalplotareparallelinthiscase.

Figure5

Figure6

Covalentinhibitioninvolvesthechemicalmodificationoftheenzymesothatitis
nolongeractive.Forexample,thecompounddiisopropylfluorophosphatereactswith
manyenzymesbyaddingaphosphategrouptoanessentialserinehydroxylgroup
intheenzymes'activesites.Whenphosphorylated,theenzymeistotallyinactive.
Manyusefulpharmaceuticalcompoundsworkbycovalentmodification.Aspirinisa
covalentmodifierofenzymesinvolvedintheinflammatoryresponse.Penicillin
covalentlymodifiesenzymesrequiredforbacterialcellwallsynthesis,rendering
theminactive.Becausethecellwallisnotabletoprotectthebacterialcell,the
organismburstseasilyandiskilled.

Cliff'sNotes
DealingwiththemythofCinderella,writtenbytheGrimmbrothers,howcouldyou
analyzeitintermsofarchetypesthatCarlJungused?
DidClarenceDarrowreallycallananimalintotestifyatthefamousmonkeytrial?
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