Pengantar enzim

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    Chapter 5Enzymes, Coenzyme and

    Energy

    Biology 100

    Spring 2009

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    Energy

    All living things require energy

    Nutrientsare one sour!e o" energy,as #ell as $eing mole!ules organisms

    require to gro#, reprodu!e or repair Biochemical reactionsare the

    pro!esses used "or the "ormation,

    $rea%do#n and rearrangement o"mole!ules to provide organisms#ith energy

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    A!tivation Energy

    Activation Energyis the requiredinput o" energy to ma%e area!tion start

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    Catalyst

    A catalyst is a !hemi!al thatspeeds up the rea!tion $ut is notused up in the rea!tion

    &o#ers the a!tivation energy neededto start a rea!tion

    's not used up during the rea!tion

    's un!hanged a"ter a rea!tion

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    Enzymes

    Enzymes a!t as !atalystsEnzymes are proteins that speedup a rate o" rea!tion

    (ound in !ells throughout the $ody &o#ers a!tivation energy

    Enzymes #ill end in ase

    S)EC'('C*

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    Enzymes

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    +o# Enzymes or%

    Ea!h enzyme has a spe!i-! sizeand ./ shape

    Ea!h enzyme is going to -t #ith a

    !ertain substratemole!ule enzyme!onne!ts to

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    +o# Enzymes or%

    hen the enzyme and su$strateare !onne!ted, it is %no#n asenzyme-substrate complex

    3he binding site is #here theenzyme physi!ally atta!hes itsel"to the su$strate

    3heactive site is #here theenzyme #ill !ause a spe!i-! parto" the su$strate to !hange

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    Co"a!tors4Coenzynes

    Some enzymes need an additionalmole!ule to !arry out the pro!ess

    Cofactorsare inorgani! ions or

    organi! mole!ules that serve anenzyme helpers

    Coenzymes are organi! mole!ulesthat "un!tion as a !o"a!tor ay $e !ertain amino a!ids, nitrogenous

    $ases, and vitamins

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    Co"a!tors

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    3urnover 6um$er

    3he num$er o" mole!ules o"su$strate #ith #hi!h a singleenzyme !an rea!t at a given time

    e7 reactions/minute is %no#n asthe turnover number

    Can $e quite large !ompared to

    un!atalyzed rea!tions Can depend on the environment

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    Environment

    3emperature !an have a hugeimpa!t on turnover rate

    a higher temperate #ill in!rease the

    rate o" mole!ular motion, to a !ertaine7tent

    3oo high o" temperatures may !ausethe enzyme to !hange its shape, this

    is %no#n as denaturing, #here aprotein stru!ture is permanently!hanged

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    Environment

    !ptimum temperature is #henthe rate o" "ormation o" theenzyme/su$strate !omple7 is

    "astest

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    Environment

    p+ also a8e!ts the rate o"

    enzyme/su$strate !omple7es ost enzymes have an optimum p+

    o" around neutral +o#ever, some pre"er a!idi! or $asi!

    !onditions

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    CompetitionCompetition

    Enzymatic competition is #here thereare several %inds o" enzymes availa$leto !om$ine #ith the same %ind o"su$strate mole!ule3he su$strate a!etyl !an $e a!ted upon $y

    three di8erent enzymes: !itratesynthetase, "atty a!id synthetase, andmalate synthetase

    Fig.5.7,

    pg.103

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    ;ene

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    Fig.5.7,

    pg

    .103

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    'nhi$itor

    %nhibitor is a mole!ule thatatta!hes itsel" to an enzyme andinter"eres #ith the enzymes

    a$ility to "orm an enzyme/su$strate !omple7

    Competitive 'nhi$ition

    6egative/(eed$a!% 'nhi$ition

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    Competitive 'nhi$itionCompetitive 'nhi$ition 'n competitive inhibitionan

    inhi$itor has a shape that is !loselyresem$ling the normal su$strate o"an enzyme

    Enzyme $e!omes ine8e!tive

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    6egative/(eed$a!%6egative/(eed$a!%

    'nhi$ition'nhi$ition 'n negative-feedbac& inhibitionis apro!ess #here the output o" asystem a!ts to oppose !hanges tothe input o" the system

    Allosteric #egulation is theregulation o" an enzyme or otherprotein $y $inding an e8e!tormole!ule at the protein>s allosteri!site a site other than the a!tive site

    http:44higheredm!gra#/hill!om4ol!4dl4120004$io10s#"