enzyme 1enzyme 2enzyme 3 d cb a reaction 1reaction 3reaction 2 starting molecule product 1
TRANSCRIPT
Enzyme 1 Enzyme 2 Enzyme 3
DCBAReaction 1 Reaction 3Reaction 2
Startingmolecule
Product
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Climbing up converts the kineticenergy of muscle movementto potential energy.
A diver has less potentialenergy in the waterthan on the platform.
Diving convertspotential energy tokinetic energy.
A diver has more potentialenergy on the platformthan in the water.
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(a) First law of thermodynamics (b) Second law of thermodynamics
Chemicalenergy
Heat CO2
H2O
+
3
(a) Gravitational motion (b) Diffusion (c) Chemical reaction
• More free energy (higher G)• Less stable• Greater work capacity
In a spontaneous change• The free energy of the system decreases (∆G < 0)• The system becomes more stable• The released free energy can be harnessed to do work
• Less free energy (lower G)• More stable• Less work capacity
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Reactants
Energy
Fre
e e
ne
rgy
Products
Amount ofenergy
released(∆G < 0)
Progress of the reaction
(a) Exergonic reaction: energy released
Products
ReactantsEnergy
Fre
e e
ne
rgy
Amount ofenergy
required(∆G > 0)
(b) Endergonic reaction: energy required
Progress of the reaction
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(a) An isolated hydroelectric system
∆G < 0 ∆G = 0
(b) An open hydroelectric system ∆G < 0
∆G < 0
∆G < 0
∆G < 0
(c) A multistep open hydroelectric system
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Phosphate groupsRibose
Adenine
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Inorganic phosphate
Energy
Adenosine triphosphate (ATP)
Adenosine diphosphate (ADP)
P P
P P P
P ++
H2O
i
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(b) Coupled with ATP hydrolysis, an exergonic reaction
Ammonia displacesthe phosphate group,forming glutamine.
(a) Endergonic reaction
(c) Overall free-energy change
PP
GluNH3
NH2
Glu i
GluADP+
PATP+
+
Glu
ATP phosphorylatesglutamic acid,making the aminoacid less stable.
GluNH3
NH2
Glu+
Glutamicacid
GlutamineAmmonia
∆G = +3.4 kcal/mol
+2
1
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(b) Mechanical work: ATP binds noncovalently to motor proteins, then is hydrolyzed
Membrane protein
P i
ADP+
P
Solute Solute transported
Pi
Vesicle Cytoskeletal track
Motor protein Protein moved
(a) Transport work: ATP phosphorylates transport proteins
ATP
ATP
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P iADP +
Energy fromcatabolism (exergonic,energy-releasingprocesses)
Energy for cellularwork (endergonic,energy-consumingprocesses)
ATP + H2O
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Sucrose (C12H22O11)
Glucose (C6H12O6) Fructose (C6H12O6)
Sucrase
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Progress of the reaction
Products
Reactants
∆G < O
Transition state
Fre
e en
erg
y EA
DC
BA
D
D
C
C
B
B
A
A
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Progress of the reaction
Products
Reactants
∆G is unaffectedby enzyme
Course ofreactionwithoutenzyme
Fre
e en
erg
y
EA
withoutenzyme EA with
enzymeis lower
Course ofreactionwith enzyme
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Substrate
Active site
Enzyme Enzyme-substratecomplex
(b)(a)
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Substrates
Enzyme
Products arereleased.
Products
Substrates areconverted toproducts.
Active site can lower EA
and speed up a reaction.
Substrates held in active site by weakinteractions, such as hydrogen bonds andionic bonds.
Substrates enter active site; enzyme changes shape such that its active siteenfolds the substrates (induced fit).
Activesite is
availablefor two new
substratemolecules.
Enzyme-substratecomplex
5
3
21
6
4
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Ra
te o
f re
ac
tio
n
Optimal temperature forenzyme of thermophilic
(heat-tolerant) bacteria
Optimal temperature fortypical human enzyme
(a) Optimal temperature for two enzymes
(b) Optimal pH for two enzymes
Ra
te o
f re
ac
tio
n
Optimal pH for pepsin(stomach enzyme)
Optimal pHfor trypsin(intestinalenzyme)
Temperature (ºC)
pH543210 6 7 8 9 10
0 20 40 80 60 100
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(a) Normal binding (c) Noncompetitive inhibition(b) Competitive inhibition
Noncompetitive inhibitor
Active siteCompetitive inhibitor
Substrate
Enzyme
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Allosteric enyzmewith four subunits
Active site(one of four)
Regulatorysite (oneof four)
Active form
Activator
Stabilized active form
Oscillation
Non-functionalactivesite
InhibitorInactive form Stabilized inactive
form
(a) Allosteric activators and inhibitors
Substrate
Inactive form Stabilized activeform
(b) Cooperativity: another type of allosteric activation
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Intermediate C
Feedbackinhibition
Isoleucineused up bycell
Enzyme 1(threoninedeaminase)
End product(isoleucine)
Enzyme 5
Intermediate D
Intermediate B
Intermediate A
Enzyme 4
Enzyme 2
Enzyme 3
Initial substrate(threonine)
Threoninein active site
Active siteavailable
Active site ofenzyme 1 nolonger bindsthreonine;pathway isswitched off.
Isoleucinebinds toallostericsite
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