Biology in Focus - Chapter 6
Transcript of Biology in Focus - Chapter 6
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CAMPBELL BIOLOGY IN FOCUS
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Urry • Cain • Wasserman • Minorsky • Jackson • Reece
Lecture Presentations by Kathleen Fitzpatrick and Nicole Tunbridge
6An Introduction to Metabolism
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Overview: The Energy of Life
The living cell is a miniature chemical factory where thousands of reactions occur
The cell extracts energy and applies energy to perform work
Some organisms even convert energy to light, as in bioluminescence
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Figure 6.1
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Concept 6.1: An organism’s metabolism transforms matter and energy
Metabolism is the totality of an organism’s chemical reactions
Metabolism is an emergent property of life that arises from interactions between molecules within the cell
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Metabolic Pathways
A metabolic pathway begins with a specific molecule and ends with a product
Each step is catalyzed by a specific enzyme
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Figure 6.UN01
Enzyme 1Startingmolecule
Enzyme 2 Enzyme 3
Reaction 1 Reaction 2 Reaction 3ProductDCBA
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Catabolic pathways release energy by breaking down complex molecules into simpler compounds
Cellular respiration, the breakdown of glucose in the presence of oxygen, is an example of a pathway of catabolism
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Anabolic pathways consume energy to build complex molecules from simpler ones
The synthesis of protein from amino acids is an example of anabolism
Bioenergetics is the study of how organisms manage their energy resources
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Forms of Energy
Energy is the capacity to cause change Energy exists in various forms, some of which can
perform work
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Kinetic energy is energy associated with motion Thermal energy is kinetic energy associated with
random movement of atoms or molecules Heat is thermal energy in transfer from one object to
another Potential energy is energy that matter possesses
because of its location or structure
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Chemical energy is potential energy available for release in a chemical reaction
Energy can be converted from one form to another
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Animation: Energy Concepts
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Figure 6.2
A diver has more potentialenergy on the platform.
A diver has less potentialenergy in the water.
Diving convertspotential energy tokinetic energy.
Climbing up converts the kineticenergy of muscle movementto potential energy.
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The Laws of Energy Transformation
Thermodynamics is the study of energy transformations
An isolated system, such as that approximated by liquid in a thermos, is isolated from its surroundings
In an open system, energy and matter can be transferred between the system and its surroundings
Organisms are open systems
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The First Law of Thermodynamics
According to the first law of thermodynamics, the energy of the universe is constant Energy can be transferred and transformed, but it
cannot be created or destroyed The first law is also called the principle of
conservation of energy
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Figure 6.3
(a) First law of thermodynamics (b) Second law of thermodynamics
Chemicalenergy
Heat
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Figure 6.3a
(a) First law of thermodynamics
Chemicalenergy
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Figure 6.3b
(b) Second law of thermodynamics
Heat
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The Second Law of Thermodynamics
During every energy transfer or transformation, some energy is unusable and is often lost as heat
According to the second law of thermodynamics Every energy transfer or transformation increases the
entropy of the universe Entropy is a measure of disorder, or randomness
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Living cells unavoidably convert organized forms of energy to heat
Spontaneous processes occur without energy input; they can happen quickly or slowly
For a process to occur without energy input, it must increase the entropy of the universe
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Biological Order and Disorder
Cells create ordered structures from less ordered materials
Organisms also replace ordered forms of matter and energy with less ordered forms
Energy flows into an ecosystem in the form of light and exits in the form of heat
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Figure 6.4
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Figure 6.4a
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Figure 6.4b
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The evolution of more complex organisms does not violate the second law of thermodynamics
Entropy (disorder) may decrease in an organism, but the universe’s total entropy increases
Organisms are islands of low entropy in an increasingly random universe
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Concept 6.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously
Biologists want to know which reactions occur spontaneously and which require input of energy
To do so, they need to determine energy changes that occur in chemical reactions
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Free-Energy Change (G), Stability, and Equilibrium
A living system’s free energy is energy that can do work when temperature and pressure are uniform, as in a living cell
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The change in free energy (∆G) during a chemical reaction is the difference between the free energy of the final state and the free energy of the initial state
∆G = Gfinal state – Ginitial state
Only processes with a negative ∆G are spontaneous Spontaneous processes can be harnessed to
perform work
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Free energy is a measure of a system’s instability, its tendency to change to a more stable state
During a spontaneous change, free energy decreases and the stability of a system increases
At equilibrium, forward and reverse reactions occur at the same rate; it is a state of maximum stability
A process is spontaneous and can perform work only when it is moving toward equilibrium
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Figure 6.5
(a) Gravitationalmotion
(c) Chemicalreaction
(b) Diffusion
• More free energy (higher G)• Less stable• Greater work capacity
• Less free energy (lower G)• More stable• Less 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
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Figure 6.5a
• More free energy (higher G)• Less stable• Greater work capacity
• Less free energy (lower G)• More stable• Less 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
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Figure 6.5b
(a) Gravitational motion
(c) Chemical reaction
(b) Diffusion
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Free Energy and Metabolism
The concept of free energy can be applied to the chemistry of life’s processes
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Exergonic and Endergonic Reactions in Metabolism
An exergonic reaction proceeds with a net release of free energy and is spontaneous; ∆G is negative
The magnitude of ∆G represents the maximum amount of work the reaction can perform
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Figure 6.6(a) Exergonic reaction: energy released, spontaneous
(b) Endergonic reaction: energy required,nonspontaneous
Amount ofenergy
released(G 0)
Amount ofenergy
required(G 0)
Reactants
ProductsEnergy
Progress of the reaction
Reactants
Products
Energy
Progress of the reaction
Free
ene
rgy
Free
ene
rgy
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Figure 6.6a
(a) Exergonic reaction: energy released, spontaneous
Amount ofenergy
released(G 0)
Reactants
ProductsEnergy
Progress of the reaction
Free
ene
rgy
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Figure 6.6b
(b) Endergonic reaction: energy required, nonspontaneous
Amount ofenergy
required(G 0)
Reactants
Products
Energy
Progress of the reaction
Free
ene
rgy
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An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous; ∆G is positive
The magnitude of ∆G is the quantity of energy required to drive the reaction
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Equilibrium and Metabolism
Reactions in a closed system eventually reach equilibrium and then do no work
Cells are not in equilibrium; they are open systems experiencing a constant flow of materials
A defining feature of life is that metabolism is never at equilibrium
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A catabolic pathway in a cell releases free energy in a series of reactions
Closed and open hydroelectric systems can serve as analogies
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Figure 6.7
(a) An isolated hydroelectric system
G 0
G 0
G 0
G 0 G 0
G 0
(c) A multistep open hydroelectric system
(b) An openhydroelectricsystem
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Figure 6.7a
(a) An isolated hydroelectric system
G 0 G 0
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Figure 6.7b
G 0 (b) An open
hydroelectric system
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Figure 6.7c
G 0 G 0
G 0
(c) A multistep open hydroelectric system
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Concept 6.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions
A cell does three main kinds of work Chemical Transport Mechanical
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To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one
Most energy coupling in cells is mediated by ATP
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The Structure and Hydrolysis of ATP
ATP (adenosine triphosphate) is composed of ribose (a sugar), adenine (a nitrogenous base), and three phosphate groups
In addition to its role in energy coupling, ATP is also used to make RNA
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Video: ATP Space-filling Model
Video: ATP Stick Model
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Figure 6.8
(a) The structure of ATP
Phosphate groups
(b) The hydrolysis of ATP
Adenine
Ribose
Energy
Adenosine triphosphate (ATP)
Adenosine diphosphate (ADP)Inorganic
phosphate
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Figure 6.8a
(a) The structure of ATP
Phosphate groups
Adenine
Ribose
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Figure 6.8b
(b) The hydrolysis of ATP
Energy
Adenosine triphosphate (ATP)
Adenosine diphosphate (ADP)Inorganic
phosphate
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The bonds between the phosphate groups of ATP can be broken by hydrolysis
Energy is released from ATP when the terminal phosphate bond is broken
This release of energy comes from the chemical change to a state of lower free energy, not from the phosphate bonds themselves
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How the Hydrolysis of ATP Performs Work
The three types of cellular work (mechanical, transport, and chemical) are powered by the hydrolysis of ATP
In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction
Overall, the coupled reactions are exergonic
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Figure 6.9
(a) Glutamic acid conversion to glutamineGlutamic acid
GGlu 3.4 kcal/mol
Glutamine
(b) Conversion reaction coupled with ATP hydrolysis
(c) Free-energy change for coupled reaction
Ammonia
Glutamic acid GlutaminePhosphorylatedintermediate
GGlu 3.4 kcal/mol
GATP −7.3 kcal/mol GGlu 3.4 kcal/mol GATP −7.3 kcal/mol
G −3.9 kcal/mol Net
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Figure 6.9a
(a) Glutamic acid conversion to glutamine
Glutamic acid
GGlu 3.4 kcal/mol
GlutamineAmmonia
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Figure 6.9b
(b) Conversion reaction coupled with ATP hydrolysis
Glutamic acid
GlutaminePhosphorylatedintermediate
Phosphorylatedintermediate
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Figure 6.9c
(c) Free-energy change for coupled reaction
GGlu 3.4 kcal/mol
GATP −7.3 kcal/mol GGlu 3.4 kcal/mol GATP −7.3 kcal/mol
G −3.9 kcal/mol Net
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ATP drives endergonic reactions by phosphorylation, transferring a phosphate group to some other molecule, such as a reactant
The recipient molecule is now called a phosphorylated intermediate
ATP hydrolysis leads to a change in a protein’s shape and often its ability to bind to another molecule
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Figure 6.10
(a) Transport work: ATP phosphorylates transport proteins.
(b) Mechanical work: ATP binds noncovalently to motor proteinsand then is hydrolyzed.
Transport protein
Solute transported
Solute
Motor protein
Vesicle Cytoskeletal track
Protein andvesicle moved
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The Regeneration of ATP
ATP is a renewable resource that is regenerated by addition of a phosphate group to adenosine diphosphate (ADP)
• The energy to phosphorylate ADP comes from catabolic reactions in the cell
• The ATP cycle is a revolving door through which energy passes during its transfer from catabolic to anabolic pathways
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Figure 6.11
Energy fromcatabolism(exergonic, energy-releasing processes)
Energy for cellularwork (endergonic, energy-consuming processes)
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Concept 6.4: Enzymes speed up metabolic reactions by lowering energy barriers
A catalyst is a chemical agent that speeds up a reaction without being consumed by the reaction
An enzyme is a catalytic protein Hydrolysis of sucrose by the enzyme sucrase is an
example of an enzyme-catalyzed reaction
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Figure 6.UN02
Sucrase
Sucrose(C12H22O11)
Fructose(C6H12O6)
Glucose(C6H12O6)
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The Activation Energy Barrier
Every chemical reaction between molecules involves bond breaking and bond forming
The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA)
Activation energy is often supplied in the form of thermal energy that the reactant molecules absorb from their surroundings
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Figure 6.12
Transition state
Reactants
Progress of the reaction
Products
G 0
Free
ene
rgy
A
A
A
B
C
D
B
B
C
D
C D
EA
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Enzymes catalyze reactions by lowering the EA barrier
Enzymes do not affect the change in free energy (∆G); instead, they hasten reactions that would occur eventually
How Enzymes Speed Up Reactions
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Animation: How Enzymes Work
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Figure 6.13
Products
G is unaffectedby enzyme
Reactants
Progress of the reaction
Free
ene
rgy
EA withenzymeis lower
EA withoutenzyme
Course of reactionwithoutenzyme
Course of reactionwith enzyme
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Substrate Specificity of Enzymes
The reactant that an enzyme acts on is called the enzyme’s substrate
The enzyme binds to its substrate, forming an enzyme-substrate complex
The active site is the region on the enzyme where the substrate binds
Enzyme specificity results from the complementary fit between the shape of its active site and the substrate shape
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Enzymes change shape due to chemical interactions with the substrate
This induced fit of the enzyme to the substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
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Video: Enzyme Induced Fit
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Figure 6.14
Enzyme-substratecomplex
Enzyme
Substrate
Active site
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Catalysis in the Enzyme’s Active Site
In an enzymatic reaction, the substrate binds to the active site of the enzyme
The active site can lower an EA barrier by Orienting substrates correctly Straining substrate bonds Providing a favorable microenvironment Covalently bonding to the substrate
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Figure 6.15-1
SubstratesEnzyme-substratecomplex
Substrates areheld in active site byweak interactions.
Substrates enteractive site.
21
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Figure 6.15-2
Substrates
Substrates areconverted toproducts.
Enzyme-substratecomplex
Substrates areheld in active site byweak interactions.
Substrates enteractive site.
3
21
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Figure 6.15-3
Substrates
Substrates areconverted toproducts.
Products arereleased.
Products
Enzyme-substratecomplex
Substrates areheld in active site byweak interactions.
Substrates enteractive site.
43
21
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Figure 6.15-4
Substrates
Enzyme
Substrates areconverted toproducts.
Products arereleased.
Products
Enzyme-substratecomplex
Substrates areheld in active site byweak interactions.
Substrates enteractive site.
Activesite is
availablefor new
substrates.
5
43
21
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Effects of Local Conditions on Enzyme Activity
An enzyme’s activity can be affected by General environmental factors, such as
temperature and pH Chemicals that specifically influence the enzyme
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Effects of Temperature and pH
Each enzyme has an optimal temperature in which it can function
Each enzyme has an optimal pH in which it can function
Optimal conditions favor the most active shape for the enzyme molecule
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Figure 6.16
Temperature (C)
Optimal temperature forenzyme of thermophilic
(heat-tolerant) bacteria (77C)
Optimal temperature fortypical human enzyme(37C)
Optimal pH for pepsin(stomach enzyme)
Optimal pH for trypsin(intestinalenzyme)
(a) Optimal temperature for two enzymes
(b) Optimal pH for two enzymespH
120100806040200
9 1086420 7531
Rat
e of
reac
tion
Rat
e of
reac
tion
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Figure 6.16a
Temperature (C)
Optimal temperature forenzyme of thermophilic
(heat-tolerant) bacteria (77C)
Optimal temperature fortypical human enzyme(37C)
(a) Optimal temperature for two enzymes
120100806040200
Rat
e of
reac
tion
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Figure 6.16b
Optimal pH for pepsin(stomach enzyme)
Optimal pH for trypsin(intestinalenzyme)
(b) Optimal pH for two enzymespH
9 1086420 7531
Rat
e of
reac
tion
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Cofactors
Cofactors are nonprotein enzyme helpers Cofactors may be inorganic (such as a metal in ionic
form) or organic An organic cofactor is called a coenzyme Coenzymes include vitamins
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Enzyme Inhibitors
Competitive inhibitors bind to the active site of an enzyme, competing with the substrate
Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective
Examples of inhibitors include toxins, poisons, pesticides, and antibiotics
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Figure 6.17
(b) Competitive inhibition (c) Noncompetitive inhibition
(a) Normal binding
Competitiveinhibitor
Noncompetitiveinhibitor
Substrate
Enzyme
Active site
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The Evolution of Enzymes
Enzymes are proteins encoded by genes Changes (mutations) in genes lead to changes in
amino acid composition of an enzyme Altered amino acids in enzymes may alter their
substrate specificity Under new environmental conditions a novel form of
an enzyme might be favored
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Concept 6.5: Regulation of enzyme activity helps control metabolism
Chemical chaos would result if a cell’s metabolic pathways were not tightly regulated
A cell does this by switching on or off the genes that encode specific enzymes or by regulating the activity of enzymes
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Allosteric Regulation of Enzymes
Allosteric regulation may either inhibit or stimulate an enzyme’s activity
Allosteric regulation occurs when a regulatory molecule binds to a protein at one site and affects the protein’s function at another site
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Allosteric Activation and Inhibition
Most allosterically regulated enzymes are made from polypeptide subunits
Each enzyme has active and inactive forms The binding of an activator stabilizes the active form
of the enzyme The binding of an inhibitor stabilizes the inactive
form of the enzyme
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Figure 6.18
(b) Cooperativity: another type of allostericactivation
(a) Allosteric activators and inhibitors
Substrate
Inactive form Stabilizedactive form
Stabilizedactive form
Active form
Active site(one of four)
Allosteric enzymewith four subunits
Regulatorysite (one of four)
Activator
Oscillation
Stabilizedinactive form
Inactiveform
InhibitorNon-functionalactive site
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Figure 6.18a (a) Allosteric activators and inhibitors
Stabilizedactive form
Active form
Active site(one of four)
Allosteric enzymewith four subunits
Regulatorysite (one of four)
Activator
Oscillation
Stabilizedinactive form
Inactiveform
InhibitorNon-functionalactive site
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Figure 6.18b
(b) Cooperativity: another type of allosteric activation
Substrate
Inactive form Stabilizedactive form
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Cooperativity is a form of allosteric regulation that can amplify enzyme activity
One substrate molecule primes an enzyme to act on additional substrate molecules more readily
Cooperativity is allosteric because binding by a substrate to one active site affects catalysis in a different active site
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Feedback Inhibition
In feedback inhibition, the end product of a metabolic pathway shuts down the pathway
Feedback inhibition prevents a cell from wasting chemical resources by synthesizing more product than is needed
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Figure 6.19Active site available
Intermediate A
End product(isoleucine)
Intermediate B
Intermediate C
Intermediate D
Enzyme 2
Enzyme 3
Enzyme 4
Enzyme 5
Feedbackinhibition
Isoleucinebinds toallostericsite.
Isoleucineused up bycell
Enzyme 1(threoninedeaminase)
Threoninein active site
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Specific Localization of Enzymes Within the Cell
Structures within the cell help bring order to metabolic pathways
Some enzymes act as structural components of membranes
In eukaryotic cells, some enzymes reside in specific organelles; for example, enzymes for cellular respiration are located in mitochondria
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Figure 6.20
Mitochondria
The matrix containsenzymes in solutionthat are involved in
one stage of cellularrespiration.
Enzymes for anotherstage of cellular
respiration areembedded in theinner membrane.
1 m
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Figure 6.20a
The matrix containsenzymes in solutionthat are involved in
one stage of cellularrespiration.
Enzymes for anotherstage of cellular
respiration areembedded in theinner membrane.
1 m
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Figure 6.UN03
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Figure 6.UN04
Products
G is unaffectedby enzyme
Reactants
Progress of the reaction
Free
ene
rgy
EA withenzymeis lower
EA
withoutenzyme
Course of reactionwithoutenzyme
Course of reactionwith enzyme