2007-2008 Metabolism & Enzymes Adapted from explorebiology.con.
Chapter 8 Metabolism & Enzymes From food webs to the life of a cell energy.
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Transcript of Chapter 8 Metabolism & Enzymes From food webs to the life of a cell energy.
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Chapter 8Metabolism & Enzymes
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From food webs to the life of a cell
energy
energy
energy
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Flow of energy through life• Life is built on chemical reactions
– transforming energy from one form to another
organic molecules ATP & organic molecules
organic molecules ATP & organic molecules
sun
solar energy ATP & organic molecules
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Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the
laws of thermodynamics
• 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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Enzyme 1
A B
Reaction 1
Enzyme 2
C
Reaction 2
Enzyme 3
D
Reaction 3
ProductStarting
molecule
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Metabolism• Chemical reactions of life
– forming bonds between molecules• dehydration synthesis• synthesis• anabolic reactions
– breaking bonds between molecules• hydrolysis• digestion• catabolic reactions
That’s why they’re called
anabolic steroids!
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Examples • dehydration synthesis (synthesis)
• hydrolysis (digestion)
+
H2O
+
H2O
enzyme
enzyme
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Examples • dehydration synthesis (synthesis)
• hydrolysis (digestion)
enzyme
enzyme
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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– Kinetic energy is energy associated with motion
• Heat (thermal energy) is kinetic energy associated with random movement of atoms or molecules
– Potential energy is energy that matter possesses because of its location or structure
• 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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On the platform,the diver hasmore potentialenergy.
Diving convertspotentialenergy to kinetic energy.
Climbing up convertskinetic energy ofmuscle movement topotential energy.
In the water, the diver has lesspotential energy.
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The Laws of Energy Transformation
• Thermodynamics is the study of energy transformations
• A closed 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– Energy cannot be created or destroyed
• The first law is also called the principle of conservation of energy
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The Second Law of Thermodynamics
• During every energy transfer or transformation, some energy is unusable, often lost as heat
• According to the second law of thermodynamics, every energy transfer or transformation increases the entropy (disorder) of the universe
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LE 8-3
Chemical energy
Heat CO2
First law of thermodynamics Second law of thermodynamics
H2O
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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
• 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
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Concept 8.2: The free-energy change of a reaction tells us whether 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
• 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 process is related to the change in enthalpy, or change in total energy (∆H), and change in entropy (T∆S):
∆G = ∆H - T∆S• Only processes with a negative ∆G are
spontaneous• Spontaneous processes can be harnessed to
perform work
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Free Energy, Stability, and Equilibrium
• 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
• Equilibrium 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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LE 8-5
Gravitational motion Diffusion Chemical reaction
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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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Chemical reactions & energy• Some chemical reactions release energy
– exergonic– digesting polymers– hydrolysis = catabolism
• Some chemical reactions require input of energy– endergonic– building polymers – dehydration synthesis = anabolism
digesting molecules= less organization=lower energy state
building molecules= more organization=higher energy state
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Endergonic vs. exergonic reactionsexergonic endergonic
- energy released- digestion
- energy invested- synthesis
-G
G = change in free energy = ability to do work
+G
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Energy & life• Organisms require energy to live
– where does that energy come from?
• coupling exergonic reactions (releasing energy) with
endergonic reactions (needing energy)
+ + energy
+ energy+
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What drives reactions?• If reactions are “downhill”, why don’t they
just happen spontaneously?– because covalent bonds are stable bonds
Stable polymersdon’t spontaneously
digest into theirmonomers
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Activation energy
• Breaking down large molecules requires an initial input of energy– activation energy
– large biomolecules are stable
– must absorb energy to break bonds
energycellulose CO2 + H2O + heat
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Too much activation energy for life
• The amount of energy needed to destabilize the bonds of a molecule– moves the reaction over an “energy hill”
Not a match!That’s too much energy to expose
living cells to!
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Reducing Activation energy• Catalysts
– reducing the amount of energy to start a reaction
Pheeew…that takes a lot
less energy!
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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 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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Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic
reactions
• A cell does three main kinds of work:– Mechanical– Transport– Chemical
• To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one
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The Structure and Hydrolysis of ATP
• ATP (adenosine triphosphate) is the cell’s energy shuttle
• ATP provides energy for cellular functions
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LE 8-8
Phosphate groups
Ribose
Adenine
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• The bonds between the phosphate groups of ATP’s tail 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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LE 8-9
Adenosine triphosphate (ATP)
Energy
P P P
PPP i
Adenosine diphosphate (ADP)Inorganic phosphate
H2O
+ +
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• 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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LE 8-10
Endergonic reaction: G is positive, reactionis not spontaneous
Exergonic reaction: G is negative, reactionis spontaneous
G = +3.4 kcal/mol
G = –7.3 kcal/mol
G = –3.9 kcal/mol
NH2
NH3Glu Glu
Glutamicacid
Coupled reactions: Overall G is negative;together, reactions are spontaneous
Ammonia Glutamine
ATP H2O ADP P i
+
+ +
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How ATP Performs Work• ATP drives endergonic reactions by
phosphorylation, transferring a phosphate group to some other molecule, such as a reactant
• The recipient molecule is now phosphorylated• The three types of cellular work (mechanical,
transport, and chemical) are powered by the hydrolysis of ATP
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LE 8-11
NH2
Glu
P i
P i
P i
P i
Glu NH3
P
P
P
ATPADP
Motor protein
Mechanical work: ATP phosphorylates motor proteins
Protein moved
Membraneprotein
Solute
Transport work: ATP phosphorylates transport proteins
Solute transported
Chemical work: ATP phosphorylates key reactants
Reactants: Glutamic acidand ammonia
Product (glutamine)made
+ +
+
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The Regeneration of ATP• ATP is a renewable resource that is
regenerated by addition of a phosphate group to ADP
• The energy to phosphorylate ADP comes from catabolic reactions in the cell
• The chemical potential energy temporarily stored in ATP drives most cellular work
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LE 8-12
Pi
ADP
Energy for cellular work
(endergonic, energy-
consuming processes)
Energy from catabolism
(energonic, energy-
yielding processes)
ATP
+
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Concept 8.4: 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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LE 8-13
SucroseC12H22O11
GlucoseC6H12O6
FructoseC6H12O6
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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 heat from the surroundings
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LE 8-14
Transition state
C D
A B
EA
Products
C D
A B
G < O
Progress of the reaction
Reactants
C D
A B
Fre
e en
erg
y
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How Enzymes Lower the EA Barrier
• 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
Animation: How Enzymes Work
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LE 8-15
Course ofreactionwithoutenzyme
EA
without enzyme
G is unaffectedby enzyme
Progress of the reaction
Fre
e en
erg
y
EA withenzymeis lower
Course ofreactionwith enzyme
Reactants
Products
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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
• Induced fit of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
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LE 8-16
Substrate
Active site
Enzyme Enzyme-substratecomplex
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Catalysis in the Enzyme’s Active Site
• In an enzymatic reaction, the substrate binds to the active site
• 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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LE 8-17
Enzyme-substratecomplex
Substrates
Enzyme
Products
Substrates enter active site; enzymechanges shape so its active siteembraces the substrates (induced fit).
Substrates held inactive site by weakinteractions, such ashydrogen bonds andionic bonds.
Active site (and R groups ofits amino acids) can lower EA
and speed up a reaction by• acting as a template for substrate orientation,• stressing the substrates and stabilizing the transition state,• providing a favorable microenvironment,• participating directly in the catalytic reaction.
Substrates areconverted intoproducts.
Products arereleased.
Activesite is
availablefor two new
substratemolecules.
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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
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LE 8-18
Optimal temperature fortypical human enzyme
Optimal temperature forenzyme of thermophilic (heat-tolerant bacteria)
Temperature (°C)
Optimal temperature for two enzymes
0 20 40 60 80 100
Ra
te o
f re
ac
tio
n
Optimal pH for pepsin(stomach enzyme)
Optimal pHfor trypsin(intestinalenzyme)
pH
Optimal pH for two enzymes
0
Ra
te o
f re
ac
tio
n
1 2 3 4 5 6 7 8 9 10
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Cofactors
• Cofactors are nonprotein enzyme helpers
• Coenzymes are organic cofactors
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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
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LE 8-19Substrate
Active site
Enzyme
Competitiveinhibitor
Normal binding
Competitive inhibition
Noncompetitive inhibitor
Noncompetitive inhibition
A substrate canbind normally to the
active site of anenzyme.
A competitiveinhibitor mimics the
substrate, competingfor the active site.
A noncompetitiveinhibitor binds to the
enzyme away from theactive site, altering the
conformation of theenzyme so that its
active site no longerfunctions.
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Concept 8.5: Regulation of enzyme activity helps control metabolism
• Chemical chaos would result if a cell’s metabolic pathways were not tightly regulated
• To regulate metabolic pathways, the cell switches on or off the genes that encode specific enzymes
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Allosteric Regulation of Enzymes
• Allosteric regulation is the term used to describe cases where a protein’s function at one site is affected by binding of a regulatory molecule at another site
• Allosteric regulation may either inhibit or stimulate an enzyme’s activity
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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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LE 8-20a
Allosteric enzymewith four subunits
Regulatorysite (oneof four) Active form
Activator
Stabilized active form
Active site(one of four)
Allosteric activatorstabilizes active form.
Non-functionalactive site
Inactive formInhibitor
Stabilized inactive form
Allosteric inhibitorstabilizes inactive form.
Oscillation
Allosteric activators and inhibitors
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• Cooperativity is a form of allosteric regulation that can amplify enzyme activity
• In cooperativity, binding by a substrate to one active site stabilizes favorable conformational changes at all other subunits
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LE 8-20b
Substrate
Binding of one substrate molecule toactive site of one subunit locks allsubunits in active conformation.
Cooperativity another type of allosteric activation
Stabilized active formInactive form
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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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LE 8-21
Active siteavailable
Initial substrate(threonine)
Threoninein active site
Enzyme 1(threoninedeaminase)
Enzyme 2
Intermediate A
Isoleucineused up bycell
Feedbackinhibition Active site of
enzyme 1 can’tbindtheoninepathway off
Isoleucinebinds toallostericsite
Enzyme 3
Intermediate B
Enzyme 4
Intermediate C
Enzyme 5
Intermediate D
End product(isoleucine)
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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
• Some enzymes reside in specific organelles, such as enzymes for cellular respiration being located in mitochondria
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LE 8-22
Mitochondria,sites of cellular respiration
1 µm
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Catalysts
• So what’s a cell got to do to reduce activation energy?– get help! … chemical help…
ENZYMES
G
Call in the ENZYMES!
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Enzymes • Biological catalysts
– proteins (& RNA) – facilitate chemical reactions
• increase rate of reaction without being consumed• reduce activation energy• don’t change free energy (G) released or required
– required for most biological reactions– highly specific
• thousands of different enzymes in cells
– control reactionsof life
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Enzymes vocabularysubstrate
• reactant which binds to enzyme• enzyme-substrate complex: temporary association
product • end result of reaction
active site • enzyme’s catalytic site; substrate fits into active site
substrate
enzyme
productsactive site
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Properties of enzymes• Reaction specific
– each enzyme works with a specific substrate • chemical fit between active site & substrate
– H bonds & ionic bonds
• Not consumed in reaction– single enzyme molecule can catalyze thousands
or more reactions per second• enzymes unaffected by the reaction
• Affected by cellular conditions– any condition that affects protein structure
• temperature, pH, salinity
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Naming conventions• Enzymes named for reaction they catalyze
– sucrase breaks down sucrose
– proteases break down proteins
– lipases break down lipids
– DNA polymerase builds DNA• adds nucleotides
to DNA strand
– pepsin breaks down proteins (polypeptides)
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Lock and Key model• Simplistic model of
enzyme action– substrate fits into 3-D
structure of enzyme’ active site
• H bonds between substrate & enzyme
– like “key fits into lock”
Size doesn’t matter…Shape matters!
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Induced fit model• More accurate model of enzyme action
– 3-D structure of enzyme fits substrate– substrate binding cause enzyme to change
shape leading to a tighter fit • “conformational change”• bring chemical groups in position to catalyze
reaction
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How does it work?• Variety of mechanisms to lower
activation energy & speed up reaction– synthesis
• active site orients substrates in correct position for reaction
– enzyme brings substrate closer together
– diegstion• active site binds substrate & puts stress on
bonds that must be broken, making it easier to separate molecules
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Got any Questions?!
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Factors that Affect Enzymes
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Factors Affecting Enzyme Function• Enzyme concentration
• Substrate concentration• Temperature • pH• Salinity• Activators• Inhibitors
catalase
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Enzyme concentration
enzyme concentration
reac
tio
n r
ate
What’shappening here?!
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Factors affecting enzyme function
• Enzyme concentration – as enzyme = reaction rate
• more enzymes = more frequently collide with substrate
– reaction rate levels off• substrate becomes limiting factor• not all enzyme molecules can find substrate
enzyme concentration
reac
tio
n r
ate
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Substrate concentration
substrate concentration
reac
tio
n r
ate
What’shappening here?!
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Factors affecting enzyme function
substrate concentration
reac
tio
n r
ate
• Substrate concentration – as substrate = reaction rate
• more substrate = more frequently collide with enzyme
– reaction rate levels off• all enzymes have active site engaged• enzyme is saturated• maximum rate of reaction
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37°
Temperature
temperature
reac
tio
n r
ate
What’shappening here?!
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Factors affecting enzyme function
• Temperature– Optimum T°
• greatest number of molecular collisions• human enzymes = 35°- 40°C
– body temp = 37°C
– Heat: increase beyond optimum T°• increased energy level of molecules disrupts bonds in
enzyme & between enzyme & substrate– H, ionic = weak bonds
• denaturation = lose 3D shape (3° structure)– Cold: decrease T°
• molecules move slower • decrease collisions between enzyme & substrate
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Enzymes and temperature
• Different enzymes function in different organisms in different environments
37°Ctemperature
reac
tio
n r
ate
70°C
human enzymehot spring
bacteria enzyme
(158°F)
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How do ectotherms do it?
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7
pH
pH
reac
tio
n r
ate
20 1 3 4 5 6 8 9 10
pepsin trypsin
What’shappening here?!
11 12 13 14
pepsin
trypsin
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Factors affecting enzyme function• pH
– changes in pH• adds or remove H+
• disrupts bonds, disrupts 3D shape – disrupts attractions between charged amino acids – affect 2° & 3° structure– denatures protein
– optimal pH?• most human enzymes = pH 6-8
– depends on localized conditions– pepsin (stomach) = pH 2-3– trypsin (small intestines) = pH 8
720 1 3 4 5 6 8 9 10 11
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Salinity
salt concentration
reac
tio
n r
ate
What’shappening here?!
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Factors affecting enzyme function• Salt concentration
– changes in salinity• adds or removes cations (+) & anions (–)• disrupts bonds, disrupts 3D shape
– disrupts attractions between charged amino acids – affect 2° & 3° structure– denatures protein
– enzymes intolerant of extreme salinity• Dead Sea is called dead for a reason!
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Compounds which help enzymes
• Activators– cofactors
• non-protein, small inorganic compounds & ions– Mg, K, Ca, Zn, Fe, Cu– bound within enzyme molecule
– coenzymes• non-protein, organic molecules
– bind temporarily or permanently toenzyme near active site
• many vitamins– NAD (niacin; B3)– FAD (riboflavin; B2)– Coenzyme A
Mg inchlorophyll
Fe inhemoglobin
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Compounds which regulate enzymes• Inhibitors
– molecules that reduce enzyme activity– competitive inhibition– noncompetitive inhibition– irreversible inhibition– feedback inhibition
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Competitive Inhibitor • Inhibitor & substrate “compete” for active site
– penicillin blocks enzyme bacteria use to build cell walls
– disulfiram (Antabuse)treats chronic alcoholism
• blocks enzyme that breaks down alcohol
• severe hangover & vomiting5-10 minutes after drinking
• Overcome by increasing substrate concentration– saturate solution with substrate
so it out-competes inhibitor for active site on enzyme
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Non-Competitive Inhibitor • Inhibitor binds to site other than active site
– allosteric inhibitor binds to allosteric site – causes enzyme to change shape
• conformational change• active site is no longer functional binding site
– keeps enzyme inactive
– some anti-cancer drugsinhibit enzymes involved in DNA synthesis
• stop DNA production
• stop division of more cancer cells
– cyanide poisoningirreversible inhibitor of Cytochrome C, an enzyme in cellular respiration
• stops production of ATP
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Irreversible inhibition• Inhibitor permanently binds to enzyme
– competitor• permanently binds to active site
– allosteric• permanently binds to allosteric site • permanently changes shape of enzyme• nerve gas, sarin, many insecticides (malathion,
parathion…)– cholinesterase inhibitors
» doesn’t breakdown the neurotransmitter, acetylcholine
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Allosteric regulation• Conformational changes by regulatory
molecules – inhibitors
• keeps enzyme in inactive form
– activators • keeps enzyme in active form
Conformational changes Allosteric regulation
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Metabolic pathways
A B C D E F G enzyme
1
enzyme
2
enzyme3
enzyme4
enzyme5
enzyme6
• Chemical reactions of life are organized in pathways– divide chemical reaction into
many small steps• artifact of evolution efficiency
– intermediate branching points control = regulation
A B C D E F G enzyme
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Efficiency• Organized groups of enzymes
– enzymes are embedded in membrane and arranged sequentially
• Link endergonic & exergonic reactionsWhoa!
All that going onin those littlemitochondria!
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allosteric inhibitor of enzyme 1
Feedback Inhibition• Regulation & coordination of production
– product is used by next step in pathway– final product is inhibitor of earlier step
• allosteric inhibitor of earlier enzyme• feedback inhibition
– no unnecessary accumulation of product
A B C D E F G enzyme
1
enzyme2
enzyme3
enzyme4
enzyme
5
enzyme6
X
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Feedback inhibition• Example
– synthesis of amino acid, isoleucine from amino acid, threonine
– isoleucine becomes the allosteric inhibitor of the first step in the pathway
• as product accumulates it collides with enzyme more often than substrate does
threonine
isoleucine
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Don’t be inhibited! Ask Questions!
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Cooperativity
• Substrate acts as an activator– substrate causes conformational
change in enzyme• induced fit
– favors binding of substrate at 2nd site– makes enzyme more active & effective
• hemoglobinHemoglobin 4 polypeptide chains can bind 4 O2; 1st O2 binds now easier for other
3 O2 to bind