You are on page 1of 36

Chapter 8: Metabolism

Flow of energy through life
• Life is built on chemical reactions
– transforming energy from one form to another

sun
Metabolism
• Chemical reactions of life
– forming bonds between molecules


– breaking bonds between molecules



Metabolic pathways

A→ B→ C→ D→ E→ F→ G



enzyme enzyme enzyme enzyme enzyme enzyme
2 3 4 5 6
1

• Series of enzyme-catalyzed
steps from starting molecule to
product
– Anabolic pathways

– Catabolic pathways

Forms of Energy

• Potential
– Gravity
– Chemical
(bonds)
• Kinetic
– Heat
– Light
1st and 2nd Law of Thermodynamics
• Conservation of Energy
• Every energy transfer increases entropy
(disorder) of the universe – Some energy is
unusable
– Transfers that increase entropy occur
spontaneously
Free Energy Change (ΔG)
Free energy – amount of energy a system has that is available to do work
Chemical Reactions and Energy
• Exergonic reactions
release energy
– digesting polymers
– hydrolysis =
catabolism
• Endergonic reactions
need input of energy
– building polymers
– dehydration synthesis
= anabolism
Organisms are Open
Systems
What drives reactions?
• If reactions are “downhill”, why don’t they just
happen spontaneously?

starc
h
Activation energy
• Even exergonic reactions require an initial input of energy
– activation energy
– large biomolecules
are stable
– must absorb energy
to break bonds
Enzymes Lower Activation Energy.
Catalyst: ___________________________________
Enzymes
• Biological catalysts


• increase rate of reaction without being consumed
• reduce activation energy
• don’t change free energy (∆ G) released or required
– required for most biological reactions

• thousands of different enzymes in cells
– control reactions
of life
Enzyme vocabulary
substrate
• reactant which binds to enzyme
• enzyme-substrate complex: temporary association
active site
• enzyme’s catalytic site; substrate fits into active site
product
• end result of reaction
Naming conventions

• Enzymes named for
reaction they
catalyze
– sucrase breaks down
________________
– lipases break
down
_____________
– DNA polymerase
_________________
Enzymes Lower Activation
Energy. How?
• Variety of mechanisms
– synthesis
• active site orients substrates in correct position for
reaction
– ____________________________________________
– digestion
• active site binds substrate & puts stress on bonds
that must be broken, ________________________
_________________________________________
Induced fit/Lock and key
• 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
• __________________________
• bring chemical groups in position to catalyze reaction
Factors Affecting Enzyme Function

• Enzyme concentration
• Substrate
concentration
• Temperature
• pH
• Salinity
• Activators
• Inhibitors
Factors affecting enzyme function
• Substrate concentration
– more substrate = more frequently collide with
enzyme = ↑ reaction rate
– reaction rate levels off
• all enzymes have active site engaged
• enzyme is saturated
reaction rate

substrate concentration
Temperature
What’s
happening here?!
reaction rate

37°
temperature
Factors affecting enzyme function
• Temperature
– Optimum T°
• greatest number of _______________
• human enzymes = 35°- 40°C
– body temp = 37°C _____________
– Heat: increase beyond optimum T°
• increased energy of molecules disrupts bonds in enzyme &
between enzyme & substrate
– H, ionic = weak bonds
• denaturation = ___________________________
Compounds that help enzymes
• Activators Fe in
– cofactors hemoglobi
• non-protein, small _______________compounds n
&
ions
– Mg, K, Ca, Zn, Fe, Cu (trace elements, minerals
in nutrition)
– bound to enzyme. Required for proper function
– coenzymes
• non-protein, _________________cofactors
– bind near active site
– Participate in reaction
• many _________________
– NAD (niacin; B3) Mg in
– FAD (riboflavin; B2) chlorophyl
– Coenzyme A l
– Also ATP
Regulation of
Enzyme Activity

• Enzyme Inhibitors
– molecules that reduce
enzyme activity
– competitive inhibition
– noncompetitive
inhibition
– irreversible inhibition
– feedback inhibition
Regulation of Enzyme Activity -
Competitive Inhibitors
• Inhibitor & substrate “compete” for active site
– __________________blocks enzyme bacteria use
to build cell walls
– disulfiram (___________)
treats chronic alcoholism
• blocks enzyme that
breaks down alcohol
• severe hangover & vomiting
5-10 minutes after drinking
• Overcome by increasing substrate
concentration
Regulation of Enzyme Activity -
Non-Competitive Inhibitors
• Inhibitor binds to site other than active site
– __________________ binds to allosteric site
– causes _______________________ in enzyme
• keeps enzyme inactive
– some __________________ drugs
inhibit enzymes involved in DNA synthesis
• stop division of more cancer cells
– ______________________________
irreversible inhibitor of Cytochrome C,
an enzyme in cellular respiration
• stops production of ATP
Regulation of
Enzyme Activity -
Control of Metabolism
____________________
• Conformational changes by
regulatory molecules
– inhibitors
• keeps enzyme in inactive
form
– activators
• keeps enzyme in active
form
Regulation of Enzyme Activity -
Control of Metabolism
Allosteric Regulation – Cooperativity
• Substrate acts as an activator
– substrate causes conformational
change in enzyme
• _________________________
– favors binding of substrate at 2nd site
– makes enzyme more effective

Hemoglobin
 4 polypeptide chains
 can bind 4 O2;
 1st O2 binds
 now easier for other
3 O2 to bind
Feedback Inhibition
• Regulation & coordination of production
– product is used by next step in pathway
– final product is inhibitor of earlier step
• allosteric inhibitor of _____________________
– no unnecessary accumulation of product

A →B →C →D →E →F →G


X enzyme
enzyme
2
enzyme enzyme enzyme enzyme
4 5 6
1 3

allosteric inhibitor of enzyme 1
Feedback inhibition threonine

• Example
– synthesis of amino acid,
isoleucine from threonine
– isoleucine becomes the
allosteric inhibitor of the
first step in the pathway

isoleucine
ATP – Cellular Energy
• Organisms/cells are
endergonic systems
• must have energy for
– Mechanical work
– Transport work Ribose, Adenine, 3 phosphates
– Chemical work
ATP – Cellular Energy
• Adenosine tri
phosphate - - -
– 3 phosphate groups
covalently bonded
– Can be removed by
hydrolysis
– High energy bonds
• Negative phosphates
repel one another,
easy to remove

Instability of its P bonds makes ATP an excellent energy donor
ATP = Energy…. How?
• Work of life is done by __________________
– use exergonic (catabolic) reactions to fuel
endergonic (anabolic) reactions

digestio
n
+ + energy

synthesi
s
+ + energy
ATP – Energy Coupling
How does ATP transfer energy?

O– O– O– O– 7.3

O P –O– P –O– P O– –
O P O– + energy
ATP
ADP O O O O

• ATP → ADP
– releases energy
• ∆G = -7.3 kcal/mole
• Fuel other reactions
• ____________________
– released Pi can transfer to other molecules
• destabilizing the other molecules
– enzyme that phosphorylates = “kinase”
An example of Phosphorylation…
• Building polymers from monomers
H H
– need to destabilize the monomers C C
OHHO
– phosphorylate! enzyme

H H synthesi
H H
s
C + C
+4.2 kcal/mol
C C + H2O
OH HO O

H “kinase” H
+ ADP
enzyme
C
OH
+ ATP -7.3 kcal/mol
C
P
H H H H
C
+ C C C + Pi
P HO -3.1 kcal/mol O
ATP – Drives Cellular Work

• Phosphorylation
– makes
molecule less
stable, more
likely to react
– Conformation
al change
ATP / ADP cycle
Cells can’t store ATP ATP
 good energy donor, cellular 7.3
not good energy storage respiration kcal/mole
 ______________________
 ______________________
 carbohydrates & fats are ADP + Pi
long term energy storage
A working muscle recycles over
10 million ATPs per second