Introduction to Metabolism

Metabolism is the sum of an organisms chemical

reactions

Metabolism is an emergent property of life that

arises from interactions between molecules within
the cell

A metabolic pathway begins with a specific

molecule and ends with a product
The product of one reaction is substrate of the
next
Each step is catalyzed by a specific enzyme

BIOCHEMICAL PATHWAY
VIDEO

ENZYMES THAT WORK TOGETHER IN A PATHWAY CAN

BE

Concentrated in
specific location

Covalently bound in
a complex

Soluble with
free floating
intermediates

Attached to
a membrane
in sequence

CATABOLIC PATHWAY (CATABOLISM)

Release of energy by the breakdown of
complex molecules to simpler compounds
EX: digestive enzymes break down food

ANABOLIC PATHWAY (ANABOLISM)

consumes energy to build complicated
molecules from simpler ones
EX: linking amino acids to form proteins

ENERGY = capacity to cause change

KINETIC ENERGY
energy associated with motion
HEAT (thermal energy) is kinetic energy
associated with random movement of
atoms or molecules
POTENTIAL ENERGY = energy that matter
possesses because of its location or
structure
CHEMICAL energy is potential energy
available for release in a chemical reaction

On the platform, the diver has

more potential energy.

Climbing up converts kinetic energy

of muscle movement to potential energy.

Diving converts
potential energy to
kinetic energy.

In the water, the diver has

less potential energy.

THERMODYNAMICS
= the study of energy transformations

CLOSED system
= isolated from its surroundings
OPEN system
energy + matter can be transferred between the
system and its surroundings

Organisms are open systems

The First Law of Thermodynamics

= 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

The Second Law of Thermodynamics

During every energy transfer or transformation
entropy (disorder) of the universe INCREASES
some energy is unusable, often lost as heat

First law of thermodynamics

Chemical
energy

Second law of thermodynamics

Heat
CO2

ORGANISMS are energy TRANSFORMERS! H O

2

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
(anabolic)

Free-Energy Change ( G) can help us determine

which reactions will happen spontaneously

G = change in free energy

H = change in total energy (enthalpy) change
S = entropy
T = temperature
G = H - TS
Only processes with a negative G are
spontaneous

G = H - TS

Using the following values for H,

S, and T, determine the change in
free energy and if the reaction is
spontaneous or nonspontaneous.
I) H = 40 kJ, S = 300 J/K, T = 130
K
II) H = 40 kJ, S = 300 J/K, T = 150
K
III) H = 40 kJ, S = -300 J/K, T =
13
150 K

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End Show

Exergonic and Endergonic Reactions in Metabolism

EXERGONIC reactions
(- G)
Release energy
are spontaneous

ENDERGONIC reactions
(+ G)
Absorb energy from
their surroundings
are non-spontaneous

8-1 Energy And Life

Dont miss
this!

Catabolic= Endergonic= nonspontaneous=

+G
Energy is stored in bonds
Anabolic = Exergonic= spontaneous= -G
Energy is released when we break
bonds.
15

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of 20
End Show

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
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

ATP (adenosine triphosphate) is the cells

renewable and reusable energy shuttle
ATP provides energy for cellular functions
Energy to charge ATP comes from catabolic
reactions

Adenine

Phosphate groups

Ribose

Adenosine triphosphate (ATP)

H2O

P i

Inorganic phosphate

Adenosine diphosphate (ADP)

Energy

ATP
Energy for cellular work
provided by the loss of
phosphate from ATP

Energy from catabolism

(used to charge up
ADP into ATP
ADP +

Endergonic reaction:
G is positive, reaction is not spontaneous
NH2
Glu

NH3
Ammonia

Glutamic
acid

G = +3.4 kcal/mol

Glu
Glutamine

Exergonic reaction:
G is negative, reaction is spontaneous
ATP

H2O

ADP

P i

G = 7.3 kcal/mol

Coupled reactions:
Overall G is negative;
Together, reactions are spontaneous G = 3.9 kcal/mol

P i

Motor protein

Protein moved

Mechanical work: ATP phosphorylates motor proteins

Membrane
protein
ADP
+
P i

ATP
P i

Solute transported

Solute

Transport work: ATP phosphorylates transport proteins

P
Glu

NH2
+ NH3

Reactants: Glutamic acid

and ammonia

Glu

+ P i

Product (glutamine)
made

Chemical work: ATP phosphorylates key reactants

The Activation Energy Barrier

A

Free energy

Transition state
A

EA

Reactants
A

B
G < O

Products
Progress of the reaction

Every chemical reaction between molecules involves

bond breaking and bond forming
ACTIVATION ENERGY =
amount of energy required to get chemical reaction started
Activation energy is often supplied in the form
of heat from the surroundings

Free energy animation

ITS LIKE PUSHING A

SNOWBALL UP A HILL . . .
Once you get it up there,
it can roll down by itself

CATALYST = a chemical agent that speeds up a

reaction without being consumed by the
reaction
ENZYMES = biological catalysts
Most enzymes are PROTEINS
Exception = ribozymes (RNA)

Free energy

Course of
reaction
without
enzyme

EA
without
enzyme

EA with
enzyme
is lower

Reactants
Course of
reaction
with enzyme

G is unaffected
by enzyme

Products
Progress of the reaction
ENZYMES work by LOWERING ACTIVATION ENERGY;

ENZYMES LOWER ACTIVATION ENERGY BY:

Orienting substrates correctly

Straining substrate bonds

Providing a favorable microenvironment
Enzymes change
ACTIVATION ENERGY
but NOT
energy of
REACTANTS or PRODUCTS

ENZYMES

Most are proteins

Lower activation energy
Specific
Shape determines function
Re-usable
Unchanged by reaction

 The REACTANT that an enzyme acts on

= SUBSTRATE
Enzyme + substrate =
ENZYME-SUBSTRATE COMPLEX
Region on the enzyme where the substrate binds
= ACTIVE SITE
Substrate held in active site by WEAK interactions
(ie. hydrogen and ionic bonds)

TWO MODELS PROPOSED

LOCK & KEY

Active site on enzyme
fits substrate exactly
INDUCED FIT
Binding of substrate causes change
in active site so it fits substrate
more closely

Enzyme Activity can be affected by:

General environmental factors, such as
temperature, pH, salt concentration,
etc.
Chemicals that specifically influence the
enzyme
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Choose narrated

TEMPERATURE & ENZYME ACTIVITY

Each enzyme has an optimal temperature at
which it can function (Usually near body temp)

Increasing temperature increases the rate of an

enzyme-catalyzed reaction up to a point.
Above a certain temperature, activity begins to
decline because the enzyme begins to denature.

pH and ENZYME ACTIVITY

Each enzyme has an optimal pH at which it can

function

COFACTORS
= non-protein enzyme helpers
EX: Zinc, iron, copper

COENZYMES
= organic enzyme helpers
Ex: vitamins

REGULATION OF ENZYME PATHWAYS

GENE REGULATION
cell switches on or off the genes that code for specific
enzymes

REGULATION OF ENZYME PATHWAYS

FEEDBACK INHIBITION
end product of a pathway interacts with and
turns off an enzyme earlier in pathway

FEEDBACK INHIBITION

prevents a cell from wasting chemical resources by

synthesizing more product than is needed

NEGATIVE FEEDBACK
An accumulation of an end product slows the process that produces
that product

Negative
feedback

Enzyme 1
B

A
Enzyme 1
B

Enzyme 2
C

C
Enzyme 3

D
D

D
D

D
D

D
D

Example: sugar breakdown generates ATP; excess ATP

inhibits an enzyme near the beginning of the pathway

POSITIVE FEEDBACK (less common)

The end product speeds up production
W

W
Enzyme 4

Enzyme 4
Positive
feedback

Enzyme 5

Enzyme 5

Y
Enzyme 6

Enzyme 6
Z

Z
Z
Z

Z
Z

Z
Z

Z
Z

Z
Z

EXAMPLE: Chemicals released by platelets that accumulate

at injury site, attract MORE platelets to the site.

Z
Z

REGULATION OF ENZYME ACTIVITY

ALLOSTERIC REGULATION
proteins function at one site is affected by binding of a
regulatory molecule at another site
Allosteric regulation can inhibit or stimulate an enzymes
activity

Allosteric enzyme
inhibition

SOME ALLOSTERIC ENZYMES HAVE MULTIPLE SUBUNITS

Each enzyme has active and inactive forms

The binding of an
ACTIVATOR stabilizes
the active form

The binding of an
INHIBITOR stabilizes
the inactive form

Binding of one substrate molecule to

active site of one subunit locks all
subunits in active conformation.

Substrate

Inactive form

Stabilized active form

COOPERATIVITY another type of allosteric activation

COOPERATIVITY
= form of allosteric regulation that can amplify
enzyme activity
Binding of one substrate to active site of one
subunit locks all subunits in active conformation

Enzyme Inhibitors

COMPETITIVE inhibitor
REVERSIBLE; Mimics substrate and
competes with substrate for active site on
enzyme

Enzyme Inhibitors
NONCOMPETITIVE inhibitors bind to another part of an
enzyme, causing the enzyme to change shape and
making the active site less effective