CHAPTER 5

INTRODUCTION
TO METABOLISME

Learning goals :
Define energy and the underlying
organization of life
Explain cellular works
Describe enzymes structure and
functions
Explain factors influencing enzymes
activity

The Energy of life :

Laws of thermodynamics : I and II .

METABOLISME : an emergent property of life

that arises from orderly interactions between
molecules.
Two metabolic pathways :
CATABOLIC
PATHWAYS
Release energy
Breaking down
complex molecules to
simpler compounds.

ANABOLIC PATHWAYS
Consume energy
Build up a complex
molecules from
simpler elements.

Energy Conversion :
Exergonic
Reaction :
Chemical products
have less free
energy than the
reactant molecules.
Reaction is
energetically
downhill.
Spontaneous
reaction

Endergonic
Reaction
Products store more
free energy than
reactants.
Reaction is
energetically uphill.
Non-spontaneous
reaction ( requires
energy input)

The energy profile of a reaction

In order to make these molecules

reactive when necessary, cells use
biological catalysts :

Named ENZYMEs which are :

Proteins
Lower activation energy
Speed up reaction without
change their nature
Very selective for which
reaction they will catalyze.

The Mechanism of enzyme reaction

LEKeS

Important Terms :

Chemical agent that accelerates

Catalyst
a reaction without being
permanently changed in the
process, so it can be used over
Enzymes and over.
Biological catalysts.
Substrate
The substance an enzyme acts on
and makes more reactive.
Active Site
Restricted region of an enzyme
molecule which binds to the
substrate.

 Lock and key hypothesis

Active
site

E
Enzym
e

S
+ Substra
te

ES
Enzymesubstrate
complex

E
Enzym
e

P
+ Produc
t

Factors affecting enzyme activity

E. Cofactors
A small non protein molecules that are
required for proper enzyme catalysis.
Some are inorganic (zinc, iron or
copper)
Some are organic and are called
coenzymes (mostly vitamins)
They may bind tightly to active site or
bind loosely to both active site and
substrate.

F. Enzyme Inhibition

G. Allosteric Regulation
Allosteric site is a specific receptor site on
some part of enzyme molecule other than
the active site.
Binding of an activator to an allosteric site
stabilizes the active conformation.
Binding of an inhibitor (noncompetitive) will
stabilizes the inactive conformation.
Subunits may interact so that a single
activator or inhibitor at one allosteric site
will affect the active sites of the other
subunits.

H. Cooperativity
Substrate molecules themselves may
enhance enzyme activity.
Cooperativity is the phenomenon
where substrate binding to the active
site of one subunit induces a
conformational change that
enhances substrate binding at the
active sites of the other subunits.

1. Enzyme is not destroyed by the reactions its catalyse 2. Enzyme are highly specific.
Lock and key hypothesis

Lipase is used in the ripening of cheese