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 • ANABOLIC PATHWAYS
– Release energy – Consume energy
– Breaking down – Build up a complex
complex molecules to molecules from simpler
simpler compounds. 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 a
• Catalyst
reaction without being permanently
changed in the process, so it can be
used over and over.
• Enzymes • 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
 ES
E S Enzyme- E P
Enzyme + Substrate substrate Enzyme + Product
complex
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