Done by: Azizul, Izzah and Fatin

Enzymes are
Proteins.(Tertiary and
Quaternary)
Act as catalyst to
accelerate a reaction.
Not permanently
changed in the process.
Enzymes are specific,
will only catalyse one
particular reactions.




Enzymes work
by weakening
the bonds
which lowers
the activation
energy.


FREE
ENERGY

} ACTIVATION ENERGY

REACTANTS




PRODUCTS

REACTION PATHWAY
Without Enzyme
With Enzyme
A restricted region of
an enzyme molecule
which binds to the
substrate.
The shape and the
chemical
environment inside
the active site permits
a chemical reaction to
proceed more easily.

H.PELLETIER, M.R.SAWAYA
ProNuC Database
An additional non-
protein molecule that
is needed by some
enzymes to help the
reaction.
Tightly bound
cofactors are called
prosthetic groups
Cofactors that are
bound and released
easily are called
coenzymes
Vitamins are most
likely coenzymes.
Nitrogenase enzyme with Fe, Mo and ADP
cofactors
The substrate of an enzyme are the
reactants that are activated by the enzyme
Enzymes are specific to their substrates
The specificity is determined by the
active site

Fit between the substrate and the active site of the
enzyme is exact
Like a key fits into a lock very precisely
The key will be the enzyme and the substrate will
be the lock.
Temporary structure called the enzyme-substrate
complex formed
Products have a different shape from the substrate
Once formed, they are released from the active site
Leaving it free to become attached to another
substrate


S
E
P
P
Enzyme-
substrate
complex
1. The enzyme is surrounded by variously shaped substrate
molecules.
2. The enzyme is capable of changing the shape of the active
site slighty to accomodate for the substrate and ultimately
form an Enzyme-Substrate Complex.
3. The enzyme breaks down the substrate into smaller pieces.
4. The enzyme then releases the substrate and the active site
then returns to its original shape, ready to bind to more
substrate molecules.

The are 6 factors:
1. Temperature
2. pH
3. Enzyme Concentration
4. Substrate Concentration
5. Presence of Inhibitors
6. Presence of Cofactors
Increasing the temperature,
- double the reaction
- more collisions between particles
but only up to optimum temperature. (40

c)
As temperature increases ( >40

c), more bonds,

especially the weaker Hydrogen and Ionic bonds,
will break as a result of this strain. Breaking bonds within
the enzyme will cause the Active Site to change shape.
This change in shape means that the Active Site is less
Complementary to the shape of the Substrate, so that
it is less likely to catalyse the reaction. Eventually, the
enzyme will become Denatured and will no longer
function.










40
Extreme pH levels will produce denaturation
The structure of the enzyme is changed
The active site is distorted and the substrate
molecules will no longer fit in it
At pH values slightly different from the enzymes
optimum value, small changes in the charges of the
enzyme and its substrate molecules will occur
This change in ionisation will affect the binding of
the substrate with the active site.


Optimum pH values
pH
Enzyme
activity
A substrate that can slow down or stop an
enzyme controlled reaction they combine
with the enzyme and stop the substrate
attaching to it.
Can be reversible and non-reversible
There are two types of inhibitors:-
Competitive Inhibitors
Non-Competitive Inhibitors
Has a structure that similar to that of the
substrate and so compete with the substrate for
the active site.
As a result, it will reduce the no. of enzyme
substrate complexes and so reduce the reaction
rate.
This type of inhibition is reversible by an increase
in substrate concentration: eventually allow
substrate to bind.
So the more substrate available, the less
inhibitor will bind its active site.
Does not compete for active site.
It attached to another part of enzyme causing the
overall shape of the enzyme molecules to change.
Changes the shape of the active site so substrate can
no longer bind.
Increasing the amount of substrate will not reduce
this inhibitors since there are not in competition
for active site.
Removal of inhibitor will restore normal shape of
the enzymes.
Some inhibitors bind irreversibly to an enzyme
and so destroy its catalytic properties completely.
Usually poisonous to the cells because they close
down some part of the metabolism.
Are always non competitive inhibitors.
Other small molecules can improved the action of enzymes, sometimes
enzymes will not work without them.
These substances are called Co-factors.
Substances derived from vitamin can often act as Co-factors, in some
cases just improving the action of enzymes.
E.g: Carbonic Anhydrase.
Has an Zn
2+
as an active site.
Without them, the enzyme will not work.