They catalyse metabolic reaction. Active site
has a specific shape determined by the
tertiary structure.
They can be
extracellular
or intracellular
Activation energy
Enzymes reduce the activation energy by allowing
the reaction to occur at a lower temperature. This
speeds up the reaction. An ESC forms. The
enzyme reduces the repulsion of the molecules so
they can bonds more easily. The enzymes put
strain on the bonds so it break more easily
Models
Lock and key changed
into the induced fit to
show that the ESC
changed shape slightly to
fit better
Factors affecting enzymes
Temperature: Higher temperature means
more kinetic energy and more successful
collisions resulting in more ESC. Too high
a temperature causes the enzymes to
denature as the bonds break
pH: The H+ and OH- ions
disrupt the bonds in the
tertiary structure and denature
at high and low pH's
Enzyme concentration: The more enzyme
molecules increases the ESC but a limited supply
of substrate results in to further effect
Substrate concentration: The more substrate
there is the higher ESC. Until saturation where
all active sites are occupied when more
substrate has no further effect
Inhibition/cofactors
Cofactors
Coenzymes are small
organic non proteins
molecules, they take
part in the reaction but
are then recycled back
Inorganic molecules are
in the enzyme and don't
take part in the reaction.
They help the substrate
and active bind
together.
Competitive/Non competitive
Competitive inhibitors have a similar shape to
the substrate and are complementary to the
active site. They compete with the substrate for
the active site and occupy it with no reaction.
Non competitive inhibitors bind to the enzyme in
an alosteric site away from the active site.
Changes the shape of the active site so no more
substrate can bind to it.
Poisons and drugs
Cyanide: irreversible
inhibitor of cytochrome
c oxidase.