Enzymes

Activation energy is the energy required to start a reaction. All chemical reactions need activation
energy. Enzymes reduce the activation energy required to initiate a reaction.

Enzymes are protein molecules that increase the rate of a chemical reaction (catalyst).
They reduce the activation energy required to start a reaction
They participate in reactions but are not used up or permanently altered in the reaction and are
available for reuse
Without enzymes, metabolism is too slow for life to exist
Enzymes are specific for one reaction - each enzyme acts on only one substrate. This is because the
active site of an enzyme matches that of only one substrate.

Enzyme:

Breaks down:

Amylase
Maltase
Protease
Lipase
Aminopeptidases

Glucose
Maltose
Protein
Lipids/fats
Peptides (amino acids)

Many enzymes are intracellular they are used within cells that produce them
Some enzymes are extracellular they are secreted by cells and act outside. Eg: digestive enzymes.
Exergonic Reactions (Catabolic)
Break down of substrates
Releases energy
Eg: Cellular Respiration

Endergonic Reactions (Anabolic)

Combine substrates
Requires energy
Eg: Photosynthesis

Coenzymes and cofactors

Many enzymes require other, non-substrate molecules to be present to increase the ease with which the
enzyme binds to the substrate.

Cofactors are non protein parts required by enzymes before they act. These parts include metallic
ions such as zinc and magnesium.
If a cofactor is an organic molecule its called a coenzyme.
Coenzymes are organic non-substrate molecules required to be present to increase the ease with
which the enzyme binds to the substrate. Many are vitamins, or are derived from vitamins.

Factors Affecting Enzyme Activity

The rate of an enzyme reaction is influenced by: pH, temperature, enzyme concentration, substrate
concentration & inhibitors.
Temperature
In any chemical reaction, warming the reactants will increase the rate of reaction due to the increased
rate of interaction between molecules. Similarly, decreasing the temperature will reduce the movement
of molecules, hence the rate of the reaction will slow. Freezing the reactants will stop the reaction.

Enzymes have an optimal temperature, reflecting the optimal temperature of the organism.
If too much heat is applied the enzyme will permanently denature - causing it to permanently lose its
3D shape, resulting in the reaction slowing and then eventually stopping.
When the temperature is too low, the enzyme will become inactive (but not denatured). It will
become active again once when it reaches optimal temperature.

pH
Enzymes have optimal pH reflecting the pH of its working environment. Mostly pH 7 in animals.
A change in pH from the optimum will change the hydrogen bonding between amino acids. Hence, it
will change the 3D structure of the enzyme and the shape of the active site, affecting its ability to
combine with substrate molecules. When this happens, the rate of metabolic reaction declines.
Inhibitors
Competitive inhibition inhibitors act by binding to the active site of the enzyme.
Non-competitive inhibition inhibitors act by binding to a distinct (allosteric) site away from the
active site and changing the shape of the active site

Competitive inhibitors can be overcome by increasing the concentration of substrate. This increases the
likelihood that a substrate molecule will interact with the active site instead of an inhibitor molecule.
Non-competitive inhibitors cannot be overcome this way.

Substrate & product concentration

Increasing substrate concentration will increase the rate of the reaction until the enzyme is saturated.
At this point, all enzymes and active sites are constantly occupied.
Increasing enzyme concentration will increase the rate of the reaction as there are more enzymes
reacting with substrates.

As a reaction progresses, the increasing concentration of product will also begin to exert an effect,
slowing the rate of reaction.