Enzymes

Compendium

Enzymes (biological catalysts)

- globular proteins with a tertiary structure.

- structure of enzymes is specific to their function.
- contain an active site within the catalytic activity takes place.
- act as catalysts by reducing the activation energy, therefore reactions happen quicker and at lower
temperatures.
- their activity is affected by temperature, pH, inhibitors and substrate & enzyme concentrations.
- do not get used up in the reaction

Intracellular enzymes – enzymes which work inside cells, involved in digestive processes.
Extracellular enzymes – enzymes which are secreted (released from the cells) into the digestion
system.

Active site – a cleft area within the catalytic activity of an enzyme takes place, complimentary to the
substrate molecule.

Brownian motion – molecules continually and randomly move around colliding with each other.
These random collisions of enzymes with substrates lead to formation of products.

Activation energy – amount of energy that must be applied for a reaction to proceed.

Catalyst – a molecule that speeds up a chemical reaction but does not get used up and remains
unchanged.

Rate of reaction - the speed at which a chemical reaction proceeds.

Lock and Key hypothesis – complimentary shaped substrate molecule fits perfectly into a specific
active site like a key fits into the lock forming an E-S complex. Reaction occurs, and an E-P complex is
formed. The product molecule diffuses away from the active site. Enzyme remains unchanged and
can be reused.

Induced fit hypothesis – substrate molecule induces the active site to change shape, so it fits around
the substrate more closely, forming an E-S complex. Reaction occurs, and an E-P is formed. The
product molecule diffuses away from the active site, and the active site reverts to its original shape.
The enzyme can be reused.

Since the active site relies on charged R-Groups activity, changing pH alters the charge around the
active site and interferes binding with the substrate.

Marek Gojtowski
Examples of enzymes

Denaturation – irreversible changes to the tertiary structure of an enzyme which stop it from
functioning.

How does temperature affect enzyme-controlled reactions?

Applying heat to molecules makes them move faster and vibrate. These
vibrations can break ionic, hydrogen and disulphide bonds which are
responsible for holding the tertiary structure, including the active site.

Below the optimum temperature, increasing temperature will increase

the rate of the enzyme-controlled reaction by increasing the number of
successful collisions. Increasing heat beyond the optimum temperature
reduces the ROR due to changes to the tertiary structure and might lead
to denaturation.

pH Scale - measure of concentration of H+. The higher the concentration of H+ the lower the pH
value.

Optimum pH – pH value at which the rate of an enzyme-controlled reaction is at its maximum.

Buffer - a chemical solution that resists changes in pH by maintaining a constant level of hydrogen
ions in solution.

Denaturation – irreversible changes to the tertiary structure of an enzyme such that it cannot
function.

How does pH affect enzyme-controlled reactions?

Hydrogen ions have a positive charge, hence changing their

concentration around an enzyme can interfere with hydrogen and ionic
bonds responsible for holding enzyme’s tertiary structure, and therefore
change to the active site shape and ROR.

- This definition also applies to concentration of OH-.

Enzymes work optimally within a narrow pH range, therefore a change in

pH may result in fall in the ROR. Extreme changes of pH can lead to
denaturation.

Marek Gojtowski
Limiting factor – a situation where all other conditions are kept constant, increasing the
concentration of that factor will increase the ROR.

How does substrate concentration affect enzyme-controlled reactions?

As the concentration of substrate increases, successful collisions

between enzyme and substrate molecules occur more often. More
E-Z complexes form, so more
E-P complexes are formed. ROR increases.

When substrate concentration reaches the maximum value, all

active sites are occupied at all times. Further increase in
concentration has no effect on ROR.
Limiting factor: enzyme concentration.

How does enzyme concentration affect enzyme-controlled reactions?

As the enzyme concentration increases, more active sites are

available. More E-Z complexes form and therefore E-P complexes as
well. ROR increases.

When enzyme concentration reaches the maximum value, all

substrate molecules are occupying enzyme active sites. Further
Increase in enzyme concentration has no effect on ROR.
Limiting factor: substrate concentration.

Inhibitor – substance that slows down the rate of an enzyme-

controlled reaction by affecting the enzyme molecule in some way.

Inhibitors are an essential form of cellular control, allowing enzyme

reaction rate to be slowed when necessary.

Competitive inhibitors – molecules with a similar shape to substrate

molecule. Can occupy the active site, forming E-I complexes so the
substrate molecule cannot enter. ROR falls.

The amount of inhibition depends on the concentration of inhibitor and

substrate. More substrate = more successful collisions.

Non-competitive inhibitor – attaches to an enzyme molecule but not at

the active site. This process distorts enzyme’s tertiary structure, which
leads to a shape change of the active site. Substrates cannot longer fit
into the active site, E-S cannot form, ROR falls.

If all the enzymes form an E-I complex, the reaction will stop. More
substrate = no effect on ROR.

Marek Gojtowski