Bio cheat sheet -

Enzymes are proteins that act as catalysts, reducing the activation energy required for a
substrate to catalyze. They have an active site where the substrate binds to the enzyme,
allowing it to be broken down or bonded together. The active site is shaped specifically for a
specific substrate. Temperature can affect the active site, leading to denaturation. Denaturation
occurs when the optimum temperature range is exceeded, which is the temperature in which an
enzyme works most effectively. In liver, enzymes have an optimum temperature of 37.5˚C,
which increases kinetic energy and substrate speed. However, if the temperature rises above
this, weak bonds may break, leading to thermal denaturation, leaving the enzyme permanently
inactive. Denatured enzymes are destroyed when the active site changes too much to catalyze
substrates.

Enzymes are essential biological catalysts that speed up chemical reactions in the body, both
anabolic and catabolic. They lower the activation energy required to catalyze substrates by
capturing the substrate within its active site through the induced fit or 'lock and key' mechanism.
Without enzymes, these simple reactions would take significantly longer than necessary for life.
Our metabolism involves processes like synthesis of organic molecules, energy transformations,
and the breakdown of unwanted substances, all of which require hundreds of enzymes.
Enzymes are used in chain reactions, evolving and changing with more reactions. They can be
reused repeatedly and are always useful unless denatured.

Introduction
Enzymes are large globular proteins that reduce the activation energy required to initiate a reaction
as they weaken the bonds in the substrate. Therefore, they act as organic catalysts by increasing
the rate of chemical reactions. Their function primarily depends on the presence of an active site or
substrate binding site, which is a region that has a complementary 3D shape to the substrate.

Key Components
Before we begin, here are some terms which you should familiarise yourself with.

● Activation Energy: the energy required to initiate a reaction

● Catalysts: substances which accelerate a reaction without being consumed
● Substrate: the substance(s) which an enzyme acts upon

Types of Chemical Reactions

● Anabolic and Endergonic: energy is absorbed by combining smaller molecules
● Catabolic and Exergonic: energy is released by splitting up large molecules

Models of Enzyme Function

There are currently two models for how enzymes function, the lock and key model and the induced
fit model which is more recent and plausible. The lock and key model states that the active site is an
exact match for its substrate. While the induced fit model states that the active site is a close match
for the substrate, but the binding of the substrate induces a conformation change allowing it to bind.

Induced Fit Model

Factors Affecting Enzymatic Activity

The functioning of enzymes relies heavily on the 3D shape of their active site. Any factor that alters
this will affect the activity of the enzyme as it may inhibit the formation of substrate-enzyme
complexes.

Temperature
All enzymes have optimal temperatures where they operate most efficiently. For Example, most
humans enzymes have an optimum temperature of around 37°C, the normal body temperature.
When the temperature increases, the molecules would have more kinetic energy, resulting in more
collisions between the substrates and enzymes. However, if the temperature is increased beyond
the optimum temperature, this causes the enzyme to denature, and hence the rate of the reaction to
rapidly decrease. When an enzyme denatures, the bonds within the enzyme break and the tertiary
structure unravels, leading to the loss of its conformation 3D shape, and therefore the substrate can
no longer bind with the active site. When the temperature is decreased, there is less kinetic energy
available and the movement between the enzymes and substrates will decrease, thereby slowing
the reaction. Ultimately, freezing the reactants will stop the reactions, however it can be reversed.

pH
Just like temperature, all enzymes have an optimal pH level. If the pH deviates significantly either
side of its optimum value, then this will cause changes within the hydrogen bonding within the
enzyme changing the 3D structure and thus inhibiting its activity.

Inhibitors
There are two types of inhibitors, competitive inhibitors and non-competitive inhibitors. If the inhibitor
covalently binds to the enzyme, permanently altering the structure of the enzyme then it is referred
to as being irreversible inhibition.

Competitive inhibitors work by having a similar shape to the usual substrate molecule and so they
can bind to the active site of the enzyme, preventing the formation of enzyme-substrate complexes.
These enzymes can be overcome by increasing the concentration of the substrate, as this increases
the likelihood that a substrate molecule will interact with the active site instead of an inhibitor
molecule.

Non-competitive inhibitors work by binding to an allosteric site on the enzyme. By binding to the
allosteric site, it causes a conformational 3D change within the enzyme, changing the shape of the
active site and thereby preventing it from binding to its substrate.

Typically, competitive inhibitors are reversible, while non-competitive inhibitors are irreversible.

Affect of Increasing Temperature

 Affect of Inhibitors

Cofactors
Many enzymes require other, non-protein molecules to be present to activate or increase the rate of
an enzyme. Coenzymes are a subset of cofactors and we will discuss some specific examples later
when we cover photosynthesis and cellular respiration. Some enzymes also require inorganic ions,
metal ions such as Mg2+ and Cu2+