Enzymes

• An enzyme is a biological catalyst and is almost always a protein.

• It speeds up the rate of a specific chemical reaction by lowering activation energy

• The enzyme is not destroyed during the reaction and is used over and over.
ROLE OF ENZYMES
Just like inorganic catalysts, enzymes:
• are only needed in relatively small amounts
• are not used up or changed at the end of
the reaction
• do not alter a reaction’s equilibrium position
• provide an alternative reaction pathway that
lowers the activation energy for a reaction
Active Site
• The specific part of the enzyme molecule with which a reactant can interact is known as
its active site.
• The active site is usually a uniquely shaped flexible hollow or cavity within the protein
where the reaction occurs.

Substrate
The reactant molecule that binds with the
active site is referred to as the substrate

Enzyme-substrate complex
Substrate molecule fits into the enzyme like a
key in a lock, forming an enzyme–substrate complex,
allowing the enzyme to break the bonds in the substrate
LOCK-AND-KEY MODEL OF ENZYME ACTION
• The catalytic activity of an enzyme is highly specific and depends on its overall three-
dimensional structure.

• Because enzymes are proteins, their overall three dimensional structure is dictated by their
tertiary and quaternary structure

• In the lock-and-key model, the substrate molecule fits into the enzyme like a key in a lock,
forming an enzyme–substrate complex, allowing the enzyme to break the bonds in the
substrate.

• The enzyme is specific for a particular substrate, so binding of a different molecule will not
result in a reaction
• The shape of the substrate molecule must match the shape of the active site.
Only reactant molecules that have a suitable ‘key’ shape can enter and form
the necessary intermolecular interactions with the active site (‘lock’) of
the enzyme.
Chiral enzymes (optical isomers)
Enzymes, which are chiral, often distinguish between the two enantiomers of a chiral
substrate.

Because enantiomers have different three-dimensional shapes, they may interact with an
active site differently.

Only one enantiomer might fit the active site and participate in the reaction, so that
enantiomer is the only one that is biologically active.
Induced Lock and Key Model

• Since the lock-and-key model for enzyme action was proposed, chemists have realised that
enzymes have flexible structures.

• The shape of an enzyme’s active site can be modified markedly by the binding of a
substrate.

• This discovery led to a modification of the lock-and-key model and the development of the
induced fit’ model.
Coenzymes and cofactors
Coenzymes and cofactors are molecules that help an enzyme or protein to function
appropriately.

Coenzymes interact with the enzyme during catalysis and their role is often to act
as carriers of electrons or specific groups of atoms.

They change the surface shape of the enzyme and hence the binding properties of
the active site, allowing the enzyme to better interact with the substrate
Enzyme Activity

Enzyme activity is the amount of substrate that is converted to products per unit time.

• Enzyme activity depends on the quantity of active enzyme that is present as well as
reaction conditions

• As most enzymes are proteins, enzyme activity is also affected by factors that
disrupt protein structure.

• These factors include

- pH of the surroundings
- Temperature.
DEPENDENCE ON pH
Enzyme activity is at its maximum value at the optimum pH.

As the pH value is increased above or decreased below the optimum, pH the enzyme activity
decreases.

Example:
Pepsin is active only at pH values below 3 and
amylase is active between pH 5 and 9.

The pH at which the enzyme activity is

greatest is known as the enzyme’s optimum
pH.

The optimum pH of pepsin is 1.5, while the

optimum pH of salivary amylase is 7.2
WHY does very low or very high pH change enzyme activity?
- When enzyme is exposed to very high or low pH, the amino acid/carboxylic acid groups the
active site could be protonated or de-protonated and protein structure of the enzyme changes.

- This means that its active site changes shape, and the enzyme is said to have denatured.

- The active site no longer has a complementary shape to its

specific substrate molecule, and it will no longer be able to
function to catalyze a biological reaction
DEPENDENCE ON TEMPERATURE
Enzyme activity is also affected by temperature
The temperature at which the enzyme activitis greatest is known as the enzyme’s optimum
temperature.

Enzymes that operate inside human cells have an

optimum temperature of about 37°C.

At temperatures above and below the optimum

temperature, enzyme function is impaired.

This is one of the reasons why conditions such

as hypothermia and fever (when you have an
abnormally low or high temperature) are
life threatening.
WHY does very low or high temperature change enzyme activity?

An increase above or decrease below the optimum temperature have different effects on
an enzyme.

1. Increase in temperature
As the temperature increases above the optimum temperature, the increased kinetic energy of
the molecules disrupts the structure of the enzyme. The increased movement throughout the
enzyme breaks some of the intermolecular forces responsible for the tertiary and quaternary
structure. This change in three-dimensional shape of the enzyme means the active site can no
longer effectively catalyse the reaction so the reaction rate decreases rapidly.

2. Decrease in Temperature
As the temperature decreases below the optimum temperature, the enzyme and substrate
molecules have lower kinetic energies, resulting in less frequent and less energetic collisions
between the molecules.
Denaturation
A change in the enzyme’s catalytic activity due to the change in the shape of the active
site is called denaturation of enzyme

Denaturation due to temperature: Once the temperature becomes too high, the
increased kinetic energy of the polypeptide chains of the enzyme breaks some of the
bonds between side chains of the amino acid units and new bonds are formed.

Denaturation due to pH: When the pH is above or below the enzyme’s optimum pH, the
enzyme’s overall three dimensional shape can be disrupted. Substantial changes in pH can
change an enzyme’s structure permanently and denature it
HYDROLYSIS OF PROTIENS
The hydrolysis of a protein molecule involves breaking covalent bonds in the peptide link to
produce smaller peptides and amino acids.
 HOMEWORK

Complete Chapter review

Questions 4-12
(Pages 562/563)