ENZYMES

Scientists in the 19th century, like

Louis Pasteur, observed that some
chemical reactions occurred with the
addition of ferments, or living
organisms like yeast. But they also
noticed that that some reactions
occurred without the living organisms
themselves but instead just some of
their extracts. What catalysts made
these reactions happen without the
actions of a living cell? This lead to
the discovery of enzymes.
Anselme Payen

A French chemist who

was the first to
discover an enzyme
called diastase in 1833
 Wilhelm
Kuhne
In 1878, a German
physiologist who coined
the term “enzyme”,
which comes from the
Greek word
“enzymos”which means
“leavened”
What are Enzymes?
 Enzymes are organic or biological catalysts
Catalysts – are substances that speed up a
reaction without being used up, destroyed, or
incorporated into the end product

 The basic role of any enzyme is to increase

the rate of biochemical reactions. Most
reactions inside cells occurs almost one million
times faster with the aid of enzymes.
 Enzymes in the body also help carry out various
chemical functions like respiration, digestion of
food, assist in the process of providing cellular
energy, support the brain functions, repairing and
healing processes within the body, breaking down
toxins, detoxification of blood, etc. In short, our
bodies will cease to function, if there were no
enzymes.

 Majority of enzymes are proteins (RNA can also

act as an enzyme in some cases, it is called
ribozymes)
 Enzymes are made from amino acids, and nearly all
of them are proteins. When an enzyme is formed,
it is made by stringing together between 100 and
1000 amino acids in a very specific and unique
order. The chain of amino acids then folds into a
unique shape. That shape allows the enzyme to
carry out specific chemical reactions – an enzyme
acts as a very efficient catalyst for a specific
chemical reaction. The enzyme speeds that reaction
up tremendously.
 How do enzymes work?
 There are 2 models on how enzymes work.
These are the:

1. Lock and Key Model (1894)

2. Induced Fit Model (1958)
Lock and Key Model

• Substrates – is a molecule upon which an enzyme acts.

• Active Site – a part of an enzyme where the binding of the substrates happen.
• Enzyme-Substrate Complex – is the intermediate formed when a substrate molecule
interacts with the active site of an enzyme. Following the formation of an enzyme-
substrate complex, the substrate molecules undergoes a chemical reaction and is
converted into a new product.
Induced Fit Model
  Enzymes can be regulated by other molecules that either increase or
reduce their activity. Molecules that increase the activity of an
enzymes are called activators. Molecules that decrease the activity of
an enzymes are called inhibitors. Other than substrates, inhibitors and
activators can also bind in the active site of an enzyme.

 Enzymes’ activity can be inhibited in a number of ways:

1. Competitive Inhibitors – a molecule blocks the active site so

that the substrate has to compete with the inhibitor to attach
to the enzymes.
Reversible Inhibitors 2. Non-competitive Inhibitors – a molecule binds to an enzyme
somewhere other than the active site and reduces how
effectively it works.
3. Uncompetitive Inhibitors – the inhibitor binds to an enzyme
and substrate after they have bound to each other. The
products leave the active less easily, and the reaction is slowed
down.
4 Irreversible Inhibitors – binds to an enzyme and permanently
inactivates it.
 Coenzymes
- are organic molecules that are required by
certain enzymes to carry out catalysis. They bind to the
active site of the enzyme and participate in catalysis but
are not considered substrates of the reaction.

 Cofactors
- are often classified as inorganic substances that
are required for, or increase the rate of catalysis.
Characteristics of an
Enzyme
It is easily
Enzyme is a influenced, It acts as
protein. by catalyst
environment
al change,
It functions
specifically. It functions
in reverse.

A small
amount of
Enzymes is
required
Classes of Enzymes
 Classes of Enzymes

Oxidoreductases
 catalyze oxidation or reduction reactions.
 These reactions involve the transfer of electrons from one molecule ( the
reductant ) to another ( the oxidant).
 Classes of Enzymes
 Example:
 Classes of Enzymes
Transferase
 Catalyze the transfer of a functional group from one molecule to another.
 The first molecule is called the donor and the second molecule is called the
acceptor.
Classes of Enzymes
 Example
 Classes of Enzymes
Hydrolases/ Hydrolysis
 the most common type of enzymes
 The term comes from the Greek prefix hydro- (water) with lysis ( meaning
to break apart).
 this is the breaking of chemical bonds with the addition of water.
 Classes of Enzymes
• Example
 Classes of Enzymes
Lyase
 catalyzes the removal or formation of C-C, C-N, C-O or C -S bonds from a
substrate by means other than hydrolysis.
 Classes of Enzymes
Somerace
 catalyzes the structural rearrangement of a molecule due to the isomeration
in the molecule.
 Classes of Enzymes
Ligase
 catalyzes the joining of two molecules by forming a new chemical bond of C
- O,C -S,C-N or C -C and it requires the breaking down of ATP.
 Example of Specific Enzymes
 Lipases - a group of enzymes that help digest fats
in the gut.
 Amylase - helps change starches into sugars.
- also found in saliva.
 Maltase - also found in saliva; breaks the sugar
maltose into glucose.
- found in foods such as potatoes, pasta,
and beer.
 Trypsin - found in the small intestine, breaks
proteins down into amino acids.
Example of Specific Enzymes

 Lactase - found in a small intestine, breaks lactose,

the sugar in milk, into glucose and
galactose.
 Acetylcholinesterase - breaks down the
neurotransmitter acetylcholine in nerves
and muscles.
 Helicase – unravels DNA.
 DNA polymerase – synthesize DNA from deoxy
ribonucleotides.
Factors Affecting Enzyme Activity:

• Temperature - raising temperature generally speeds up a

reaction and lowering temperature slows down a reaction.
However, extreme high temperatures can cause an enzyme to
lose its shape (denature) and stop working.
• pH - each enzyme has an optimum pH range. Changing the pH
outside of this range will slow enzyme activity .Extreme pH
values can cause enzymes to denature.
• Concentration

 Enzyme concentration - increasing enzyme concentration will

speed up the reaction, as long as there is substrate available to bind to.
Once all of the substance is bound, the reaction will no longer speed up
since there will be nothing for additional enzymes to bind to.

 Substrate concentration - increasing substrate concentration also

increases the rate of reaction to a certain point. Once all of the
enzymes have bound, any substance increase will have no effect on the
rate of reaction, as the available enzymes will be saturated and working
at their maximum rate.