Enzymes Control

Biochemical Reactions in
Living Organisms
What is a catalyst?
● A substance that speeds up the rate of a chemical reaction and is not

changed by the reaction.

● Enzymes are biological catalysts.

What is an enzyme?
Enzymes are proteins that are involved in all metabolic reactions where
they function as biological catalysts.
● They act as catalysts.
● They are made of protein.
● They alter the rate of chemical reactions without themselves being
chemically changed.
● Each enzyme has a unique shape.

Enzymes are synthesised in living cells.

INTRACELLULAR ENZYMES
Most enzymes work inside the cell- an example of these intracellular
enzymes is catalase (which breaks down harmful peroxide in liver cells).

EXTRACELLULAR ENZYMES
Other enzymes are made inside cells and then released from the cell to
perform their function- examples of these extracellular enzymes include
the digestive enzyme lipase (which breaks down fats to fatty acids and
glycerol) and amylase, which converts starch to maltose.

Enzyme action/ How enzymes work?

KEY TERMS
Substrate: The substance that an enzyme causes to react.
Product The new substance formed by a chemical reaction.
Active site: The part of an enzyme molecule to which the substrate
temporarily binds.
Complementary: With a perfect mirror-image shape.
Enzyme-substrate complex: The short lived structure formed as the
substrate binds temporarily to the active site of an enzyme.
Specificity (of enzymes): Only able to act on specific substrates.

Active site
They are specific dents on the surface of an enzyme molecule into which only a
complementary substrate binds temporarily.

LOCK AND KEY HYPOTHESIS

Use the following words and explain the LOCK AND KEY
HYPOTHESIS.
● Enzyme is the lock
● Substrate is the key
● Active site
● Complementary shape
● Enzyme substrate complex
● Products

LOCK AND KEY HYPOTHESIS

● This theory explains the mechanism of enzymatic reactions where
enzymes acts as a lock and substrate is the key.

● Each enzyme has an active site and only the substrate with the
complementary shape can fit to the active site of the enzyme forming
a temporary enzyme substrate complex.

● The enzyme then changes the substrate into product either by

 splitting the substrate or by joining the substrates to form a new
product. Now the enzyme is free and ready to bind with another
substrate.

USES
1. Digestion
Complex insoluble molecules are broken down into small soluble molecules.

2. Cellular respiration
All living things obtain energy by a type of catabolic reaction called respiration.
This uses oxygen to break down glucose into carbon dioxide, water and energy.

Factors that affect enzymes and their action

● Temperature and pH
● Each type of enzyme has a particular temperature and pH at which it
works fastest.
● These are called OPTIMUM TEMPERATURE and OPTIMUM pH.

NOTE: Most human enzymes have an optimum temperature around 37॰C while the
optimum temperature for most of the plants is around 25॰C.

Remember!
● Enzymes increase the rate of a reaction.
● Enzymes DO NOT increase the amount of product formed at the end
of the reaction.

ACTIVATION ENERGY
● In any chemical reaction, molecules must reach a certain energy state before
reaction is possible. This is known as the activation energy.
 ● The activation energy acts as a barrier to the reaction.
● The activation energy can be overcome through increasing the temperature
and pressure.
● Enzymes lower the activation energy needed to start a chemical reaction.

How do enzymes speed up chemical

reactions?
● Enzymes lower the activation energy of a
chemical reaction
● They allow the reactions to be carried out at a
LOWER TEMPERATURE RANGE!

Characteristics of Enzymes

1) Enzymes speed up the rate of reactions.

2) Enzymes are required in minute amounts. A small quantity is capable of
catalysing a huge reaction.
3) Enzymes are very specific, amylase will only act on starch and NOT on
proteins or fats. The specificity is due to its shape as explained by LOCK
AND KEY.

4) Enzyme activity is affected by temperature.

● The activity of the enzyme and the rate of reaction is highest at the optimum
temperature. At low temperatures, enzymes are inactive.
● As temperature rises, the rate of reaction increases because:
○ Heating leads to an increase in kinetic energy of molecules.
○ This leads to more successful or effective collisions, and more
formation of enzyme-substrate complexes.
● Beyond the optimum temperature, the enzyme activity decreases as the enzyme is denatured.
 5) Enzyme activity is affected by pH
● Enzymes are affected by the acidity or alkalinity of
solutions.
● Some work best in acidic environment e.g pepsin
● Some work best in the alkaline environment
e.g intestinal enzyme eg amylase
● Extreme changes in pH can denature the enzymes.

DENATURATION
● The 3D shape of the active site is determined by weak hydrogen bonds that
hold the chains of amino acids in place.
● An increase in temperature or a pH well above or below their optimum
causes vibrations in the atoms of the enzyme, causing the hydrogen bonds to
be disrupted/break.
● The active site loses its shape and is no longer complementary to the
substrate.
● The enzyme can no longer act as a catalyst.

6) Enzymes catalyse reversible

reactions
Most reactions in the living organisms are
reversible therefore enzymes catalyse
reversible reaction.

Why are enzymes required in small

amounts?
 ● Enzymes remain unchanged at the end of a reaction.
● The active site of an enzyme may be used again.
● Therefore, enzymes can work efficiently at low concentrations.
● Provided that the substrate(s) are present in excess, increasing the enzyme
concentration will increase the rate of reaction.

Enzyme Concentration
● Enzyme concentration affects the rate of reaction
● The higher the enzyme concentration in a reaction mixture, the
greater the number of active sites available and the greater the
likelihood of enzyme-substrate complex formation.
● As long as there is sufficient substrate available, the initial rate of
reaction increases linearly with enzyme concentration.
● If the amount of substrate is limited, at a certain point any further
increase in enzyme concentration will not increase the reaction rate
as the amount of substrate becomes a limiting factor.

Substrate Concentration
● The greater the substrate concentration, the higher the rate of
reaction:
○ As the number of substrate molecules increases, the
likelihood of enzyme-substrate complex formation
increases.
○ If the enzyme concentration remains fixed but the amount
of substrate is increased past a certain point, however, all
available active sites eventually become saturated and any
further increase in substrate concentration will not increase
the reaction rate.
○ When the active sites of the enzymes are all full, any
substrate molecules that are added have nowhere to bind
in order to form an enzyme-substrate complex.
● For this reason, in the graph below there is a increase in reaction
rate as substrate is added, which then plateaus when all active
 sites become occupied.

What happens at low substrate

concentration?
● At low substrate concentrations, collisions between enzyme and substrate molecules
are infrequent and reaction proceeds slowly.
● As the substrate concentration increases, the rate of reaction initially increases
proportionately as collisions between enzyme molecules and substrates become
more frequent.