 Enzymes which are produced
and retained in the cell for
the use of the cell itself are
called intracellular enzymes.
 These enzymes are formed in
the cytoplasm, nucleus,
mitochondria and
chloroplasts.
 For example, the enzyme
oxidoreductase catalyses
biological oxidation and
reduction in the
mitochondria.
 Enzymes are which produced
in the cell but secreted from
the cell to function externally
are called extracellular
enzymes.
 For example, digestive
enzymes produced by the
pancreas are not used by the
cells in the pancreas but are
transported to the
duodenum, which is the
actual site of the enzymatic
reaction.
 Ribosomes are the sites of protein synthesis. Since enzymes are
proteins, ribosomes are also the sites of enzyme synthesis.
The sequence of events in the synthesis of enzymes :
1. The information for the synthesis of enzymes is carried by the DNA. The
sequence of bases on the DNA are codes to make protein.
2. In the nucleus, the DNA double helix unwind and exposes its two strands
for the synthesis of a messenger RNA (mRNA) strand. The mRNA is
synthesised according to the instruction on the DNA.
3. The mRNA then leaves the nucleus and moves to a ribosomes.
4. The mRNA attaches itself to the ribosome. The ribosome acts as a
workbench for the mRNA. The mRNA contains information which codes for
the sequence of amino acids.
5. This genetic information is translated into the primary structure of a
specific protein.
6. Each amino acid is bonded to the next and as a result, a chain of amino
acids (polypeptide) is formed and is ready for release into the cytoplasm.
The information for the synthesis of The DNA double helix unwind and exposes its two strands
enzymes is carried by the DNA. The for the synthesis of a messenger RNA (mRNA) strand.
sequence of bases on the DNA are The mRNA is synthesised according to the instruction on
codes to make protein. the DNA.

The mRNA then leaves the nucleus and

moves to a ribosomes.

The mRNA attaches itself

to the ribosome. The
ribosome acts as a
workbench for the mRNA.

This genetic information is translated into the

primary structure of a specific protein.
 Many enzymes produced by specialised cells are secreted
outside the cell.
 For example, pancreatic cells secrete pancreatic amylase
outside the cells to be transported to the target organ.
1. The nucleus contains DNA which carries the information for the synthesis
of enzymes.
2. Proteins that are synthesised at the ribosomes are transported through the
space within the rough endoplasmic reticulum (rough ER).
3. Proteins depart from the rough ER wrapped in vesicles that bud from the
membranes of the rough ER.
4. These transport vesicles then fuse with the membranes of the Golgi
apparatus and empty their contents into the membranous space.
5. The proteins are further modified during their transport in the Golgi
apparatus, for example, carbohydrates are added to protein to make
glycoproteins.
6. Secretory vesicles containing these modified proteins bud off from the
Golgi apparatus and travel to the plasma membrane.
7. These vesicles will then fuse with the plasma membrane before releasing
the proteins outside the cell enzymes.
1. Most enzymes are complex 3. Hence, the shape of the substrate
which are made up of one must fit the enzyme precisely if a
or more polypeptide reaction is to take place.
chains. 4. This explains why enzymes are
2. An enzyme has three highly specific.
dimensional shape which is
very precise. The
polypeptide chains of the
enzyme molecule are
folded to form a cleft or
pocket called an active site.
3. The active site of an
enzyme has a distinctive
shape and charges that
complement those of its
substrate.
6. The way an enzyme binds to its substrate can be explained by
the ‘lock and key’ hypothesis.
[ lock : enzyme molecule, key : substrate molecule]

7. The substrate molecule binds to the active site to form an

enzyme-substrate complex, like a key fits into a lock.
8. The enzyme catalyses the substrate molecule and produces
product molecules.
9. Product molecules leave the active site of the enzyme molecule.
10. The enzyme molecule is now free to bind to more molecules of
the substrate.
Enzymes are very specific and it was suggested by Emil Fischer in 1890 that this was
because the enzyme had a particular shape into which the substrate(s) fit exactly.
This is often referred to as "the lock and key" hypothesis. An enzyme combines with
its substrate(s) to form a short lived enzyme-substrate complex.
1. Enzymes are particularly sensitive to the chemical and
physical changes in the surrounding environment.
2. The factors which affect enzyme activity include :
▪ pH
▪ Temperature
▪ Substrate concentration
▪ Enzyme concentration
3. The rate of enzyme-catalysed reaction can be investigated
by measuring the amount of substrate used up, or the
amount of products formed, per unit time.
1. At low temperature, an 3. For every 10⁰C rise in
enzyme-catalysed reaction takes temperature, the rate of enzymatic
place slowly. This is because the reaction is doubled. However, this is
substrate molecules are moving only true until the optimum
at relatively slow rate. temperature is reached.
4. As the surrounding
temperature increases, the
rate of reaction is increased
until it reaches the optimum
temperature.
The optimum temperature is
the temperature at which an
enzyme catalyses a reaction
at the maximum rate. Most
enzymes in humans and
animals have an optimum
temperature of about 37⁰C.
2. At higher temperature, the rate of reaction between the
substrate and enzyme increases. As the temperature increases,
the substrate molecules move faster. Collisions between the
substrate and enzyme molecules occur more frequently and
increase the chances of the substrate molecules coming into
contact with the active sites of the enzymes.
5. Beyond the optimum
temperature, any increase
in temperature causes the
rate of reaction to
decrease, sharply until it
stops completely at about
60⁰C. At very high
temperature, the chemical
bonds holding the enzyme
molecules in their precise
shape begin to break. This
alters the 3-D shape of the
enzyme molecules and
eventually destroys the
active sites. This means
that the substrate can no
longer fit into the active
sites of the enzyme. The
enzymes is said to be
denatured. Denaturation
of enzymes is irreversible.
1. The activity of enzymes is affected by the 5. However, there are a few exception, such as pepsin
acidity and alkalinity of the solutions in which which can only function optimally in an acidic condition
they act. A slight change in pH can have an (pH 2) in the stomach, while trypsin can only function
adverse effect on the rate of enzyme- optimally in an alkaline condition (pH 8.5) in the
catalysed reactions as each enzyme can only duodenum.
function optimally at a particular pH.
6. Unlike the effects of heat on enzymes, the effect of
2. The optimum pH at which the rate of pH on the active sites of enzymes are normally
enzymatic reaction is at its fastest. In a cell, reversible. When the pH reverts to the optimum level
most enzymes function optimally at a pH for the enzyme, the ionic charges on the active sites are
that ranges from 6 to 8. restored, thus enabled the enzyme to resume its
normal function.
3. A change in the pH value can alter the
charges on the active sites of an enzyme and
the surface of a substrate. This can reduce
the ability of both molecules to bind with
each other. For example, at a low pH value,
excess hydrogen ions attach themselves to
the active site of the enzyme, thus altering
the ionic charges on the active site.

4. In extreme pH conditions (acidic or

alkaline), the configuration of the enzyme is
altered and the enzyme structure is altered,
destroying its normal function.
1. At low substrate concentrations, substrate
few substrate molecules are
present. As such, there are many enzyme
active sites which are available.

2. An increase in substrate
concentration means more Rate of
substrate molecules are available. reaction
This means there are more chances
of collision between the substrate
molecules and enzyme molecules 1.0
for a catalytic reaction to take place.
As more substrate molecules fill the
0.5
active sites, more products are
formed per unit time. Therefore, the
rate of reaction increase in direct
Substrate concentration
proportion to the substrate
The effect of substrate concentration on
concentration.
the activity of enzymes.
3. The increase in substrate
concentration will only lead to an
increase in the rate of reaction if
there are enough enzyme molecules
which are available to catalyse the
additional substrate molecules.
4. However, there is a limit to how the rate of a reaction can be 6. At high substrate concentrations,
further increased by adding more substrate molecules to a fixed there are more substrate molecules
concentration of an enzyme. At a certain substrate than enzyme molecules. The excess
concentration, the rate of reaction will not increase further and substrate molecules will have to
become constant. The reaction is at a maximum rate. At this compete with one another for the
point, all active sites are filled and engaged in catalysis. The active sites. These sites only
enzyme molecules are said to be saturated. available after the enzyme
molecules have finished catalysing
5. As soon as the product leaves an active sites, another the substrate molecules. When all
substrate molecules enters the active site. active sites are engaged in the
catalysis of the substrate, an
increase in the substrate
concentration will not alter the rate
of reaction. The rate of reaction
becomes constant. At this point, the
enzyme concentration becomes a
limiting factor. The rate of reaction
Rate of
can only be increased if the enzyme
reaction
concentration is increased.

1.0

0.5

Substrate concentration
1. The rate on an enzyme-catalysed reaction 3. Beyond the 4. When the enzyme
increases when the enzyme concentration is maximum rate concentration is doubled, the
increased. It will increases as long as no of reaction, the rate of reaction or the number
other factors limiting the rate of reaction and concentration of substrate molecules that are
the substrate molecules available are in of substrate converted to products per unit
excess. This is because more active sites are becomes a time will be doubled as long as
available for enzyme action. limiting factor. the substrate are present in
excess concentration.
2. The rate of enzyme-catalysed reaction is directly
proportional to the concentration of the enzyme
present until a maximum rate is achieved.

Rate of

Amount of substrate used

reaction •Maximum rate of reaction
•The concentration of substrate 4x
becomes a limiting factor
Enzyme
concentration
2x
1x
time
Enzyme concentration When the enzyme concentration is doubled,
The relationship between the rate of the number of substrate molecules
reaction and enzyme concentration converted into products also doubles
1. Enzymes can be used as catalysts in various industrial
processes.
2. The use of enzymes in industrial processes is known as
enzyme technology.
3. Enzymes can be isolated from cells and function outside the
cell.
4. Enzymes can be obtained from plants and animals although
most enzymes are obtained from microorganisms, mainly
bacteria and fungi.
5. Microorganisms are grown on a large scale industrial
fermenters, so that large quantities of enzymes can be
produced.
Type of Enzymes used Uses
industry/application
1. Food processing Protease Tenderise meat.
industry
a. Meat products
b. Starch products Amylase and Change starch to sugar in the making of
amyloglucoxidase syrup.
Glucose isomerase Production of high fructose syrup : glucose
is converted into fructose. Since fructose is
much sweeter than glucose, it is widely
used in slimming products as only small
amounts are needed.
c. Fish products Protease Removes the skin of fish.
d. Dairy products Lipase Ripening of cheese.
Lactase Hydrolyses lactose to glucose and galactose
in the making of ice cream.
Rennin Solidifies milk proteins.
Type of Enzymes used Uses
industry/application
e. Alcoholic drinks Zymase Converts sugars into ethanol.
(beer/wine)
f. Bread and other Amylase Converts starch flour into sugar in the
bakery products making of bread.
g. Cereal grain Cellulase Breaks down cellulose and removes seed
products coats from cereal grains.
h. Seaweed products Cellulase Extracts agar from seaweed.
2. Leather products Trypsin Removal of hair from animal hides.
3. Textile products Amylase Removes starch that is used as stiffeners
from fabrics.
4. Medical/pharmace •Pancreatic trypsin •Treats inflammation
utical products •Microbial trypsin •Dissolves blood clots
5. Biological washing Protease and Dissolve protein and starch stains in clothes.
powder or amylase
detergents
1. Cells contain various types of chemical substances.
2. These chemical substances are important to enable the cells
to function optimally.
3. If our bodies lack of certain types of compounds such as
protein, new cells and tissues cannot be produced to
replace damaged ones. This will inhibit body growth.
4. Enzymes and hormones are made up of proteins. Without
enzymes, all biological reactions will proceed too slowly to
sustain life. Hence, chemical substances are very important
to cells.