Gen Bio

COMPONENTS AND
CHARACTERISTICS
OF AN ENZYME
Princess Niña Barruca Justine Puyo Mike Christian Cabataña
Different types of cells, tissues, and other
complex organs make up the human body. To
maintain a healthy existence, our body
produces substances to speed up biological
functions such as breathing, digestion,
excretion, and a few other metabolic activities
Enzymes play a crucial role in
all living things, governing all
biological processes.
Biochemical reactions are
catalyzed by enzymes, which
are biological polymers that
act as catalysts.
• The SUBSTRATE is the
REACTANT in an enzyme-
catalyzed chemical, the material
that is CHANGED.
• The ACTIVE SITE is the part of

the enzyme where the substrate
binds, and its shape controls
which substrates the enzyme can
bind
COMPONENTS OF THE ENZYMES
• Active site
The active site is a region of an enzyme
that is frequently referred to as the
binding site. The substrate interacts
with amino acids in the binding site to
bind to tue enzyme. It comprises amino
acids that both bind the substrate and
aid in its conversion to a product.
• Cofactor
A cofactor is a non-protein chemical molecule
that is necessary for tue biological action of a
protein. The proper functioning of many
enzymes necessitates the presence of cofactor.
Cofactors are "helper molecules" that aid
enzyme activity. Ions and organic compounds
can both be used as confactors. Vitamins or
vitamins derived from vitamins are common
organic cofactors.
• Coenzyme
A conenzyme is an organic non-protein
compound that catalyzes a reaction by
binding with an enzyme. Confactors and
coenzymes are similar chemically, but
they are not the same. When coupled
with an enzyme, a coenzyme can be
used several times.
• Apoenzyme
Apoenzyme is the protein part of an enzyme.
The non-protein part cofactor together with
the protein part apoenzyme forms a
holoenzyme. Apoenzyme are important for
enzymatic acticity since they are responsible
for the specificity of enzymes to their
substratee. Apoenzymes alone are not active
enzymes; they must bind to an organic or
inorganic cofactor in order to be activated.
• Holoenzyme
Enzymes' active forms are called
holoenzymes. It is consist of apoenzyme and
cofactor. The function of a holoenzyme is to
change substrate into product, just like an
enzyme does, but holoenzymes require a
cofactor to be present. Additionally,
holoenzymes are often made up of smaller
protein parts called subunits.
Characteristics of
Enzymes
1. Good catalyst
In order for a cell to function properly it has to

undergo several chemical reactions.
Enzymes or also called “biological catalyst”,

increases the speed of a reaction.
2. Reusable
Enzymes are not used up in reactions.
They can be used again for more reactions after

they bind to the substrate and catalyze the reaction.
3. A few number of enzymes is required
It only requires a minimal number of

enzymes in a cell because an enzyme can
be employed multiple times in the process.
4. Selective to its substrates
Enzymes interact with substrates, which are chemical

reactants. The locations, patterns, structure, and
characteristics of these residues all contribute to the
active site's chemical environment. Like a jigsaw puzzle
piece, a specific chemical substrate binds to this location,
making the enzyme unique to that substrate.
5. Chemically recognizes, binds and
modififies substrates.
With the use of their active sites, enzymes bind

the substrate and modify it into different
molecules as a product of the reaction.
Factors Affecting
Enzyme Activity
Temperature
Increasing the temperature of a

reaction often accelerates it, and
a reaction is slowed by lowering
the temperature. An extremely
high temperature, on the other
hand, can cause an enzyme to
denature (lose its shape) and stop
working.
(a measure of acidity)
pH
Each enzyme has a pH range where it works best.

Enzyme activity will be slowed if the pH is changed
outside of this range. can denature if the pH is too high.
Even low pH changes the electrical charges on various
chemical groups of enzyme molecules, affecting the
enzyme's capacity to bind substrate and catalyze a
process.
pH
The pH scale ranges from 1 to 14, with pH 7 being neutral,

pH 1–6 acidic, and pH 8–14 basic. The enzyme amylase,
which is present in saliva, has its maximum activity at pH
7. The activity of amylase changes as the pH changes – a
higher enzyme activity will result in a faster rate of
reaction.
Concentration Effects
Substrate Enzyme
Concentration Concentration
Substrate Concentration
To a certain extent, increasing the substrate concentration

raises the reaction rate. Any increase in substrate will have
no influence on the rate of reaction once all of the enzymes
have bonded, as the available enzymes will be saturated
and operating at their maximal rate.
Enzyme Concentration
As long as there is substrate available for binding,

increasing enzyme concentration will increase the chemical
reaction rate. When all of the substrate has been bound, the
reaction will no longer accelerate because thing for
additional enzymes to bind to.
Activators Effect
As long as there is substrate available for binding,

increasing enzyme concentration will increase the chemical
reaction rate. When all of the substrate has been bound, the
reaction will no longer accelerate because thing for
additional enzymes to bind to.
Inhibitors Effect
Enzyme activity can be inhibited in a number of ways.

The following are two of them:
Competitive Noncompetitive
Inhibition Inhibition
Competitive Inhibition
When molecules that are substantially similar to the

substrate molecules bind to the active site, they inhibit
the actual substrate from binding. Penicillin, for
example, is a competitive inhibitor that inhibits the active
site of an enzyme used by many bacteria to build their
cell walls.
Noncompetitive Inhibition
1.Happens when an inhibitor binds to the enzyme somewhere

other than the active site.
2. The inhibitor is believed to bind to the enzyme in such a way that
the typical active site is blocked in some cases of noncompetitive
inhibition.
3. In other cases,the inhibitor's binding is thought to change the shape of the
enzyme molecule, deforming its active site and preventing it from reacting with
its substrate. This sort of noncompetitive inhibition is known as allosteric
inhibition, and the allosteric site is where the inhibitor interacts with the enzyme.
Enzyme
Applications
• In the human body
Digestion would be impossible without enzymes.

Sugars and lipids are broken down by the enzymes
amylase and lipase in our saliva. Protease is a
digestive enzyme found in our stamach that aids in
the digestion of proteins. Potato starch molecules
are too large to be absorbed from the intestine, but
enzymes hydrolyze it into smaller molecules, which
can subsequently be taken to supply energy and
building blocks for the many organs.
• In nature
Herbivorous ruminants need tue cellulase (enzyme) produced by

the bacteria in their stomach to break down plant cellulose into
nutrients that they can ingest.
• In the food industry
Enzymes are frequently utilized in the food business as

processing aids in the manufacture of a wide range of goods,
including: dairy products incluee cheese, milk, and yoghurt;
bakery products include bread, cookies, and meat; beverages
include fruit juice, beer, and wine.
• In the technical industry
- Cleaning products.
Enzymes are crucial components of modern detergents because
they help to break down dirt and stains, resulting in better washing
results. They also contribute to environmental friendly products that
use less energy and have lower chemical burden
- Pulp and paper production.

Enzymes are used in pulp and paper manufacture to remove
ink, modify starches for paper applications, increase
bleaching, and soften tissues, among other things.
• In the technical industry
- Production of Ethanol
Ethanol has a wide range of uses, including beverages,
green chemicals, medicines, plastics, cosmetics, industrial
products (solvents, paint), and, increasingly, as a renewable
transportation fuel. In this scenario, it's referred to as
bioethanol. Fungal enzymatic techniques are used to create
bioethanol from biomass.
Thank You!

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COMPONENTS AND

• The ACTIVE SITE is the part of

In order for a cell to function properly it has to

Enzymes or also called “biological catalyst”,

Enzymes are not used up in reactions.

They can be used again for more reactions after

It only requires a minimal number of

Enzymes interact with substrates, which are chemical

With the use of their active sites, enzymes bind

Increasing the temperature of a

Each enzyme has a pH range where it works best.

The pH scale ranges from 1 to 14, with pH 7 being neutral,

To a certain extent, increasing the substrate concentration

As long as there is substrate available for binding,

As long as there is substrate available for binding,

Enzyme activity can be inhibited in a number of ways.

When molecules that are substantially similar to the

1.Happens when an inhibitor binds to the enzyme somewhere

Digestion would be impossible without enzymes.

Herbivorous ruminants need tue cellulase (enzyme) produced by

• In the food industry

Enzymes are frequently utilized in the food business as

- Pulp and paper production.

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