ROLES OF ENZYMES IN

METABOLIC REACTIONS
Presented by:
Ayesha Naaz, Aliza Shabnam, Vidhi Sindoor, Uma Naicker and Prakriti Narayan.
 CONTENT
RECAP ROLES OF ENZYMES
• History of Enzymes • Metabolic reactions
• Introduction to enzymes? • Anabolic and catabolic reactions
• Parts of an enzyme • ATP
• How enzymes work? • The Kalvin cycle
• The two models of substrate binding • Glycolysis
• Factors affecting enzyme activities
• Types of enzymes
• The 6 categories of enzymes
• Roles of enzymes
 HISTORY OF ENZYMES
• A French chemist named Anselme Payen was the first person to discover enzymes in
1833 and named them diastase.

• Few decades later, a man named Louis Pasteur made a discovery while studying the
fermentation of sugar to alcohol by yeast. He found that there is an essential force, which
he named ferments, that works only within living organisms.

• In 1878, a German physiologist, named Wilhelm Kuhne was the first to use the name
enzyme.

• They were able to demonstrate that the enzyme is not life but a large biomolecule made
of amino acids, which behavesss as catalysts in the functioning of a cell.
INTRODUCTION TO ENZYMES
• Enzymes are simply globular proteins that act
as biological catalysts to help speed up
chemical reactions in the cell.
• These cells contain hundreds of different types
of enzymes each specific to a certain chemical
reaction.
• The enzymes are not destroyed during a
chemical reaction, rather are used over and over
again.
 PARTS OF AN ENZYME

• Consists of an active site mostly composed of 10 to

12 amino acids which comes closer to each other
through the folding of the polypeptide chain.
• The active site is responsible for engaging the
substrate for enzyme action during enzyme
catalysis.
• There are 2 types of active site:
•1. Binding site- identifies substrate and aids in
binding the inhibitor.
•2. Catalytic site- when engaged, helps to
catalyze.
 PARTS OF AN ENZYME- CONT’D
• There is also the cofactor which facilitates in the enzyme-
substrate binding.
• Up to 90%of the cofactor is composed of amino acids while
the remaining 10% includes non-proteinous molecules.
• In these kinds of enzymes, the proteinous parts are called
apoenzymes and the non- proteinous parts are known as
cofactors.
• Apoenzymes are inactive until bound with a cofactor.
• Apoenzyme- cofactor complex is known as holoenzyme, a
functional enzyme.
• Cofactor is important for the catalytic activities of
holoenzymes.
 COFACTOR AND COENZYME
• A coenzyme is small, organic, non-protein
molecule that carries chemical groups between
enzymes, while a cofactor is an inorganic, non-
protein chemical compound that tightly and
loosely binds with an enzyme or protein
molecule.
• A coenzyme is loosely bound to the enzyme
while a cofactor is covalently bound with the
enzyme.
• A coenzyme is required for enzymatic activities
while cofactor is not.
• All coenzymes are cofactors, but not all cofactors
are coenzymes.
• A cofactor facilitates enzymatic reactions but is
not required.
HOW ENZYMES WORK?
THE MODELS OF SUBSTRATE
BINDING
 1. LOCK & KEY MODEL

• This model explains the theory of enzyme

action.
• This model shows how the active site of the
enzyme is specifically structured to fit a
certain substrate.
• Once substrate is bound to the active site,
the enzyme facilitates the reaction and
releases the reaction products.
 2. INDUCED
FIT MODEL

• In this model, both the

substrate and active site
changes their initial shape
once bound together to
accommodate for an ideal fit
for catalysis.
CLASSIFICATIONS OF
ENZYMES
THE 6 MAIN CLASSIFICATIONS OF ENZYMES
INCLUDE:
1. Oxidoreductases
2. Transferases
3. Hydrolases
4. Lyases
5. Isomerases
6. Ligases
 OXIDOREDUCTASES

These are enzymes that help carry out redox

reactions. They help transfer electrons to an
acceptor molecule from a donor molecule.

An example of enzyme oxidoreductases

includes cytochrome C oxidase, which is an
enzyme responsible for the reduction of
oxygen to water in the respiratory electron
transport chain.
 TRANSFERASES

An enzyme that helps to transfer functional

groups from one molecule to another.

An example of transferases includes

hexokinase, an enzyme that aids in the
transfer of a phosphate group from ATP to
glucose in the glycolytic pathway, forming
glucose-6-phosphate.
 HYDROLASES

Enzyme that aids in the catalysis of

hydrolysis reactions.

An example of hydrolases may include

lipases. It is the enzyme that during
digestion breaks down fats into fatty acids
and glycerol.
 LYASES

Are enzymes that catalyze the breaking

of chemical bonds in ways other than
oxidation or hydrolysis, after the
formation of double bonds or ring
structures.

An example of lyases is enzyme

fumarase. This enzyme converts
fumarate to malate by adding water
molecule in the citric acid cycle
 LIGASES

Ligases are enzymes that join two

molecules together. They catalyze
reactions through breaking of a
pyrophosphate bond in ATP and similar
compounds.

The best example of ligases enzyme is

DNA ligase. Which is an enzyme that
aids in DNA replication whereby it
connects two DNA fragments with a bond
forming between them.
 This enzyme catalyzes
isomerization changes of a
molecule.
An example of this enzyme
may include phosphoglucose
isomerase. This enzyme aids
in the process of glycolysis

ISOMERASES and gluconeogenesis by

interconverting fructose-6-
phosphate and glucose-6-
phosphate.
SUMMARY TABLE
EFFECTS OF PH BALANCE AND
TEMPERATURE ON ENZYME
ACTIVITY
 1. pH effect on ionization of active site:

Enzyme activity is affected by pH changes as it alters the ionization state of the

chemical groups in enzyme and substrate.

2. pH effect on denaturing of enzymes:

PH BALANCE Extreme pH levels disrupts the ionic interactions of amino acid side chains which are
needed for the maintenance of the protein’s catalytic structure, causing the enzymes
to denature.

3. Variable pH optimum:

This refers to the different optimum pH levels of enzymes in which they work best
e.g. pepsin, enzyme found in stomach functions best at a pH level of 2, where
enzymes of neutral or basic pH would not work.
 With increase in temperature, there is an increase in
enzyme activity due to faster molecular movement.
However, at a much higher temperature, enzymes tend to
denature, losing both their structure and their function.

TEMPERATUR Denaturation leads to a decreased reaction velocity as the

active site of the enzyme cannot effectively bind to the
substrate anymore.
E MODULATIONS
Therefore, even though increase in temperature enhances
enzyme activity, further elevations may lead to enzyme
denaturation.
ENZYMES IN METABOLIC
PROCESSES
INTRODUCTION TO METABOLIC PROCESSES
• Metabolic processes also known as metabolic pathways refers to all the chemical processes
or reactions happening in a living cell that are essential for life.
• Metabolic reactions = catabolic reactions + anabolic reactions.
 ANABOLIC REACTIONS

• Anabolic reactions refers to reactions responsible in the building of or assembling

of complex molecules from simpler molecules, for example protein synthesis
from amino acids.
• Anabolic reactions require energy (energy in this context refers to ATP, the
cellular unit of energy).
• Any reaction that requires energy is known as endergonic reactions
 CATABOLIC REACTIONS

• Catabolic reactions refers to reactions that responsible in the breaking down of

large, complex molecules into simpler molecules, such as sugar breakdown
during cellular respiration.
• Catabolic reactions release energy.
• Any chemical reaction that releases energy is termed as exergonic reactions.
THE METABOLIC PATHWAYS
 ATP (ADENOSINE TRIPHOSPHATE)
• ATP is the unit of energy used by cells.
• ATP is a nucleotide consisting of a ribose sugar, adenine base, and three phosphate
groups.
• It contains chemical energy in its phosphate group bonds, so as the bond breaks and the
phosphate ion releases from ATP, energy is released along with it.
• The remaining molecule is adenosine diphosphate (ADP).
• Through the means of cellular respiration, ADP can be re-phosphorylated to form ATP.
• The ATP and ADP molecules cycle within the cells, donate and receive phosphate ions as
they move along between exergonic and endergonic reactions.
• ATP can be thought of as nature’s rechargeable chemical battery whereby ADP is in the
‘flat’ state and ATP is the ‘charged’ state.
 THE CALVIN CYCLE
• This is a light, independent photosynthesis stage that builds carbohydrates. Since this
process requires energy to both molecules, it can be termed as an example of an endergonic
and anabolic process.
• The calvin cycle takes place after energy from sun is captured to be converted to ATP and is
catalyzed (sped up) by the enzyme rubisco.
 Step 1:

A five-carbon sugar ribose biphosphate or rubp is combined by

rubisco with carbon dioxide.

Three carbon dioxide (CO2) molecules are combined with the rubp
STEPS molecules.

INVOLVED IN This results in a very unstable compound that splits itself in half
THE CALVIN forming six, 3-carbon molecules known as 3-phosphoglycerate
acid or 3-pga

CYCLE
This process converts the CO2 molecule into organic compounds by
living organisms.

This whole process is known as carbon fixation.

 Step 2:

In this stage ATP ( adenosine triphosphate) and NADPH, converts

the six molecules of 3-phosphoglycerate acid from stage 1, into a
different3-carbon compound, glyceraldehyde-3-phosphate (g3p).

CONT’D One of these glyceraldehyde-3-phosphate molecules exits the kalvin

cycle and is used as the starting material for the synthesis of other
organic compounds like glucose (C6H12O6), or other
carbohydrates.

This whole process is known as reduction.

 Step 3:

In this stage the remaining glyceraldehyde-3-

phosphate molecules which are now five
glyceraldehyde-3-phosphate molecules, are
recycled into rubp and the cycle repeats.
CONT’D
This whole process is called regeneration of rubp.

It takes six turns of the cycle to synthesize one

glucose molecule.
 GLYCOLYSIS
• Living organisms undergo cellular respiration, which is a metabolic process, for them to be
able to use the chemical energy derived from carbohydrates.
• Glycolysis is the first step of cellular respiration. It is the process whereby glucose is broken
down in to two pyruvate molecules, a 3-carbon compound, in order to produce energy.
• Since energy is produced, it is considered as a catabolic pathway which is exergonic.
• Glycolysis has a straight pathway unlike the calvin cycle which means that the products of
the process do not return to form reactants.
• The process of glycolysis has many steps, and each step is catalyzed by a different enzyme.
 CONT’D

• The first half of the glycolysis pathway is endergonic as it takes in two ATP molecules
(energy), but the second half of the glycolysis pathway synthesizes four ATP molecules
making it exergonic.
• However, since two ATP molecules are used up and four ATP molecules are synthsized, the
net change in ATP is two ATP produced making this pathway an overall energy producing i.e
exergonic pathway.
THANK YOU FOR
LISTENING
QUIZ
QUESTION:

• Classify the following as either catabolic or anabolic reaction:

1. protein synthesis
2. Food digestion
3. DNA replication
4. Muscle creation
5. Breakdown of stored fats
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 REFERENCES CONT’D
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