Understanding Enzymes:

Nature's Catalysts GROUP 3

Joanna Trish Velez
Jowe Varnal
 PRE-TEST
Direction: Read the question carefully and write the letter on a ¼
sheet of pad paper.

1. Proteins that act as biological catalyst.

a. Anino Acid
b. Enzymes
c. Enzyme Catalyst
d. All of the Above
 PRE-TEST

2. These are the example of what enzymes do?

a. DNA Replication
b. Liver Enzymes
c. Enzyme Catalyze
d. Both a and B
 PRE-TEST

3. These classification of enzymes facilitate the transfer of

functional groups between molecules?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 PRE-TEST

4. These classification of enzymes catalyze hydrolysis reactions,

where water is used to break chemical bonds?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 PRE-TEST

5. These classification of enzymes catalyze oxidation and reduction

reactions?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 PRE-TEST

6. These classification of enzymes catalyze the rearrangement of

atoms within a molecule to create isomers?

a. Transferases
b. Isomerase
c. Oxidoreduction
d. Ligases
 PRE-TEST

7. These classification of enzymes cleave chemical bonds by adding

or removing atoms without hydrolysis or redox reactions?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Lysase
 PRE-TEST

8. These classification of enzymes join two molecules together by

forming new covalent bonds, often using ATP as an energy source?

a. Transferases
b. Isomerase
c. Ligase
d. Ligases
 PRE-TEST

9. It is a region on the surface of an enzyme to which substrates will

bind atalyses a chemical reaction?

a. Substrate
b. Active Site
c. Enzymes
d. Ligases
 PRE-TEST

10. It is the environmental factors that can significantly influence

enzyme activity?

a. Ph
b. Temperature
c. Concentration Substrate
d. All of the Above
 PRE-TEST

11. It is reactions takes place by binding of the substrate with the

active site of the enzyme molecule by several weak bonds
a. Enzymatic reactions
b. Enzyme Reaction
c. Catalyst Rection
d. None of the Above
 PRE-TEST

12. These are cofactors tightly bound to an enzyme at all times.

a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 PRE-TEST

13. It binds to an enzyme only during catalysis. At all other times, it

is detached from the enzyme.
a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 PRE-TEST

14. It required at the active site to form coordinate bonds. Zinc is a

metal ion cofactor used by a number of enzymes.
a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 PRE-TEST

15. Inhibitors that do not enter the active site, but bind to another
part of the enzyme causing the enzyme to change its shape, which in
turn alters the active site.
a. Coenzymes
b. Competitive Inhibitor
c. Non-competitive Inhibitor
d. None of the Above
 PRE-TEST

16. These are chemicals that resemble an enzyme’s normal substrate

and compete with it for the active site.
a. Coenzymes
b. Competitive Inhibitor
c. Non-competitive Inhibitor
d. None of the Above
 PRE-TEST

17. The main components of the reaction are the enzyme, which is
present at very low quantities, and the molecule being acted on,
which is called the _______.
a. Substance
b. Substrate
c. Active Site
d. Enzyme
 PRE-TEST

18. This model assumes that the enzyme is a rigid three-dimensional

body.
a. Induce- Fit Model
b. Lock-and-Key Model
c. Three Dimensional Model
d. None of the Above
 PRE-TEST
19. American biochemist, Daniel Koshland introduce this model
which he compared the changes occurring in the shape of the cavity
upon substrate binding to the changes in the shape of a glove when a
hand is inserted.
a. Induce- Fit Model
b. Lock-and-Key Model
c. Three Dimensional Model
d. None of the Above
 PRE-TEST

20. In Enzyme Activity, the result if Reactant (1) + Intermediate

(Enzyme-Substrate Complex) → _______?
a. Intermediate
b. Product + Enzyme
c. Product
d. None of the Above
Understanding Enzymes: Nature's
Catalysts
 What is Enzymes?
Enzymes are proteins that act as catalysts in biological
reactions. They facilitate these reactions by lowering the
activation energy required for the reaction to occur.
Without enzymes, many biochemical reactions would not
occur at a sufficient rate to sustain life.
 WHAT DO ENZYMES DO?
Enzymes help speed up chemical reactions in the human body. They are
essential for respiration, digesting food, muscle and nerve function,
among thousands of other roles.

• The digestive system

• DNA replication
• Liver enzymes
Structure Of Enzymes
The structure of an enzyme is optimized for its specific function. Enzymes
have a three-dimensional structure that includes a specifically shaped active
site, where the substrate molecule binds. The active site and the substrate
have a complementary fit, often referred to as the lock-and-key model or the
induced fit model. This specificity allows enzymes to recognize and bind to
specific substrates, promoting selective reactions.
 Enzymes Classification
Oxidoreductases

Transferases

Hydrolases
6 MAJOR Classification
Enzymes
Lyases

Isomerases

Ligases
 Enzymes Classification
Oxidoreductases These enzymes catalyze
Transferases oxidation-reduction
reactions, transferring
Hydrolases
electrons from one
Lyases
molecule to another.
Isomerases

Ligases
 Enzymes Classification
Oxidoreductases

Transferases Transferases catalyze the

transfer of a groups of
Hydrolases
atoms, such as from
Lyases
molecule to another.
Isomerases

Ligases
 Enzymes Classification

Hydrolases catalyze
Hydrolases
hydrolysis reactions,
Lyases where water is used to
break chemical bonds.
 Enzymes Classification

Lyases cleave chemical

bonds by adding or
Lyases removing atoms without
hydrolysis or redox
reactions.
 Enzymes Classification

Isomerases catalyze the

Lyases
rearrangement of atoms
within a molecule to
Isomerases
create isomers.
 Enzymes Classification

catalyze the joining of two

Lyases
molecules together by
forming new covalent
bonds, often using ATP as
Ligases
an energy source.
tt

Cofactors
• Prosthetic groups: These are cofactors tightly bound to an enzyme at all times.
FAD (flavin adenine dinucleotide) is a prosthetic group present in many
enzymes.
• Coenzyme: A coenzyme binds to an enzyme only during catalysis. At all other
times, it is detached from the enzyme. NAD is a common coenzyme.
• Metal ions: For the catalysis of certain enzymes, a metal ion is required at the
active site to form coordinate bonds. Zinc is a metal ion cofactor used by a
number of enzymes.
tt

Enzymes Activity
• is a measure of how fast an enzyme is able to catalyze the reaction.
This can be defined in many ways, but one of the most common is to
measure the µmoles of product per time.
• The main components of the reaction are the enzyme, which is present
at very low quantities, and the molecule being acted on, which is
called the substrate.
tt

Enzymes Activity
• is a measure of how fast an enzyme is able to catalyze the reaction.
This can be defined in many ways, but one of the most common is to
measure the µmoles of product per time.
• The main components of the reaction are the enzyme, which is present
at very low quantities, and the molecule being acted on, which is
called the substrate.
 Concentration and Type of subrates
Enzymes have a saturation point where their
activity ceases once all enzymes are occupied by
substrate molecules. The velocity of enzyme
action increases with substrate addition, but the
velocity remains constant at this point. The type
of substrate also affects enzyme action, with
competitive inhibitors being chemicals that
compete with the enzyme's specific substrate.
tt

Temperature
Temperature affects enzyme activity because it changes the conformation
of the enzyme. In uncatalyzed reactions, the rate usually increases as the
temperature increases. Similarly, when the enzyme is at a low temperature,
an increase in temperature will cause an increase in the rate of reaction.
However, protein conformations are very sensitive to further temperature
changes. Once the optimal temperature is reached, any increase in
temperature alters the enzyme conformation. The substrate may then cease
to fit properly onto the changed enzyme surface, so the rate of reaction
actually decreases.
tt

Temperature and pH
Temperature and pH are critical environmental factors that can
significantly influence enzyme activity.
Enzymes require an optimum temperature and pH for their action.
The temperature or pH at which a compound shows its maximum
activity is called optimum temperature or optimum pH, respectively.
As mentioned earlier, enzymes are protein compounds. A
temperature or pH more than optimum may alter the molecular
structure of the enzymes. Generally, an optimum pH for enzymes is
considered to be ranging between 5 and 7.
 Mechanism of enzyme action

Enzymes are said to possess an active site. The active site is a part of the
molecule that has a definite shape and the functional group for the binding
of reactant molecules. The molecule that binds to the enzyme is referred to
as the substrate group. The substrate and the enzyme form an intermediate
reaction with low activation energy without any catalysts.
 Mechanism of enzyme action
Reactant (1) + Reactant (2) → product
Reactant (1) + Enzyme → Intermediate (Enzyme-Substrate Complex)
Intermediate + Reactant (2) → product + Enzyme

The basic mechanism of enzyme action is to catalyze the

chemical reactions, which begins with the binding of the
substrate with the active site of the enzyme. This active
site is a specific area that combines with the substrate.
 Lock-and-Key model
The Lock-and-Key model - his model assumes that the enzyme is a rigid
three-dimensional body. The surface that contains the active site has a
restricted opening into which only one kind of substance can fit, just as only
the proper key can fit exactly into a lock and turn open.
According to the lock-and-key model, an enzyme molecule has its particular
shape because that shape is necessary to maintain the active site in exactly
the conformation required for that particular reaction.
Lock-and-Key model
E-S Complex
 Induced-fit Model
Induced-fit model of American biochemist, Daniel Koshland, in which he
compared the changes occurring in the shape of the cavity upon substrate
binding to the changes in the shape of a glove when a hand is inserted. That is,
the enzyme modifies the shape of the active site to accommodate the substrate.
Recent experiments during actual catalysis have demonstrated that not only
does the shape of the active site change with the binding of substrate, but even
in the bound state, both the backbone and the side chains of the enzyme are in
constant motion.
INDUCE-FIT MODEL
 Inhibitors
An inhibitor is a molecule that reduces the activity of an
enzyme, and that are many different types seen in biochemistry.
Some inhibitors bind to the enzyme and then never let go,
essentially eliminating that enzyme molecule from being
productive. Such an inhibitor is an irreversible inhibitor. Most
inhibitors bind, and while bound reduce the activity; but they
can also unbind, restoring the activity to its initial level. These
are reversible inhibitors.
 Inhibitors
a. Competitive inhibitors: are chemicals that
compete with the specific substrate of the
active site
enzyme for the active site altered

Substrate
Enzyme
Competitive inhibitor
 Inhibitors
b. Noncompetitive inhibitors:
Inhibitors that do not enter the active site, but bind to another part
of the enzyme causing the enzyme to change its shape, which in
turn alters the active site.

Substrate Noncompetitive
Enzyme Inhibitor
active site
altered
tt

Active Site
•Enzymes are composed of long chains of
amino acids that have folded into a very
specific three-dimensional shape which
contains an active site.

• An active site is a region on the surface of

an enzyme to which substrates will bind and
catalyses a chemical reaction.
tt

Active Site
The perception of the active site as either a rigid cavity (lock-and-key
model) or a partly flexible template (induced-fit model) is an
oversimplification. Not only is the geometry of the active site
important, but so are the specific interactions that take place between
the enzyme surface and the substrate. To illustrate, we take a closer look
at the active site of pyruvate kinase. This enzyme catalyzes the transfer
of the phosphate group from phosphoenolpyruvate (PEP) to ADP, an
important step in glycolysis .
tt

Active Site

-
tt

Active Site
The active site of the enzyme binds both substrates, PEP and ADP. The
rabbit muscle pyruvate kinase has two cofactors, K+ and either Mn2+
or Mg2. The divalent cation is coordinated to the carbonyl and
carboxylate oxygen of the pyruvate substrate and to the glutamate 271
and aspartate 295 residues of the enzyme.
tt

Enzyme Regulation
1. Feedback Control is an enzyme regulation process in which
formation of a product inhibitors an earlier reaction in the sequence.
The reaction product of one enzyme may control the activity of
another, especially in a complex system in which enzyme work
cooperatively.
2. Zymogens these are the inactive forms of enzyme
tt

Enzyme Regulation
3. Allosterism these regulation takes place by means of an event that occurs at
a site other than the active sites, but that eventually affects the active site and
Allosteric Enzyme is the any enzyme regulated by this mechanism. If the
Substance binds noncovalently and reversibly to a site other than the active
site, it may effect the enzyme in either two ways: It may inhibit enzyme action
(negative modulation) or it may stimulate enzymes action (positive
modulation).The Substance that binds to an allosteric enzymes is call regulator,
and the site to which it binds is called a regulation site.
tt

Enzyme Regulation
4. Protein Modification is the one that control the activity of an enzymes. The
modification is usually a change in the primary structure, typically by addition
of a functional group covalently bound to the enzyme.
5. Isozymes – it is another type of regulation of enzyme activity occurs when
the same enzyme appears in different forms in different tissue,
 Enzymes in Medicine:
Enzymes play a significant role in medicine, both in diagnostics and
therapeutics. Diagnostic enzymes are used for the detection and
monitoring of diseases. For instance, various cardiac enzymes like
troponin and lactate dehydrogenase are commonly measured to
diagnose heart attacks. On the therapeutic front, enzyme
replacement therapies (ERT) are used to treat genetic enzyme
deficiencies. The review article by Parenti et al. (2015) provides
insights into the progress and challenges of enzyme replacement
therapy for lysosomal storage disorders.
 Enzymes in Medicine:
Enzymes are used in medicine in a variety of ways, including:
• As diagnostic tools: Enzymes can be used to diagnose diseases by measuring
their activity in blood or other tissues. For example, the enzyme creatine kinase is
elevated in the blood of people with heart attacks.
• As therapeutic agents: Enzymes can be used to treat diseases by replacing
missing enzymes or by catalyzing reactions that are beneficial to the body. For
example, the enzyme lactase is used to treat lactose intolerance by breaking down
lactose into glucose and galactose.
• As industrial catalysts: Enzymes are used in a variety of industrial processes,
such as the production of food and beverages, pharmaceuticals, and biofuels.
 Post-Test
Direction: Read the question carefully and write the letter on a ¼
sheet of pad paper.

1. Proteins that act as biological catalyst.

a. Anino Acid
b. Enzymes
c. Enzyme Catalyst
d. All of the Above
 Post-Test

2. These are the example of what enzymes do?

a. DNA Replication
b. Liver Enzymes
c. Enzyme Catalyze
d. Both a and B
 Post-Test

3. These classification of enzymes facilitate the transfer of

functional groups between molecules?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 Post-Test

4. These classification of enzymes catalyze hydrolysis reactions,

where water is used to break chemical bonds?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 Post-Test

5. These classification of enzymes catalyze oxidation and reduction

reactions?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Ligases
 Post-Test

6. These classification of enzymes catalyze the rearrangement of

atoms within a molecule to create isomers?

a. Transferases
b. Isomerase
c. Oxidoreduction
d. Ligases
 Post-Test

7. These classification of enzymes cleave chemical bonds by adding

or removing atoms without hydrolysis or redox reactions?

a. Transferases
b. Hydrolase
c. Oxidoreduction
d. Lysase
 Post-Test

8. These classification of enzymes join two molecules together by

forming new covalent bonds, often using ATP as an energy source?

a. Transferases
b. Isomerase
c. Ligase
d. Ligases
 Post-Test

9. It is a region on the surface of an enzyme to which substrates will

bind atalyses a chemical reaction?

a. Substrate
b. Active Site
c. Enzymes
d. Ligases
 Post-Test

10. It is the environmental factors that can significantly influence

enzyme activity?

a. Ph
b. Temperature
c. Concentration Substrate
d. All of the Above
 Post-Test

11. It is reactions takes place by binding of the substrate with the

active site of the enzyme molecule by several weak bonds
a. Enzymatic reactions
b. Enzyme Reaction
c. Catalyst Rection
d. None of the Above
 Post-Test

12. These are cofactors tightly bound to an enzyme at all times.

a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 Post-Test

13. It binds to an enzyme only during catalysis. At all other times, it

is detached from the enzyme.
a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 Post-Test

14. It required at the active site to form coordinate bonds. Zinc is a

metal ion cofactor used by a number of enzymes.
a. Coenzymes
b. Prosthetic Group
c. Metal Ions
d. None of the Above
 Post-Test

15. Inhibitors that do not enter the active site, but bind to another
part of the enzyme causing the enzyme to change its shape, which in
turn alters the active site.
a. Coenzymes
b. Competitive Inhibitor
c. Non-competitive Inhibitor
d. None of the Above
 Post-Test

16. These are chemicals that resemble an enzyme’s normal substrate

and compete with it for the active site.
a. Coenzymes
b. Competitive Inhibitor
c. Non-competitive Inhibitor
d. None of the Above
 Post-Test

17. The main components of the reaction are the enzyme, which is
present at very low quantities, and the molecule being acted on,
which is called the _______.
a. Substance
b. Substrate
c. Active Site
d. Enzyme
 Post-Test

18. This model assumes that the enzyme is a rigid three-dimensional

body.
a. Induce- Fit Model
b. Lock-and-Key Model
c. Three Dimensional Model
d. None of the Above
 Post-Test
19. American biochemist, Daniel Koshland introduce this model
which he compared the changes occurring in the shape of the cavity
upon substrate binding to the changes in the shape of a glove when a
hand is inserted.
a. Induce- Fit Model
b. Lock-and-Key Model
c. Three Dimensional Model
d. None of the Above
 Post-Test

20. In Enzyme Activity, the result if Reactant (1) + Intermediate

(Enzyme-Substrate Complex) → _______?
a. Intermediate
b. Product + Enzyme
c. Product
d. None of the Above
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