TAGUM CITY COLLEGE OF SCIENCE AND TECHNOLOGY FOUNDATION INC.

Elpidio M. Gazmen Compound, Gazmen Road, Tagum City

SEC. Reg. No. 200630691 / Tel. No. 216-6824
E-mail Address: [email protected]

Supplementary Learning
Materials for
Senior High School
Grade Levels: 12
Core Subject: General Biology 1
Semester: 1st semester

LEARNING COMPETENCY:

 Describe the components of an enzyme,

 Explain oxidation/reduction reactions,
 Determine how factors such as pH, temperature, and substrate affect
enzyme activity
 Enzymes

The cell is the structural and functional unit of life, the basic
building blocks of every living organism. In order for the cell to
perform its specific functions, it need a biocatalyst. A biocatalyst is a
substance that initiates or increases the rate of a chemical reaction.
One example of a biocatalyst is an Enzyme. Enzymes are biological
molecules (typically proteins) that significantly speed up the rate of
virtually all of the chemical reactions that take place within cells. This enzymes are
important for life and does serve wide range of functions in our body, such as aiding in
digestion and metabolism.

This unit will introduce about the structure and functions of enzymes.

In this module, you will learn about:

1. Enzymes;
2. Oxidation/ reduction reactions;
3. Factors affecting enzyme activity.

At the end of the module, you should be able to:

 Describe enzyme;
 Identify factors that affects enzyme activity; and
 Express the importance of enzymes.

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Direction: Read and understand each question carefully. Write TRUE if the statement is
correct and FALSE if the statement is wrong.

__________1. Enzymes can be defined as biological polymers that catalyze

biochemical reactions.
__________2. Ligases catalyzes the formation of an isomer of a compound.

__________3. Oxidoreductases catalyzes oxidation and reduction reactions.

__________4. The conditions of the reaction have a great impact on the activity of the
enzymes.
__________5. Temperature has no effect on the enzymes activity.

__________6. An optimum Ph level for enzymes is 3-4.

__________7. The modification of the rate of a chemical reaction, usually an

acceleration, by addition of a substance not consumed during the
reaction is called catalysis.
__________8. The basic mechanism of enzyme action is to catalyze the chemical
reactions.

__________9. Cofactors are non-proteinous substances that associate with enzymes.

__________10. Enzymes are the catalysts involved in biological chemical reactions.

Task 1: Lock and Key

Procedure: Find at least 2 Lock and Key in your house. Tyr each key on
the locks. Observe its mechanism. Write your observations on the space
provided.

1. _______________________________________________
2. _______________________________________________
3. _______________________________________________
4. _______________________________________________
5. _______________________________________________

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Task 2: The picture below is the explanation about how enzymes is related to lock and
key. Read and understand carefully the picture and answer the guide questions below.

1. How important Enzyme is?

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2. How enzyme affects the reaction?

________________________________________________________
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__________________________________

3. How will you describe the function of enzyme?

________________________________________________________
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What Are Enzymes?

“Enzymes can be defined as biological polymers that catalyze biochemical
reactions.”
Enzymes are life’s great facilitators. They create the conditions needed for
biochemical reactions to happen fast. The general name that chemists use for a
chemical entity that increases the speed of a reaction is a “catalyst.” Enzymes are

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biological catalysts--they catalyze the chemical reactions that happen inside living
things.

The definition of catalysis

Catalysis, in chemistry, the modification of the rate of a chemical reaction, usually
an acceleration, by addition of a substance not consumed during the reaction. The rates
of chemical reactions—that is, the velocities at which they occur—depend upon a
number of factors, including the chemical nature of the reacting species and the external
conditions to which they are exposed. A particular phenomenon associated with the
rates of chemical reactions that is of great theoretical and practical interest is catalysis,
the acceleration of chemical reactions by substances not consumed in the reactions
themselves—substances known as catalysts. Fundamentally, the peculiar phenomenon
of life would hardly be possible without the biological catalysts termed enzymes.

Enzymes Are Biological Catalysts

Enzymes are the catalysts involved in biological chemical reactions. They are the
“gnomes” inside each one of us that take molecules like nucleotides and align them
together to create DNA, or amino acids to make proteins, to name two of thousands of
such functions. They are so important for life that scientists weren’t satisfied with calling
them catalysts, and had to invent the fancy new name “enzyme” instead.

Enzyme Structure
Enzymes are a linear chain
of amino acids, which give rise to
a three-dimensional structure. The
sequence of amino acids specifies
the structure, which in turn
identifies the catalytic activity of
the enzyme. Upon heating,
enzyme’s structure denatures,
resulting in a loss of enzyme
activity that typically is associated
with temperature.
(Source:https://lh3.googleusercontent.com/proxy/ghLmzVa)
Compared to its substrates, enzymes are typically large with varying sizes. Only
a small section of the structure is involved in catalysis and are situated next to the
binding sites. The catalytic site and binding site together constitute the enzyme’s active
site. A small number of ribozymes exist which serves as an RNA-based biological
catalyst. It reacts in complex with proteins.

Enzymes Classification

(Source:https://cdn1.byjus.com/wp-content/uploads/2018/11/chemistry/2016/10/16074509/word-image2.png)

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 According to the International Union of Biochemists (I U B), enzymes are divided
into six functional classes and are classified based on the type of reaction in which they
are used to catalyze. The six kinds of enzymes are hydrolases, oxidoreductases,
lyases, transferases, ligases, and isomerases.
Listed below is the classification of enzymes discussed in detail:
Types Biochemical Property
The enzyme Oxidoreductase catalyzes the oxidation reaction
Oxidoreductase
where the electrons tend to travel from one form of a molecule to
s
the other.
The Transferases enzymes help in the transportation of the
Transferases
functional group among acceptors and donor molecules.
Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis
Hydrolases
reaction by adding water to cleave the bond and hydrolyze it.
Adds water, carbon dioxide or ammonia across double bonds or
Lyases
eliminate these to create double bonds.
The Isomerases enzymes catalyze the structural shifts present in a
Isomerases
molecule, thus causing the change in the shape of the molecule.
The Ligases enzymes are known to charge the catalysis of a
Ligases
ligation process.

Oxidoreductases
These catalyze oxidation and reduction reactions, e.g. pyruvate
dehydrogenase, catalysing the oxidation of pyruvate to acetyl coenzyme A.

Transferases
These catalyze transferring of the chemical group from one to another
compound. An example is a transaminase, which transfers an amino group from
one molecule to another.

Hydrolases
They catalyze the hydrolysis of a bond. For example, the enzyme pepsin
hydrolyzes peptide bonds in proteins.

Lyases
These catalyze the breakage of bonds without catalysis, e.g. aldolase (an
enzyme in glycolysis) catalyzes the splitting of fructose-1, 6-bisphosphate to
glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.

Isomerases
They catalyze the formation of an isomer of a compound. Example:
phosphoglucomutase catalyzes the conversion of glucose-1-phosphate to
glucose-6-phosphate (phosphate group is transferred from one to another
position in the same compound) in glycogenolysis (glycogen is converted to
glucose for energy to be released quickly).

Ligases
Ligases catalyzes the association of two molecules. For example, DNA
ligase catalyzes the joining of two fragments of DNA by forming a phosphodiester
bond.

Cofactors
Cofactors are non-proteinous substances that associate with enzymes. A
cofactor is essential for the functioning of an enzyme. An enzyme without a
cofactor is called an apoenzyme. An enzyme and its cofactor together constitute
the holoenzyme.
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 There are three kinds of cofactors present in enzymes:

 Prosthetic groups: These are cofactors tightly bound to an enzyme at all

times. A fad 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. Zn2+ is a metal ion cofactor used
by a number of enzymes.

Mechanism of Enzyme Reaction

Any two molecules have to collide for the reaction to occur along with the right
orientation and a sufficient amount of energy. The energy between these molecules
needs to overcome the barrier in the reaction. This energy is called activation energy.
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.

(Source: https://cdn1.byjus.com/wp-content/uploads/2018/11/Enzymes.png)

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.
Enzyme-Substrate Interactions
Enzymes are the biocatalysts with high molecular weight proteinous compound. It
enhances the reactions which occur in the body during various life processes. It helps
the substrate by providing the surface for the reaction to occur. The enzyme comprises
hollow spaces occupying groups such as -SH, -COOH, and others on the outer surface.
The substrate which has an opposite charge of the enzyme fits into these spaces, just
like a key fits into a lock. This substrate binding site is called the active site of an
enzyme (E).
The favorable model of enzyme-substrate interaction is called the induced-fit
model. This model states that the interaction between substrate and enzyme is weak,
and these weak interactions induce conformational changes rapidly and strengthen
binding and bring catalytic sites close enough to substrate bonds.

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 (Source:https://qph.fs.quoracdn.net/main-qimg-646ec2d2b6c5513ac41064962d00d9ea)

Action and Nature of Enzymes

Once substrate (S) binds to this active site, they form a complex (intermediate-
ES) which then produces the product (P) and the enzyme (E). The substrate which gets
attached to the enzyme has a specific structure, and that can only fit in a particular
enzyme. Hence, by providing a surface for the substrate, an enzyme slows down the
activation energy of the reaction. The intermediate state where the substrate binds to
the enzyme is called the transition state. By breaking and making the bonds, the
substrate binds to the enzyme (remains unchanged), which converts into the product
and later splits into product and enzyme. The free enzymes then bind to other
substrates, and the catalytic cycle continues until the reaction completes.
The enzyme action basically happens in two steps:
Step1: Combining of enzyme and the reactant/substrate.
E+S → [ES]
Step 2: Disintegration of the complex molecule to give the product.
[ES]→E+P
Thus, the whole catalyst action of enzymes is summarized as:
E + S → [ES] → [EP] → E + P

(Source:https://cdn1.byjus.com/wp-content/uploads/2018/11/ENZYME-ACTION.png)
Factors Affecting Enzyme Activity
The conditions of the reaction have a great impact on the activity of the enzymes.
Enzymes are particular about the optimum conditions provided for the reactions such as
temperature, pH, alteration in substrate concentration, etc.
Typically, enzyme activities are accelerated with increasing temperatures. As
enzymes are functional in cells, the feasible conditions for nearly all enzymes are
temperatures that are moderate. At higher temperatures, given a specific point, there is
a drastic decrease in the activity with the denaturation of enzymes. In diluted solutions,
purified enzymes denature quickly compared to enzymes in crude extracts.
Denaturation of enzymes can also take place when enzymes are incubated for long
durations. More appropriate is to utilize a shorter time duration when it comes to
incubation time to gauge the starting velocities of such enzyme reactions.
The International Union of Biochemistry suggests the standard assay
temperature to be 30 °C. Almost all enzymes are extremely sensitive to pH change. Just
some enzymes feasibly operate with pH above 9 and below 5. Most enzymes have their
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pH – optimum near to neutrality. Any alteration of pH causes the ionic state of amino
acid residues to change in the whole protein and in the active site. The modifications in
the ionic state can modify catalysis and substrate binding. The preference of substrate
concentration is critical as at lower concentrations, the rate is driven by concentration,
however, at high concentrations, the rate does not depend on any increase in the
concentration of the substrate.
Active site
Enzymatic catalysis depends upon the activity of amino acid side chains
assembled in the active center. Enzymes bind the substrate into a region of the
active site in an intermediate conformation.

Temperature and pH
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.

(Source:https://cdn1.byjus.com/wp-content/uploads/2018/11/ENZYME-TEMPERATURE-AND-PH.png)

Concentration and Type of Substrate

Enzymes have a saturation point, i.e., once all the enzymes added are
occupied by the substrate molecules, its activity will be ceased. When the
reaction begins, the velocity of enzyme action keeps on increasing on further
addition of substrate. However, at a saturation point where substrate molecules
are more in number than the free enzyme, the velocity remains the same.
The type of substrate is another factor that affects the enzyme action. The
chemicals that bind to the active site of the enzyme can inhibit the activity of the
enzyme and such substrate is called an inhibitor. Competitive inhibitors are
chemicals that compete with the specific substrate of the enzyme for the active
site. They structurally resemble the specific substrate of the enzyme and bind to
the enzyme and inhibit the enzymatic activity. This concept is used for treating
bacterial infectious diseases.

Functions of Enzymes
The enzymes perform a number of functions in our body. These include:

1. Enzymes help in signal transduction. The most common enzyme used in the
process includes protein kinase that catalyzes the phosphorylation of proteins.
2. They breakdown large molecules into smaller substances that can be easily
absorbed by the body.
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 3. They help in generating energy in the body. ATP synthase is the enzymes
involved in the synthesis of energy.
4. Enzymes are responsible for the movement of ions across the plasma
membrane.
5. Enzymes perform a number of biochemical reactions, including oxidation,
reduction, hydrolysis, etc. to eliminate the non-nutritive substances from the
body.
6. They function to reorganize the internal structure of the cell to regulate cellular
activities.

Examples in Everyday Life

Enzymes impact everyday life. For example, enzymes found in laundry
detergents help degrade stain-causing proteins, while lipases help dissolve fat stains.
Thermotolerant and cryotolerant enzymes function in extreme temperatures, and are
consequently useful for industrial processes where high temperatures are required or
for bioremediation, which occur under harsh conditions, such as those in the Arctic.
In the food industry, enzymes convert starch to sugar, in order to make
sweeteners from sources other than sugarcane. In the clothing industry, enzymes
reduce impurities in cotton and depress the need for potentially harmful chemicals used
in the leather tanning process.
Lastly, the plastics industry continually seeks ways of using enzymes to develop
biodegradable products.

Task 4: Essay. Read and answers each question. Write your answers on the
space provided.
1. Explain the mechanism of enzyme?
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2. What are the factors affecting enzyme? Explain each factors.
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3. Describe the shape of an enzyme?

________________________________________________________________
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4. What are the different types of enzyme? Explain each type.

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5. How important enzymes is?

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 ________________________________________________________________
_____________________________________________________

I have learned that ________________

______________________.

I have realized that ________________

______________________.

I will apply _____________________________________________.

Task 6. Identification. Read each questions carefully and write your answers on the
space provided.

__________1. The energy between these molecules needs to overcome the barrier in
the reaction. ACTIVATION ENERGY
__________2. Enzymes are a linear chain of amino acids, which give rise to a three-
dimensional structure. ENZYME STRUCTURE
__________3. Is a part of the molecule that has a definite shape and the functional
group for the binding of reactant molecules? ACTIVE SITE
__________4. These catalyze oxidation and reduction reactions. OXIDOREDUCTASES
__________5. __________ enzymes are known to charge the catalysis of a ligation
process. LIGASES
__________6. These are cofactors tightly bound to an enzyme at all times.
PROSTHETIC GROUPS
__________7. These catalyze the breakage of bonds without catalysis. LYASES
__________8. Are chemicals that compete with the specific substrate of the enzyme for
the active site? COMPETETIVE INHIBITOR
__________9. Binds to an enzyme only during catalysis. COENZYME
__________10. Defined as biological polymers that catalyze biochemical reactions.
ENZYMES

Glossary
Concentration Is the ratio of solute in a solution to either solvent or total
solution.
Solute Is the substance that is being dissolved.
Solvent Is the dissolving medium.

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