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 
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Redeveloped Division Initiated Self-Learning Module

Department of Education – Division of Palawan

i
Biology 1 – Grade 12
Redeveloped Division Initiated - Self-Learning Module
Quarter 1 – Module 8: Enzymes
Second Edition, 2021

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Published by the Department of Education, Division of Palawan

Schools Division Superintendent:
Roger F. Capa, CESO VI
OIC - Assistant Schools Division Superintendents:
Rufino B. Foz
Arnaldo G. Ventura

Development Team for

Development Team
Redevelopment Activity

Writer: David S. Castor Jr. Writer: Rinaly D. Pacanza

Editors: Josie Joshua R. Pasion Editors: Maribeth Q. Adier
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Rosalyn C. Gadiano Maribeth Q. Adier
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Rosalyn C. Gadiano
Rodgie S. Demalinao

Department of Education – MIMAROPA Region – Division of Palawan

Office Address: PEO Road, Barangay Bancao-Bancao, Puerto Princesa City
Telephone: (048) 433-6392
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Website: www.depedpalawan.com

ii
Introductory Message
This Self-Learning Module (SLM) is prepared so that you, our dear learners, can
continue your studies and learn while at home. Activities, questions, directions,
exercises, and discussions are carefully stated for you to understand each lesson.

Each SLM is composed of different parts. Each part shall guide you step-by-step as
you discover and understand the lesson prepared for you.

Pre-tests are provided to measure your prior knowledge on lessons in each SLM. This
will tell you if you need to proceed on completing this module or if you need to ask
your facilitator or your teacher’s assistance for better understanding of the lesson. At
the end of each module, you need to answer the post-test to self-check your learning.
Answer keys are provided for each activity and test. We trust that you will be honest
in using these.

In addition to the material in the main text, Notes to the Teacher are also provided to
our facilitators and parents for strategies and reminders on how they can best help
you on your home-based learning.

Please use this module with care. Do not put unnecessary marks on any part of this
SLM. Use a separate sheet of paper in answering the exercises and tests. And read the
instructions carefully before performing each task

If you have any questions in using this SLM or any difficulty in answering the tasks in this
module, do not hesitate to consult your teacher or facilitator.

Thank you.

iii
 Biology 1
First Quarter Enzymes
Week 7

MELCs:
1. Describe the components of an enzymes. STEM_BIO 11/12-Ii-j-17
2. Explain oxidation/reduction reactions. STEM_Bio 11/12-Ii-j-18:
3. Determine how factors such as pH, temperature, and substrate affect
enzyme activity. STEM_Bio 11/12-Ii-j-19

Objectives:
1. To describe the components of an enzymes.
2. To explain oxidation/reduction reactions happen in an enzyme.
3. To determine how factors such as pH, temperature, and substrate affect
enzyme activity.

What I Know

Directions: Choose the letter of the best answer. Write the chosen letter on a separate
sheet of paper.

1. These are organic or biological catalysts.

A. Carbohydrates C. Enzymes
B. Lipids D. Nucleic acid

2. Enzymes are mostly _________________.

A. Proteins C. Nucleic acids
B. Carbohydrates D. Lipids

3. Enzymes are mostly made up of monomers called _________________.

A. Fatty acids C. Phospholipids
B. Monosaccharides D. Amino acids

4. Chemical reactions are hasted by enzymes through ___________________.

A. Increasing the temperature
B. Lowering the temperature
C. Increasing the activation energy
D. Lowering the activation energy

1
5. Without enzymes, the reactions necessary in a living system would require
_________________________ in order to occur.
A. a greater amount of substrates C. larger protein molecules
B. high temperatures D. greater surface area

6. The substrate binds to the part of an enzyme called ____________________.

A. Cofactor B. Coenzyme C. Active site D. Apoenzyme

7. Some people are “lactose intolerant”. Which of the following enzyme do they lack?
A. Maltase B. Lactase C. Hydroxylase D. Amylase

For questions 8 – 10 refer to the illustration below.

8. Which of the following represents the substrates?
A. A B. B C. C D. D

9. Based on the picture which letter illustrates the enzyme?

A. A B.B C. C D.D

10. The by-product of the reaction is represented by letter _____.

A. A B. B C. C D. D

11. It is an unstable state that happens when reactants absorb energy from their
surroundings.
A. Transmission state C. Transformation State
B. Transition state D. Transfer state

12. These are nonprotein helpers for catalytic activity, usually are inorganic, such as
the metal atoms zinc, iron, and copper.
A. Temperature B. pH C. Cofactors D. Enzyme inhibitor

13. Why do enzymes need to be in optimal conditions?

A. To correct the arrangement of amino acids
B. To allow the bonding between amino acids
C. To favor the most active shape for the enzyme
D. To denature the enzyme

14. These are chemicals or compounds that resemble the normal substrate
molecule and compete for admission into the active site.
A. Temperature C. Cofactors
B. pH D. Enzyme inhibitors

For question 15 refer to the illustration.

15. How do we increase the reaction rate based

on the picture?
A. By adding more substrates
B. By removing excess substrates
C. By increasing the number of enzymes
D. By decreasing the number of enzymes

2
 What is It
1. Components of an Enzymes

Enzymes or enzymatic proteins are organic or biological catalysts that are

essential to living organisms especially to us, humans. It regulates the metabolism or the
processes that occur in the body. It acts as a catalyst, substances that speed up a
reaction without being used up, destroyed, or incorporated into the end product. Many
enzymes are proteins but there are also RNA enzymes or ribozymes. In this lesson, we will
focus on enzymatic proteins.

Enzyme Structure

Protein structure such as in an enzyme can be presented in four ways. Enzymes

are made up of amino acids (there are twenty-one (21) different amino acids) that are
linked together through peptide bonds. This results in a polypeptide chain. This is the
primary structure. The order of the amino acids in the polypeptide chain is derived from
the gene it is transcribed from. Different enzymes have different series of amino acids.
Thus, performs a different function.

In the secondary structure, the

amino acids can interact with each
other and form a hydrogen bond
through the hydrogen atom in the
amino group (NH2) and the oxygen
atom in the carboxyl group (COOH).

This results in the chain folding;

the protein chain can fold in two
ways. The α-helix, where the chain
wraps around or the β-sheet in which
the chain folds on top of itself.

The protein could further fold

up due to the bonds between the
side chains (R groups) of the various
amino acids forming a three-
dimensional structure. This is the
proteins’ tertiary structure. Image Credit: https://rsscience.com/eukaryote-prokaryote/

Since some proteins are consisting of two or more polypeptide chains, the
quaternary structure is the aggregation of the different polypeptide units. This is the
overall protein structure.

3
 Enzymes have different parts which are the:

1. Apoenzyme – protein portion of the enzyme

consisting of amino acid chains.
2. Cofactor – a non-protein component that
activates the enzyme.
3. Coenzyme – chemically different to cofactor
but is also an organic non-protein compound
that binds with an enzyme.
4. Holoenzyme – A cofactor and apoenzyme
conjugated together.
Figure 1.7: Parts of an Enzyme
Image Credit:
https://www.slideshare.net/AliaNajiha1/micr
obphysio4
Enzyme Function

The enzyme’s substrate is the reactant an enzyme acts on. The two bind together
forming an enzyme-substrate complex. There are cases when there are two or more
reactants that bind to the enzyme. Catalytic action takes place while the enzyme and
substrate are joined which converts the substrate to the product (or products) of the
reaction. A summarized process is shown below:

𝐸𝑛𝑧𝑦𝑚𝑒 + 𝑆𝑢𝑏𝑠𝑡𝑟𝑎𝑡𝑒(𝑠) ⇌ 𝐸𝑛𝑧𝑦𝑚𝑒 𝑆𝑢𝑏𝑠𝑡𝑟𝑎𝑡𝑒 𝐶𝑜𝑚𝑝𝑙𝑒𝑥 ⇌ 𝐸𝑛𝑧𝑦𝑚𝑒 + 𝑃𝑟𝑜𝑑𝑢𝑐𝑡(𝑠)

The names of most enzymes end in –ase. Usually, the name of the substrate then
the suffix. An example of this is the enzyme sucrase which catalyzes the hydrolysis of the
substrate sucrose. The disaccharide sucrose is broken down into its monosaccharide
components, glucose and fructose. Which is shown below:

𝑆𝑢𝑐𝑟𝑎𝑠𝑒 + 𝑆𝑢𝑐𝑟𝑜𝑠𝑒 + 𝐻2 𝑂 ⇌ 𝑆𝑢𝑐𝑟𝑎𝑠𝑒 − 𝑠𝑢𝑐𝑟𝑜𝑠𝑒 − 𝐻2 𝑂 𝑐𝑜𝑚𝑝𝑙𝑒𝑥

⇌ 𝑆𝑢𝑐𝑟𝑎𝑠𝑒 + 𝐺𝑙𝑢𝑐𝑜𝑠𝑒 + 𝐹𝑟𝑢𝑐𝑡𝑜𝑠𝑒

The specific region of the enzyme where the substrate binds and the catalytic
reaction happens is called the active site. It is like a pocket or groove in the enzyme
which is determined by its components that serves as the framework to its shape.
Complementary fit between the shape of the enzyme’s active site and the shape of the
substrate is where the specificity of an enzyme is attributed. Meaning a substrate will only
fit to its specific enzyme.

When the substrate binds and tightens in the active site of the enzyme after the
initial contact, it is called induced fit. By bringing the chemical groups of the active site
into position, the ability of the enzyme to catalyze the chemical reaction enhances.
Enzymes work by lowering the activation energy (EA) of the reaction process. This is the
energy needed for the reaction to occur. How this process takes place will be discussed
in the next lesson.

In our digestive system enzymes play a vital role in the digestion of the food we
eat. Aside from that, enzymes also facilitate the processes that correspond to the growth
and development of an organism such as cellular respiration, DNA replication, and the
like.

4
2. Oxidation and Reduction Reactions

Chemical reactions involve the breaking and forming of bonds in a molecule

which leads to the creation of new products. In facilitating reactions in the cell, enzymes
play a vital role. It is capable of contorting the molecule into a highly unstable state that
lowers the activation energy needed for the reaction to take place. Activation energy,
also known as free energy of activation, is often abbreviated as EA; it is the initial
investment of energy to start a reaction.
When molecules absorb enough energy from the surrounding environment it
reaches an unstable state which also called the transition state. It is often the thermal
energy present in the surrounding environment that is absorbed by the molecules. When
reactant molecules absorb thermal energy or heat, this causes them to collide more
frequently and more forcefully. Thus, agitates the atoms in the molecules that result in
the breaking of bonds.
The reaction ends with the forming of new bonds of the product molecules, the
release of heat, and molecules returning to stable shapes with a lower amount of
energy. This results in an overall decrease in free energy symbolized by∆𝐺.
These reactions are often called redox reactions. It involves the passing of
electrons from one molecule to another. In biological systems, these reactions are
present such as in photosynthesis and cellular respiration which are the essential
processes for the existence of most life forms here on our planet.
Oxidation in terms of electron transfer is when there is the loss of an electron from
one element or molecule. While reduction is the gain of electrons. Using the mnemonic
“OIL RIG” you can easily remember the difference between them. It means oxidation is
loss and reduction is gain. The oxidizing agent is the species doing the oxidizing or it
remove electrons. While the reducing agent is the species doing the reducing or it loses
an electron to an electron recipient.
Let us have an example, hydrogen react with fluorine to produce hydrogen
fluoride.
H2 + F2 → 2HF
In this reaction, oxidation is the loss of electron by hydrogen (H 2).
H2 → 2H+ + 2e-
While reduction is the gain of electron by fluorine (F2)
F2 + 2e- → 2F-
In the overall reaction, hydrogen is oxidized, and acts as the reducing agent.
While, fluorine is reduced, and acts as the oxidizing agent.

Knowing the oxidation number of the element in a compound will help us identify
which element is being reduced and oxidized.

5
 The oxidation number is a number that is assigned to an element in a compound
that denotes the electrons lost or gained by the atom in a compound. For binary ionic
compound, the ionic charge is equivalent to the oxidation number. For covalent
compounds or polyatomic ions, the oxidation number is less obvious and can be
determined by a given set of rules.

The rules for assigning an oxidation number is given below:

1. For an atom in its elemental form like sodium (Na), and oxygen gas (O2) the
oxidation number is equal to 0.
2. For a monatomic ion, the oxidation number is equal to the ion charge.
3. The sum of oxidation number values for the atoms in a molecule or formula
unit of a compound equals to zero (equals to the ion’s charge if it is a
polyatomic ion).

These are the rules for specific atoms or periodic table groups (A periodic table
of elements is available at the end of this module):
1. For Group 1A (1), the oxidation number is equal to +1 in all compounds.
2. For Group 2A (2), the oxidation number is equal to +2 in all compounds.
3. For Hydrogen, the oxidation number is equal to +1 in combination with
nonmetals. While, -1 in combination with metals and boron.
4. For Fluorine, the oxidation number is equal to -1 in all compounds.
5. For Oxygen, the oxidation number is equal to -1 in peroxides. While, -2 in all
other compounds (except with F).
6. For Group 7A (17), the oxidation number is equal to -1 in combination with
metals, nonmetals (except O), and other halogens lower in the group.

For example, let us determine the oxidation number of each element present in
the compound calcium oxide (CaO), commonly known as quicklime.

Following the given rules:

Ca, calcium belongs to Group 2A (2); thus, its oxidation number is +2. While O or
oxygen has an oxidation number of -2.
Another example, potassium nitrate (KNO3)
Following the given rules:
K or potassium belongs to Group 1A (1); thus, its oxidation number is +1. While O
or oxygen has an oxidation number of -2. In determining the oxidation number of
nitrogen, since that it is not mentioned in the rules, we must assume that the compound
has a sum of oxidation number values equal to 0. Then, determine it through the
oxidation numbers of other elements in the compound.
N=?
K = +1
O = 3(-2) There are three atoms of oxygen in the compound.

Assume, 0 – (+1) – 3(-2) = +5

Through subtracting the determined oxidation numbers of the other elements in
the compound to 0, we determined that the oxidation number of nitrogen is equal to
+5.

6
 Oxidation number can also be used to identify the reducing or oxidizing agent in
the reaction. For example, in the production of water or H 2O.

Oxygen was reduced since that its oxidation number changed from 0 to -2. While
hydrogen was oxidized because its oxidation number changed from 0 to +1. Oxygen
gas is the oxidizing agent. While hydrogen gas is the reducing agent.

3. Factors Affecting Enzyme Activity

1. Effects of Temperature and Ph

Temperature and pH are important environmental factors in the activity of

enzymes. Up to a certain point, the relationship between temperature and enzymatic
reaction increases as the other variable also increases. This is partly due to the effect of
temperature on the molecules in the reaction, with increasing temperature the substrate
collides with the active sites more frequently. However, above the optimal temperature,
enzymatic reaction drops sharply. The heat affects the bonds and other weak
interactions in the enzyme that stabilize the active site of the enzyme, which will lead to
the denaturalization of it.

Figure 3.1: Environmental Factors affecting Enzyme Activity

Image Credit: https://botnam.com/enzymes/

Optimal temperature differs from enzyme to enzyme at which reaction rate is

greatest. This allows the greatest molecular collisions and the conversion of the reactants
to product molecules. The optimal temperature for most human enzymes ranges from
35℃ − 40℃. Which is close to the human body temperature. Other organisms such as the
thermophilic bacteria that live in hot springs have enzymes with optimal temperatures of
70℃ or higher.

Another factor is pH. The same as temperature, dissimilar enzymes have different
optimal pH at which it is most active.

In the human body, the optimal pH range for enzymes is 6 − 8. However, there are
exceptions such as enzymes in the digestive system. Pepsin, for example, is a digestive
enzyme present in the stomach, it works best at a very low pH. An acidic environment
can denature most enzymes, but pepsin is adapted to maintain its three-dimensional
structure. Trypsin, on the other hand, is a digestive enzyme residing in the intestine which
favors a more alkaline environment. It would be denatured if it is in the stomach.

7
 2. Cofactors

Some enzymes require nonprotein helpers to facilitate the reaction. Processes like
electron transfer in which amino acids in proteins cannot easily carry out, need these
adjuncts. These are called cofactors, some may be permanently bound to the enzyme
or permanent residents, and some may bind loosely and reversibly along with the
substrate. Metal atoms such as zinc, copper, and iron in the ionic form are the inorganic
cofactors of some enzymes. However, if the cofactor is an organic molecule, it is
specifically called coenzyme. Most vitamins act as coenzymes or raw materials from
which coenzymes are made. That is why vitamins are important in nutrition.

3. Enzyme Inhibitors

There are chemicals that can selectively inhibit the action of specific enzymes.
These are called enzyme inhibitors. Sometimes an inhibitor will bind to the enzyme
through covalent bonds which makes the inhibition irreversible. But many of these are
capable of binding to the enzyme through weak interactions which makes it reversible.
Some reversible inhibitor possesses characteristics resembling the substrate of the
enzyme and competes for admission in the active site. These are called competitive
inhibitors, which reduce the capability of the enzyme by blocking substrates entering
the active site. While noncompetitive inhibitors are molecules that bind to the other part
of the enzyme which causes the enzyme molecule to change its shape. Thus, the
enzyme’s active site becomes less effective at catalyzing the substrate into a by-
product. Most toxins and poisons are examples of irreversible enzyme inhibition. Like sarin,
a type of nerve gas that was used in the mid-1990s terrorist attack in the Tokyo subway
which killed several people and injuring others. The small molecule of sarin covalently
binds to the R group of the amino acid serine that is present in the active site of the
enzyme acetylcholinesterase, an enzyme important in the nervous system. Other
inhibitors are pesticides, antibiotics, etc.

Enzyme inhibition in general is not bad or harmful. In fact, it is used by the body to
regulate enzyme activity through molecules that act as inhibitors. This type of regulation
or selective inhibition is essential to the control of cellular metabolism.

8
 What I Can Do

Activity 1.1 Label and Describe!

Directions: Label and describe the parts of the illustration below. Write your answer on a
separate sheet.
2.
1.

3.

5. 4.

Activity 1.2 Let’s Analyze!

Directions: Analyze the graph below and answer the following questions. Write your
answer on a separate sheet.

Ea reduced by
Uncatalyzed
the catalyst
Energy

Catalyzed
Reactants Products

Progress of Reaction

Guide Questions:

1. What effect does a catalyst have on the activation energy of a reaction?

___________________________________________________________________________

2. What effect does a catalyst have on the change in free energy of a reaction?
___________________________________________________________________________

3. What effect does a catalyst have on the mechanism of a reaction?

___________________________________________________________________________

9
 What’s More

Activity 1.3 Concept Map!

Directions: Create a Venn diagram describing and differentiating the following:

a. Cofactors and Coenzymes

b. Competitive and Noncompetitive Inhibitions

Activity 1.4 Enzymes in My Body!

Digestive enzymes, which are important

components of the digestion process, are present
in our digestive system. In order for you to have a
deeper understanding of the importance of
enzymes in the body, please select at least three
(3) enzymes and discuss its location, type of
digestion, and its source.

Figure 1.11: The Digestive

System)
Image Credit: https://muschealth.org/medical-
services/ddc/patients/digestive-organs

Enzyme Location Type of Digestion Source

Oral Cavity Pharynx Carbohydrate

Salivary amylase Salivary glands
Esophagus digestion

1.

2.

3.

10
 What I Have Learned

Activity 1

Directions: Fill in the blanks. Complete the sentences below by providing the correct
term based on what is being described. Write your answer on a separate
sheet.

1. __________________ are organic or biological catalysts that are essential to living

organisms.

2. _________________ are substances that speed up a reaction without being used up,
destroyed, or incorporated into the product.

3. The _________________ is the reactant an enzyme act on.

4. The specific region of the enzyme where the substrate binds and the catalytic
reaction happens is called the ____________________.

5. When the substrate binds and tightens in the active site of the enzyme after initial
contact it is called _____________________.

6. ________________________ is the initial investment of energy to start a reaction.

7. When molecules absorb enough energy from the surrounding environment it

reaches an unstable state which is called the ______________________.

8. ____________________ in terms of electron transfer, is when there is the loss or splitting

of electron from one element or molecule.

9. While _________________________ is the gain of electrons.

10. ________________________ is a number that is assigned to an element in a compound

that denotes the electrons lost or gained, by the atom in a compound.

11
 Assessment

Directions: Read the following sentence carefully. Choose the letter of the best answer.
Write the chosen letter on your answer sheet.

1. What enzyme structure is described as the aggregation of the different polypeptide

units?
A. Primary structure C. Tertiary structure
B. Secondary structure D. Quaternary structure

2. The enzyme structure characterized by the order of amino acids is called the
____________________.
A. Primary structure C. Tertiary structure
B. Secondary structure D. Quaternary structure

3. What is the portion of the substrate-enzyme complex that is not consumed during a
reaction?
A. Substrate C. Active site
B. Activation energy D. Enzyme

4. A substrate is defined as:

A. The factor that hastens the reaction.
B. Inhibitor of enzymes.
C. The product which an enzyme acts on catalysis.
D. The reactant which an enzyme acts on catalysis.

5. New molecules produced after a catalysis are referred as ______________________.

A. Substrates C. Products
B. Inhibitors D. Activation energy

6. It is the initial investment of energy to start a reaction, also known as “free energy of
activation.”
A. Activation energy
B. Transition state
C. Free energy
D. Formation of products

7. When molecules reach an unstable state through absorbing enough energy from the
surrounding environment it is called _____________________.
A. Formation of products
B. Change in free energy
C. Transition state
D. Loss of energy

12
For question 8 refer to the illustration below.

Image Credit:
https://www.khanacademy.org/science/biology/energy-and-
enzymes/free-energy-tutorial/a/gibbs-free-energy

8. Based on the given image, the line graph that represents a catalyzed reaction is the
__________.
A. Red
B. Blue
C. Blue and red
D. None of the above

For questions 9 and 10 refer to the illustration below.

Image Credit: https://www.khanacademy.org/science/biology/energy-

and-enzymes/free-energy-tutorial/a/gibbs-free-energy

9. What is the change in free energy for the reaction?

A. The reaction free energy change is positive.
B. The reaction free energy change is negative.
C. The reaction free energy change is stable.
D. The reaction free energy change is constant.

10. Which part of the reaction the molecules possess the highest energy?
A. Before the reaction.
B. During the transition state.
C. After the transition state.
D. When the products are produced.

13
For questions 11 and 12 refer to the illustration below.

Image Credit: https://brainly.com/question/13280089

11. The enzyme salivary amylase has an optimal pH of _________.

A. 10
B. 7
C. 3
D. 1

12. What is the optimal pH for the enzyme pepsin?

A. 12
B. 8
C. 4
D. 2

13. Which characteristic allows enzymes to function in a specific way?

A. Enzymes are complex compounds composed of starch.
B. Each enzyme has a specific characteristic and shape.
C. Enzymes are long, complex fats.
D. Each enzyme is made up of four subunits.

14. In our bodies, enzymes function best at about _________________________.

A. 26 degrees Celsius
B. 36 degrees Celsius
C. 46 degrees Celsius
D. 56 degrees Celsius

15. No protein helpers in order to facilitate the reaction are called ______________.
A. Substrates
B. Inhibitors
C. Cofactors
D. Enzymes

14
 15
What I Can Do What I Know
Activity 1.1 Label and Describe 1. C
2. A
3. D
4. D
5. B
6. C
7. B
8. A
9. B
1. Cofactor – a non-protein component that activates the 10. C
enzyme.
11. B
2. The enzyme’s substrate is the reactant an enzyme acts
12. C
on.
13. C
3. The specific region of the enzyme where the substrate
binds, and the catalytic reaction happens is called the 14. D
active site. 15. C
4. Coenzyme – chemically different to cofactor but is also
an organic non-protein compound that binds with an
enzyme.
5. Apoenzyme – protein portion of the enzyme consisting
of amino acid chains.
Answer Key
 16
Activity 1.2. Let’s Analyze
Rubric
Content Points
1. Accurate and well-organized. 10
2. Organized with minimal error. 7
3. Not organized and with errors. 5 and below
What I Have Learned Assessment
1. Enzymes 1. D
2. Catalysts 2. A
3. Substrate 3. C
4. D
4. Active Site
5. C
5. Induced fit 6. C
6. Activation energy 7. B
7. Transition state 8. C
8. Oxidation 9. C
9. Reduction 10. B
10. Oxidation number 11. B
12. B
13. B
14. B
15. C
 References

Books:

Commission on Higher Education in collaboration with Philippine Normal

University. (2016). General Biology 1: Teaching Guide for Senior High
School. Quezon City: CHED.
Ramos, A. C., & Ramos, J. D. (2017). General Biology 1. Quezon City: Phoenix.
Urry, L. A., Cain, L. M., Wasserman, S. A., Minorsky, P. V., & Reece, J. B. (2017).
Campbell Biology 11th Edition. New York: Pearson.

Online Source:

Science Notes, “Black and White Periodic Table”, accessed August 9, 2021,
https://sciencenotes.org/periodic-table-wallpapers/

Images Source:

1. Accessed Date: August 17, 2021. Retrieved from

https://biologydictionary.net/ap-biology/3-1-enzyme-structure/
2. Accessed Date: August 17, 2021. Retrieved from
https://www.slideshare.net/AliaNajiha1/microbphysio4
3. Accessed Date: August 17, 2021. Retrieved from
https://botnam.com/enzymes/
4. Accessed Date: August 17, 2021. Retrieved from
https://muschealth.org/medical-services/ddc/patients/digestive-organs
5. Accessed Date: August 17, 2021. Retrieved from
https://www.khanacademy.org/science/biology/energy-and-
enzymes/free-energy-tutorial/a/gibbs-
6. Accessed Date: August 17, 2021. Retrieved from
https://www.khanacademy.org/science/biology/energy-and-
enzymes/free-energy-
7. Accessed Date: August 17, 2021. Retrieved from
https://brainly.com/question/13280089

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