Claret College of Isabela

Senior High School

P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

NAME: ____________________________________________ DATE: _______________________

COURSE AND YEAR: _______________________________ OUTPUT NO: ________________

STRUCTURES AND FUNCTIONS OF BIOLOGICAL MOLECULES - ENZYMES

(LEARNING ACTIVITY SHEET 1 & 2 - GENERAL BIOLOGY 1)

MOST ESSENTIAL LEARNING COMPETENCIES:

 Describe the components of an enzyme.
 Determine how factors such as pH, temperature, and substrate affect enzyme activity.

LESSON OBJECTIVE:
 Describe the components of an enzyme.
 Value the importance of enzymes to an individual through understanding its roles to our body.
 List down the factors that affects enzyme activity.
VALUES INTEGRATION:
 Stewardship

All organisms on Earth have cells that metabolize energy to support life. Thus, there is
a need to have a constant supply of energy around us. Cellular operations are accomplished through the
biochemical reactions that take place within the cell. These reactions are switched on and off, or sped up and
slowed down, depending on the immediate needs and overall functions of the cell. At any given time, the
various reactions involved in building up and breaking down cellular components must be regulated and
balanced in a coordinated manner. To achieve this balance, cells organize these reactions or processes into
different types of enzyme-powered pathways.

ENZYMES
The chemical reactions that make up metabolism do not proceed by themselves. These reactions are
switched on and off, or sped up and slowed down, depending on the cells' immediate needs and overall
functions. The organized mechanisms of regulating and controlling the metabolic pathways are powered by
organic catalysts called enzymes. An enzyme is a molecule that helps speed up the processes in a chemical
reaction. Enzymes allow reactions to occur under mild conditions, partly by eliminating nonspecific side
reactions. They also participate in the reaction by providing an alternative reaction pathway. But unlike other
substances, they do not undergo permanent changes until the end of the reaction. They are only limited to
changing the rate of reaction.

 Structure of a globular protein enzyme

1|General Biology
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

Components of an Enzyme

Enzymes are highly selective. They catalyze specific reactions only. This specificity is
due to their shapes. A typical enzyme is composed of a protein called an apoenzyme and a nonprotein called a
cofactor.
An apoenzyme can be called as a proenzyme when it is inactive, which means either it is not attached to
any substance or the enzyme is in its original form. If you remember the different protein structures, most
protein enzymes, such as apoenzymes, have intra- and intermolecular bonds that are in secondary or tertiary
structures. The shape could be disrupted by changes in temperature and pH. When the required temperature and
pH are not achieved, some of the contours of the enzyme are affected, which may hinder any catalytic activity.

The cofactors, on the other hand, assist apoenzymes in their biological activities. Cofactors have
different types, and each type behaves in a different way.
 Metal ion activators are not permanently bound to the apoenzyme. They supply positive charges to the
enzyme through covalent bonding. Examples of these metals include magnesium (Mg), zine (Zn),
manganese (Mn), sodium (Na), iron (Fe), potassium (K), and copper (Cu). These metals are actually the
dietary minerals that are part of your daily nutritional requirements. Without these, some of the required
catalytic reactions may not proceed.
 Coenzymes are organic molecules that usually come from the vitamins that you take in every day. Like
the metal ion activators, they temporarily bind to apoenzymes.
 Prosthetic cofactors can be either metal ions or organic molecules. The only difference is that they bind
to apoenzymes permanently.
A list of sample vitamins used as coenzymes can be found in table.
List of selected vitamins as enzyme cofactors and their functions
VITAMIN FUNCTIONS

Part of coenzyme cocarboxylase; has several functions, including the metabolism of

B1 (thiamine)
pyruvate

B2 (riboflavin) Coenzyme in flavoproteins; helps transfer electrons

B6 (pyridoxine) Coenzyme in amino acid metabolism

Helps in the transfer of methyl groups (methyl cyanocobalamide); active in amino

B12 (cyanocobalamin)
acid metabolism

Niacin (nicotinic acid) Part of the nicotinic acid dinucleotide (NAD) molecule; helps transfer electrons

Pantothenic acid Part of coenzyme A; metabolizes pyruvate and lipids

Biotin Helps in carbon dioxide fixation reactions and fatty acid synthesis

Folic acid Coenzyme involved in the synthesis of purines and pyrimidines

Vitamin E Coenzyme involved in cellular and molecular synthesis

Vitamin K Coenzyme used in electron transport (napthoquinones and quinones)

When the apoenzyme and the cofactors are bound, they form an enzyme complex called a holoenzyme. The
holoenzyme now becomes active and ready for any catalytic reaction.
2|General Biology
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

 This is how the components of an enzyme work. Most enzymes are holoenzymes that are composed of a
protein (apoenzyme) and a nonprotein (cofactor).

Not all enzymes are proteins. Some enzymes are also made of RNA molecules. Examples of these are
the ribozymes, which synthesize the proteins in the ribosomes of cells. Ribozymes undergo catabolism to help
build protein chains during protein synthesis. This is why they are also called catalytic RNA.

Enzymes proceed with the required biochemical reactions in the body only when
the specific cofactors and proteins are present. Most cofactors can be derived from vitamins and minerals. It is
important, therefore, to ensure that the basic nutritional needs are met daily for efficient bodily functions.

Chemical reactions happen in an orderly manner through a series of linked reactions. Metabolic
pathways start with a particular reactant and end with a final product. The reactants in the first reaction are
converted into products, which may serve as reactants for another product, and so on. One reaction leads to the
next reaction in an organized and regulated manner, especially when controlled by the enzymes. Therefore,
enzymes are vital for one metabolic pathway to interact with another metabolic pathway. This organized
arrangement is also useful for releasing and capturing small increments of molecular energy instead of releasing
it all at once. Ultimately, you will see the importance of enzymes in ensuring that cells are able to respond to the
changing environmental conditions and maximize their efficiency.

FACTORS AFFECTING ENZYMATIC SPEED

For enzymes to be fully operational, they require specific conditions. In some instances, enzymatic
reactions are increased more than 10 million times if the conditions are favorable. The rate of reaction is the
amount of product that is produced per unit of time. There are major factors that affect the catalytic function of
enzymes-temperature, substrate concentration, optimal pH, enzyme cofactors and enzyme inhibitors.

1. Temperature
As the temperature rises, molecules are more inclined to react because they have more
kinetic energy. The heat creates a more successful and more effective collision between the substrate and the
enzyme. Every organism has a certain temperature at which an enzyme's catalytic activity is at its greatest. For
humans, the optimal temperature for human cells is around 37.5°C. When this temperature is elevated, the
enzyme structure starts to undergo denaturation, or breaking down. The enzymatic activity declines rapidly
because the change in the structure of an enzyme can no longer accommodate the shape of the substrate Thus,
binding the substrate to the enzyme just does not happen.

 In the graph, the rate of enzymatic reaction doubles with every 5˚C rise. The
maximum
temperature wherein
enzymatic reaction
occurs is at just
before 40˚C. Then,

3|General Biology
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

it decreases until the reaction stops because the enzyme has become
denatured.

Endothermic ("warm-blooded") animals keep their internal heat in balance, allowing the enzymes to perform
faster and more effectively.

 Unlike in exothermic animals, the

body temperature maintained by
endothermic animals helps promote
the enzyme’s reaction rate in their
bodies.

2. Substrate Concentration
The substrate concentration refers to the amount of substrate molecules available for chemical reactions.
For the reaction to begin, molecules must collide. Substrate concentration increases the enzyme activity
because more collisions take place between the substrate molecules and the enzymes. There are more substrate
molecules that fill the active sites, and thus more results are produced per unit of time. However, when the
active sites are all filled continuously with the substrate, the rate of reaction no longer increases. The maximum
rate is then reached.
As the availability of substrates increases the enzyme activity, the opposite occurs when the substrates
are limited. The enzymatic reactions slow down with an insufficient concentration of substrates.

 As the substrate concentration increases, the rate

of enzymatic activity also increases up to its
maximum point.

3. Optimal pH
Like the other two factors, each enzyme also has an optimal pH level for it to reach its maximum
reaction rate. If the pH level continues to increase, the enzymatic reactions begin to decline. Each pH value has
a specific structural configuration for the enzyme. The globular structure of the proteins in the enzyme is
dependent on certain interactions of the enzyme, such as the hydrogen bonding or the interactions between the
R groups. Changing the pH level may affect the ionization of the side chains and disrupt their interactions.
When the pH level is either lower or higher than the optimal pH, the enzyme loses its structure and becomes
inactive. NO substrate will fit the altered active site, resulting in a disruption in the activity.

 In the graph, the optimal pH for the enzyme

is 5.0. Alteration of the enzyme shape due to
the changes in the pH level disrupts the
binding of substances.

4|General Biology
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

4. Enzyme Cofactors
Some enzymes need the addition of inorganic ions or coenzymes to help speed up the rat of reaction.
These are small organic molecules in trace amounts that can promote enzyme activities. They help bind the
substrate to the active site or participate in the reaction at the active site. Vitamins either become part of the
coenzyme's molecular structure or become coenzymes themselves, such that if vitamins are insufficient or
deficient, certain vitamin disorders occur. Riboflavin deficiency, for instance, results in cracks at the corners of
the mouth.

 Some coenzymes are

located at the active sites
of enzymes.

5. Enzyme Inhibitors
There are instances when enzyme activity should be limited. The molecule that binds to the enzyme to
decrease its activity is called the enzyme inhibitor. The end product itself may be used as the inhibitor. Enzyme
inhibition is important in controlling enzymatic reactions because once the body has completed the necessary
chemical processes, enzymatic reactions have to stop. This is also beneficial in conserving raw
materials and energy in the body.
When the enzyme is inhibited, it is not capable of binding to any substrate. Metabolic pathways are
inhibited until conditions are altered to induce reactions to take place again. Enzyme inhibition may be
reversible or irreversible, depending on the type of enzyme. When inhibition is reversible, the enzyme itself
can still be used because it is not damaged in the inhibition process. However, some enzymes do not allow for
a reversal of inhibition. In this case, the inhibitor permanently inactivates or destroys the enzyme.
By nature, enzyme inhibition serves as a control for proper enzymatic activities. Hence, you should be
careful in the types of food that you take in because certain compounds, especially those in processed food,
may act as enzyme inhibitors to required catalytic reactions in your body. Such foods may make you unhealthy
or sickly.
Enzyme inhibitors are normally used in pharmaceutical industries, where certain chemicals or molecules
block the activity of the enzyme. For example, some antibiotics contain chemicals that may act as inhibitors to
prevent the enzymatic activity of certain disease-causing bacteria. Thus, when an antibacterial medicine is
taken in, it could kill those bacteria. However, in some cases, these medicines may also inhibit or disrupt
certain enzymatic activities in your body. This is the reason that most medicines have side effects.

ESSENTIAL LEARNING
The numerous biochemical reactions in the body are managed and regulated by enzymes. They are
vital in cellular maintenance, Because of enzymes, cells are able to respond to the changes in the
environment and proper metabolism is maintained. Without the work of enzymes, cells are not able to
sustain life.
Metabolic pathways usually occur in a series of reactions that proceed in an organized, step-by-step
manner. Enzymes manage the numerous biochemical reactions in the body by speeding up reactions.
Usually, molecules have activation energy, which is the highest point of energy required for molecules to
achieve before any reaction can take place. Enzymes help them overcome it by lowering the activation
energy through the formation of an enzyme substrate complex; thus, they speed up chemical reactions.
Generally, enzyme activities increase with an increase in substrate concentration. Other factors that
affect enzyme activities are temperature and pH levels, wherein any unfavorable changes in their level may
change the structure of the enzyme, making it unfit to accommodate a specific substrate.
While enzymatic activities are promoted through cofactors, there has to be a system to regulate them.
This is done through inhibition which inhibits the binding of any substrate in the enzyme.
Enzymes are able to maximize their full potential if there is a sufficient amount of molecules and
substances necessary for any catalytic reaction to occur. A good way of helping 5 | G e these
n e r aenzymes
l B i o l owork
gy
efficiently is to provide them with the right amount and type of substances (foods that are rich in vitamins
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

NAME: ____________________________________________ DATE: _______________________

COURSE AND YEAR: _______________________________ OUTPUT NO: ________________

STRUCTURES AND FUNCTIONS OF BIOLOGICAL MOLECULES - ENZYMES

(LEARNING ACTIVITY SHEET 1 & 2 - GENERAL BIOLOGY 1)

Activity #1
Instructions: In your own understanding base on this module, define enzyme with at least three sentences and
describe it with its components. Use the given information in this module for your reference. Write
your answer inside the given table.
ENZYME
DEFINE DESCRIBE

Activity #2
Instructions: What are the factors that affects the rate of enzymatic reactions? How do these factors influence
the rate of enzymatic speed? Use the given information in this module for your reference.
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Reflection: You have just learned that enzymes play an important role in our body as an indispensable
substance. As a student, how are you going to express the importance of teachers as an indispensable tool for
teaching especially in this pandemic?
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6|General Biology
 Claret College of Isabela
Senior High School
P.O. Box 8692 Roxas Avenue, Isabela City, Basilan Province, 7300 Philippines
Tel. No. (062) 200 - 7697 / 200 – 7009 Telefax: (062) 200 - 3865

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7|General Biology