BIOMOLECULES 1.

Monosaccharides (C6H12O6)
• Simple sugar with only one sugar unit.
A living system grows, sustains, and reproduces • Building blocks for more complex form of
itself. The most amazing thing about a living sugars.
system is that it is composed of non-living atoms Examples of Monosaccharides:
and molecules. Living systems are made up of a. Glucose (blood sugar)
various complex biomolecules that interact with • Component of the blood
each other and cons<tute the molecular logic of • Fuelforthebrain,liver,pancreas,pituitary,
life processes. andadrenal glands.
• Instant source of energy because it easily
One of the common features of organisms here dissolves in water.
on Earth is their biochemical composition. All
• Small enough to pass through the cell
organisms contain a common set of chemicals,
membrane and into the cell.
such as carbon (C), oxygen (O), nitrogen (N),
b. Galactose (milk sugar)
phosphorus (P), sulfur (S), and hydrogen (H),
• Isomer of glucose
which build larger and more complex molecules
• Found in milk as part of the sugar lactose
necessary in life. These large molecules -
o Found in dairy products.
carbohydrates, lipids, proteins, and nucleic acids
c. Fructose (fruit sugar)
– combine to produce different structures and
• Isomer of glucose
substances that perform specific functions in the
cell. These are called the biomolecules, also • Found in fruits and crops.
known as organic molecules or macromolecules. • Is the sweetest naturally occurring
carbohydrate.
Roles:
• serves as fuel for the metabolism of organisms
• their chemical composition and quantity are 2. Disaccharides (C12H22O11)
important for • Consists of two monosaccharides joined
cellular activities to proceed. by a glycosidic linkage, a covalent bond
• naturally occur in organisms formed between two monosaccharides by
a dehydration reaction.

CARBOHYDRATES
Carbohydrates are biomolecules believed to be
the most abundant of all organic compounds.
Majority of the carbohydrates have: carbon-
hydrogen-oxygen raFo of 1:2:1.
The term carbohydrate literally means “hydrated • Dehydration synthesis – a type of
carbon”, and it includes simple and complex chemical reaction in which two smaller
sugars. molecules are joined together to form a
larger molecule by removing water.
Roles: • Hydrolysis – breaking down of a
• The chief energy source of living organisms. disaccharide molecule by introduction of
• Backbone of other molecules (DNA and RNA) water.
• Primarily for storage of chemical energy (starch
for plants, Examples of Disaccharides:
glycogen for animals) Sucrose (table sugar)
• Form a structural component of living cells • Formed by combining glucose and
(chitin, cellulose, fructose.
glycoproteins, proteoglycans) • Used to sweeten our food and drink.
Lactose (milk sugar)
Classification of Carbohydrates:
 • Formed by combining glucose and - Insoluble carbohydrate abundant in
galactose. tough outer wall of plant cells which is
• Found in dairy products. used for support and protection.
Maltose (malt sugar) - Microorganisms found in the gut of
• Formed by combining two units of ruminants, termites, and other insects can
glucose. break down the linkage of sugar units in a
• Used in making beer and other alcoholic cellulose molecule because of its ability to
beverages. produce an enzyme called cellulase.
- Appear in fibers and paper is made out
Lactose intolerance is a common condition in of it.
humans who lack lactase, the enzyme that breaks
down lactose. The sugar is instead broken down
by intestinal bacteria, causing formation of gas
and subsequent cramping.

3. Oligosaccharides
• Complex form of carbohydrates that
consist of three to twenty sugar units.
• Glycosidic bonds hold each sugar unit
that is bonded together.

4. Polysaccharides
• Complex form of carbohydrates that LIPIDS
consist of more than twenty sugar units. Lipids are biomolecules containing chains
• Glycosidic bonds hold each sugar unit of hydrocarbons. When lipids are
that is bonded together. metabolized, they release large amount of
• Form long chains or branches. energy, and thus they are useful to
Examples of Polysaccharides: organisms. Lipids are varied in form and
a. Starch function, but we will focus on its types
- the major source of energy stored as a that are most important biologically: fats,
carbohydrate in plants. phospholipids, and steroids.
- It is composed of two substances: amylose,
which is a linear polysaccharide, and amylopectin, Hydrocarbons – are organic compounds
which is a branched polysaccharide. that are made up of carbon and hydrogen
- Easily digested by animals because an enzyme and are insoluble in water.
that can break the bond holding the glucose Non-essential fatty acids – fatty acids that
molecules is present. (amylase) can be synthesized or produced by the
body.
b. Glycogen
- the major source of energy stored as Essential fatty acids – fatty acids that
carbohydrate in animals. cannot be synthesized or produced by the
- contains more sugar units than starch. body to be and have consumed food or
- It is found in the liver and muscles, and a dietary supplements.
source of reserve energy and is ready to
be converted into glucose units when Functions of Lipids in the body:
needed. • Good source of energy and stored
energy in the body.
• Serves as thermal insulator in
c. Cellulose subcutaneous tissues.
 • Lipids which are nonpolar can act as • Stored in adipose tissue (body fat) and can be
electrical insulators. broken down to
• Make up the basic structure of cell release energy when needed.
membrane (phospholipids) • It also provides insulation against low
• Serve as chemical messengers that allow temperature and protect
tissues of the body to vital organs. This subcutaneous layer is especially
communicate with one another thick in whales, seals, and most other marine
(hormones) mammals, insulating their bodies in cold ocean
• Act as shock absorber or protects vital water.
organs.
3. Waxes
Classes of Lipids: • Chief storage form of energy for planktons.
1. Fatty Acids • Have water repellant properties and firm
• Transport form of metabolic fuel. consistency.
• Found in animal skin and fur of aquatic
a. Saturated fats – contains single bonds mammals, feathers of
and solid at ordinary conditions. waterfowls, and leaves of many plants.
Examples are margarine, butter, lard, • Examples are lanolin, beeswax, and carnauba
and animal fat. A diet rich in saturated wax.
fats is one of the several factors that
may contribute to an increased risk for 4. Phospholipids
heart disease and stroke. • Are essentials for cells because it is the major
constituent of the cell membrane and is
b. Unsaturated fats – contains double responsible for the bilayer structure of it.
bonds and liquid at ordinary • Has a hydrophilic (polar) head and two
conditions. Examples are vegetable oil, (nonpolar) hydrophobic
olive oil, peanut oil, corn oil, and fish tails.
oil.
Phospholipids are organized in a bilayer on the
c. Trans fats – came from partially surface of a cell. The hydrophilic heads are on the
hydrogenated oils, formed through a outside of the bilayer, in contact with the
manufacturing process that converts aqueous solutions both inside and outside the
vegetable oil into a solid fat at room cell. The hydrophobic tails point inward, away
temperature. This partially from the water. The phospholipid bilayer serves
hydrogenated oil is inexpensive and as a barrier between the cell and its
less likely to spoil, so foods made with surroundings, creating several compartments
it have a longer shelf life. within eukaryotic cells.

Trans fats create inflammation, which is linked to

heart disease, stroke, diabetes, and other chronic
conditions. They contribute to insulin resistance,
which increases the risk of developing type 2
diabetes. Some countries, such as Denmark and
Switzerland, have already banned artificially
produced trans fats in foods.

2. Triacylglycerol (TAG)
• Are fats (lipids) that function as long-term 5. Steroids
energy storage. • are lipids with the principal function of
modulating the structure of biological
membranes and signaling chemical biological
activities.
3. Storage Proteins
a. Bile acids – steroidal derivative that act as Function: Reservoir of metal ions and amino
emulsifying agent in the digestive system. acids, which can be utilized for the maintenance
b. Cholesterol- It helps regulate the fluidity of and growth of organisms.
the cell membrane and Example: Casein, the protein found in milk, serves
therefore, aid in the transport of molecules. It can as the primary supplier of amino acids for young
be harmful and cause complications if mammals. Plants, on the other hand, possess
unregulated. storage proteins within their seeds. Ovalbumin,
the protein present in egg whites, fulfills the role
Steroidal hormones - group of hormones of providing amino acids for the developing
derived from cholesterol that act as embryo.
chemical messengers in the body.
They regulate many physiologic 4. Transport Proteins
processes, including the development and Function: Also known as carrier proteins or
function of the reproductive system. transporter proteins, serve the essential function
i. ii. of facilitating the movement of various molecules
Male – androgen and testosterone across biological membranes, both within and
Female – estrogen and progesterone between cells.
Example: Hemoglobin, the iron-rich protein found
PROTEINS in the blood of vertebrates, carries oxygen from
the lungs to various tissues and organs
Proteins are recognized as the most diverse throughout the body.
among the biomolecules. They are believed to be
the central compound necessary for life, which is 5. Hormonal Proteins
why they are also called life’s “building blocks.” Function: Carry important information to
They make up over half of the solid matter in the different parts of the body to help regulate
majority of cells, playing a crucial role in nearly all various processes and coordinate activities.
activities carried out by organisms. Their Example: Insulin, a hormone secreted by the
significance is emphasized by their name, derived pancreas, prompts other body tissues to absorb
from the Greek word "proteios" signifying "first" glucose, thereby controlling the level of sugar in
or "primary". the bloodstream.

Functions of Proteins: 6. Receptor Proteins

Certain proteins accelerate chemical reactions, Function: Response of cell to chemical stimuli.
whereas others are involved in functions like Acts as molecular sensors.
protection, storage, transport, cell Example: Receptors built into the membrane of a
communication, movement, and providing cell binds to a ligand (chemical messenger
structural support. produced by signaling cells) and triggers a
response.
1. Enzymatic Proteins
Function: Selective acceleration of chemical
reactions. 7. Contractile and Motor Proteins
Example: Digestive enzymes catalyze the Function: Responsible for generating movement
hydrolysis of bonds in food molecules. in cells and tissues.
Example: Actin and myosin proteins enable
2. Defensive Proteins muscle cells to contract. This contraction is
Function: Protects against disease. essential for movements like walking, running,
Example: Antibodies inactivate and help destroy and even internal processes like heartbeats.
viruses and bacteria.
8. Structural Proteins
Function: Provide stability, support, and shape to
cells, tissues, and organisms. They form the Denaturation – disorganization of the
structural framework, ensuring the integrity and overall molecular shape of the protein
strength of various biological structures. causing it to be biologically inactive.
Example: Keratin is the protein of hair, horns,
feathers, and other skin appendages. Collagen
helps maintain the structural integrity of skin,
tendons, bones, and cartilage. Elastin enables
elasticity and flexibility to tissues.

Four Levels of Protein Structure:

1. Primary Structure – the simplest structure Denaturing agents – reagents or
of all the proteins. This is composed only conditions that brought the unfolding or
of the linear sequence of amino acids in a disorganization of a protein.
peptide chain.

2. Secondary Structure - this is a three-

dimensional shape created by several
hydrogen bonds. It is like how a ribbon
can twist and fold to create pattern, this
ribbon is a long chain of amino acids, and
these chains can twist and fold in specific
ways. The two common patterns are
called "alpha helix" and "beta sheet."

Example: Spiders secrete silk fibers made of a

structural protein containing beta pleated sheets,
which allow the spider web to stretch and recoil.

3. Tertiary Structure – a three-dimensional

shaped of peptide, which can either be
fibrous or globular in structure, it can be
determined by the interactions of the side
chains of the different amino acids in the
peptide.
AMINO ACIDS
4. Quaternary Structure – this happens : Building Blocks of Proteins
when proteins have more than one • Amino acids are organic compounds
polypeptide. that serve as the building blocks of
Example: Hemoglobin is an example of a proteins.
globular protein with quaternary • Contains carbon, hydrogen, oxygen, and
structure. It consists of four polypeptide nitrogen atoms, along with a variable side
subunits. chain that distinguishes one amino acid
from another.
Fibrous protein – elongated and thread- • All amino acids share a common
like shape. structure: they have a carboxyl group
Globular protein – compact and rounded (COOH) and an amino group (NH2)
shape separated by a carbon backbone.
• The side chain, known as the R group,
varies for each amino acid. This R group
can range from being as basic as a
hydrogen atom to a carbon structure with
different functional groups attached. The
distinctive traits of a specific amino acid,
including its physical and chemical
properties, are determined by its side
chain. be combined in various sequences to form
the vast array of proteins found in living
Polypeptide chain – is a linear chain of organisms. The sequence of amino acids
amino acids linked together by peptide in a protein determines its three-
bonds. dimensional structure and, consequently,
its function.
Peptide bond – bond between amino
acids. Amino acids are classified into two main
categories based on their role in protein
Classification of Amino Acids Based: on synthesis:
their Side Chains A. Essential Amino Acids
1. Nonpolar side chains • These are amino acids that the human
• Hydrophobic; low solubility in water body cannot synthesize on its own and
• Plays a crucial role in stabilizing protein must be obtained from the diet.
structures • 9 out of 20 amino acids are essential:
histidine, isoleucine, leucine, lysine,
methionine, phenylalanine, threonine,
tryptophan, and valine.

B. Non-Essential Amino Acids

• These are amino acids that the body can
synthesize independently, and they are
2. Polar side chains
not strictly required in the diet.
• Hydrophilic; highly soluble in water
• The rest of the 11 amino acids; alanine,
• They contribute to forming the
arginine, asparagine, aspartic acid,
boundary or interaction zone between the
cysteine, glutamic acid, glutamine,
protein
glycine, proline, serine, and tyrosine.
and its aqueous environment.

Enzymes
Enzymes can be defined as “biological polymers
that catalyze biochemical reactions”.
3. Electrically charged side chains
• Hydrophilic; highly soluble in water Most enzymes are proteins that possess essential
• Involved in enzymatic reactions, catalytic abilities required for various cellular
substrate binding, or protein-protein processes. These enzymes play a vital role in
interactions, conducting metabolic and other chemical
where electrostatic attractions or reactions within the cell, which are necessary to
repulsions are significant. sustain life.

Functions of Enzymes:
There are 20 standard amino acids • They break down large molecules into smaller
commonly found in proteins, each with its substances that can be easily absorbed by the
unique side chain. These amino acids can body.
• They help in generating energy in the body. ATP There are two theories that explain how enzymes
synthase is the enzyme involved in the synthesis work: lock and key hypothesis and induced fit
of energy. hypothesis.
Enzymes are responsible for the movement of
ions across the plasma membrane. The common analogy used in illustrating an active
• Enzymes perform a number of biochemical site is the lock-and-key relstionship. The key can
reactions, including oxidation, reduction, work perfectly when it exactly fits the lock.
hydrolysis, etc. to eliminate the non- nutritive However, there are times when certain
substances from the body. adjustments are also done by the enzyme to
• They function to reorganize the internal achieve an optimum fit for the substrates, this is
structure of the cell to regulate cellular activities. called induced fit theory.

How do enzymes work?

In order for things to change or react, they need a
certain amount of energy. Sometimes, when
there isn't enough energy, something called a
catalyst helps to make the reaction happen by
reducing the energy needed. This happens not
just in animals and plants but everywhere in the
universe.
Enzymes help reduce the activation energy of the
complex molecules in the reaction.
Factors Affecting Enzyme Activity
Active site – is part of an enzyme to which 1. Substrate Concentration - The
substrates bind and where a chemical reaction is concentration of substrates (the
catalyzed. molecules that enzymes act upon) directly
affects enzyme activity. As substrate
Substrate - is a specific molecule that the enzyme concentration increases, the rate of the
acts upon or interacts with during a chemical reaction also increases, until all enzyme
reaction. The enzyme binds to the substrate and active sites become saturated.
helps facilitate or speed up the conversion of the
substrate into one or more products. The 2. Enzyme Concentration - Increasing the
substrate is the molecule that fits into the amount of enzyme in a reaction can speed
enzyme's active site, where the actual chemical up the rate of the reaction, assuming that
reaction takes place. there is an excess of substrate available.
More enzymes mean more active sites
The basic mechanism of enzyme action is to available for substrate binding.
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 3. Temperature - With the increase in
area that combines with the substrate. temperature, the enzyme activity
increases because of the increase in
kinetic energy of the molecules. Enzymes
have an optimal temperature at which
they work most efficiently. This
temperature is often the normal body
temperature of the body. When the
temperature increases beyond a certain
limit, enzymes, which are actually made
up of proteins, begin to disintegrate and
the rate of reaction slows down.
 substrate complex. They cannot bind to
4. pH Level - Enzymes also have an optimal the free enzyme or the free substrate.
pH range at which they function best. Once the enzyme binds to the substrate,
Changes in pH can alter the charge and the uncompetitive inhibitor can attach to
shape of the enzyme's active site, the enzyme-substrate complex.
affecting substrate binding and enzyme
activity. Generally, an optimum pH for Effect on Enzyme Activity – they reduce the rate
enzymes is considered to be ranging of reaction by preventing the enzyme-substrate
between 5 and 7. complex from releasing products. This results in
the accumulation of enzyme- substrate-inhibitor
5. Inhibitors - Presence of certain substances complexes and a decrease in the formation of the
that inhibit the action of a particular reaction's products.
enzyme. This occurs when the inhibiting
substance attaches itself to the active site Uncompetitive inhibition is often non-reversible.
of the enzyme thereby preventing the
substrate attachment and slows down the
process.
Nucleic Acids
These are macromolecules made out of unit
Types of Inhibitors: called nucleotides. The two types of nucleic acids;
a.Competitive Inhibitors -are molecules deoxyribonucleic acid (DNA) and ribonucleic acid
that closely resemble the substrate and (RNA), enable living organisms to reproduce their
compete with the substrate for binding to complex components from one generation to the
the enzyme's active site. They "compete" next.
for the same spot on the enzyme.
DNA Structure
Effect on Enzyme Activity - When a 1. The genetic material inherited by
competitive inhibitor is present, it reduces the organisms from their parents. Each
rate of the enzymatic reaction because it chromosome has one long DNA molecule
occupies the active site and prevents the that normally contains several hundred
substrate from binding. This inhibition is genes. When a cell divides to reproduce
reversible, meaning that if you add more itself, its DNA molecules are duplicated
substrate, it can outcompete the inhibitor and and passed down from one generation of
restore enzyme activity. cells to the next.
2. DNA is composed of two families of
b. Non-competitive Inhibitors - do not nitrogenous bases: pyrimidines and
directly compete with the substrate for purines. They contain the sugar 2-
the active site. Instead, they bind to a deoxyribose and are joined by
different site on the enzyme, called an phosphodiester bridges.
allosteric site, causing a conformational 3. Pyrimidines – contain two fused carbon-
change in the enzyme's shape. nitrogen rings. The members of the
pyrimidine family are cytosine (C),
Effect on Enzyme Activity - The conformational thymine (T), and uracil (U).
change induced by non-competitive inhibitors 4. Purines – have a single carbon-nitrogen
makes the enzyme less effective at catalyzing the ring. The members of the purine family
reaction. Even if you add more substrate, it won't are adenine (A) and guanine (G).
fully overcome the inhibition because the active 5. Adenine, guanine, and cytosine are found
site is not directly blocked. Non-competitive in both DNA and RNA; thymine is found
inhibition is often non-reversible. only in DNA and uracil only in RNA.
6. The purine adenine (A) on one strand of
c. Uncompetitive Inhibitors - are unique in DNA is always paired with the pyrimidine
that they only bind to the enzyme- thymine (T) on the other strand, while the
 purine guanine (G) is always paired with
the pyrimidine cytosine (C); thus, the two
strands are said to be complementary.
7. The two strands are not positioned
directly opposite one another; therefore,
a major groove and a smaller minor
groove are formed by the double helix
backbone.
The two polynucleotide chains are
antiparallel. This means that their sugar-
phosphate backbones are oriented in
opposite directions.

RNA Structure
1. RNA differs from DNA in that it is composed
of sugar ribose instead of 2-deoxyribose.
2. It contains the pyrimidine uracil (U) instead
of thymine (T).
3. It consists of a single strand that can coil
back on itself, rather than
two strands coiled around each other.

Types of RNA:
• Messenger RNA (mRNA) – provides a
template for gene coding
during protein synthesis. It contains the
coding instructions for protein’s amino acid
sequence.
• Transfer RNA (tRNA) – carries/transfers
specific amino acids in the
cytoplasm to the ribosome to build a
polypeptide chain, aiding the
translation.
• Ribosomal RNA (rRNA) – it forms the
ribosomes and serves as the
structure of translation.

The Organization of DNA in cells:

1. In prokaryotes, DNA exists as a closed
circular, supercoiled molecule associated
with basic (histone like) proteins.
2. In eukaryotes, DNA is more highly
organized. It is associated with basic
(histone) proteins and is coiled into
repeating units known as nucleosomes.