● inserting a water molecule across the

I. Biological Macromolecules bond

● breaking a covalent bond
Biological macromolecules
Dehydration and hydrolysis reactions are
● large molecules, necessary for life, catalyzed, or “sped up,” by specific enzymes;
that are built from smaller organic
molecules. Dehydration reactions involve the formation
● organic (contains carbon) of new bonds, requiring energy, while
● 4 Major Biological Macromolecules hydrolysis reactions break bonds and
● Carbohydrates release energy.
● Lipids
● Protein A specific enzyme breaks down each
● Nucleic Acid macromolecule

Synthesis of Biomolecules Break down carbohydrates

Monomers - amylase
- sucrase
● single subunits or building blocks - lactase
● (most macromolecules are made - maltase
from monomers)
Break down proteins
Polymers
- proteases, such as pepsin
● monomers combine with each other - peptidase
using covalent bonds to form larger - hydrochloric acid
molecules

Dehydration Synthesis
● “to put together while losing water.”
● hydrogen of one monomer combines
with the hydroxyl group of another
monomer
● monomers share electrons and form
covalent bonds
- CARBOHYDRATE (carbo - carbon &
hydrate - water)
● provide energy to the body,
particularly through glucose, a simple
sugar that is a component of starch
Molecular Structure of Carbohydrates

Hydrolysis ● stoichiometric formula (CH2O)n

● Polymers break down into monomers n - number of carbons

during hydrolysis
● polymer breaks into two components ● carbon to hydrogen to oxygen - 1:2:1
● one part gains a hydrogen atom (H+) ● 3 SUBTYPES OF
● other gains a hydroxyl molecule CARBOHYDRATES
(OH–) ● monosaccharides
 ● disaccharides
● polysaccharides
Monosaccharides (“one”) (sacchar - sweet)
● simple sugar
● number of carbons usually ranges
from three to seven
● most names end with the suffix -ose
● can be trioses (three carbons),
pentoses (five carbons), and/or
hexoses (six carbons).
Glucose
● chemical formula for glucose is
C6H12O6
● important source of energy
● cellular respiration, energy releases
from glucose, and that energy helps
make adenosine triphosphate (ATP).
(human)
● plants synthesize glucose using
carbon dioxide and water (energy
requirement)
● often obtain glucose from catabolized
(cell breakdown of larger molecules)
starch.
Galactose - (part of lactose - milk sugar)
Fructose - (sucrose- fruit)
● Same Chemical Formula (C6H12O6)
- Glucose
- Galactose
- Fructose
● differ structurally and chemically (and
are isomers)
● different arrangement of functional
groups around the asymmetric
carbon.
Disaccharides (di- = “two”)
form when two monosaccharides undergo a
dehydration reaction
one monosaccharide's hydroxyl group
combines with another monosaccharide's
hydrogen, releasing a water molecule and
forming a covalent bond.
Glycosidic Bonds (Glycosidic Linkages)
A covalent bond forms between a
carbohydrate molecule and another
molecule (in this case, between two
monosaccharides).
● Two Types
Alpha Bond
● formed when the OH group on the
carbon-1 of the first glucose is below
the ring plane
Beta Bond
● formed when the OH group on the
carbon-1 is above the ring plane.
Common disaccharides include
● lactose, consisting of the monomers
glucose and galactose. It is naturally
in milk.
● maltose or malt sugar, disaccharide
formed by a dehydration reaction
between two glucose molecules
● and sucrose or table sugar, which is
comprised of glucose and fructose
monomers.
POLYSACCHARIDES (poly- = “many”)
•A long chain of monosaccharides linked by
glycosidic bonds The chain may be branched
or unbranched, and it may contain different
types of monosaccharides.
The molecular weight may be 100,000
daltons or more depending on the number of
joined monomers.
Primary Examples of Polysaccharides
○ Starch
○ Glycogen
○ Cellulose
○ Chitin
•Plants store sugars in the form of starch. In
plants,
○ synthesize glucose
○ store excess glucose
○ an amylose and amylopectin
mixture (both glucose
polymers) comprise these
sugars.
The starch in the seeds
○ provides food for the embryo
as it germinates
○ act as a food source for
humans and animals.
○ Enzymes break down the
starch that humans consume.
For example, an amylase
present in saliva catalyzes
Glucose starch comprises monomers that
are joined by α 1-4 or α 1-6 glycosidic bonds.
The numbers 1-4 and 1-6 refer to the carbon
number of the two residues that have joined
to form the bond.
Glycogen
○ storage form of glucose in
humans and other
 vertebrates and is comprised
of monomers of glucose.
○ animal equivalent of starch
○ highly branched molecule
usually stored in liver and
muscle cells.
Lipids
Glycogenolysis
○ blood glucose levels
decrease, glycogen breaks
down to release glucose in a
process
● Non-polar molecules are
hydrophobic (“water fearing”), or
insoluble in water.
● Cells store energy for long-term use
in the form of fats.
● provide insulation from the
environment for plants and animals.
● For example, they help keep aquatic
birds and mammals dry when forming
a protective layer over fur or feathers
because of their water-repellant
hydrophobic nature.
● the building blocks of many
hormones and are an important
constituent of all cellular membranes.
● include fats, oils, waxes,
phospholipids

FATS AND OILS

A fat molecule consists of two main

components—glycerol and fatty acids.

Glycerol is an

● organic compound (alcohol) with

● three carbons,
● five hydrogens,
● three hydroxyl (OH) groups.
● Fatty acids have a long chain of
hydrocarbons to which a carboxyl
group is attached, hence the name
“fatty acid.”
● Number of Carbons (fatty acid)
● 4 to 36
LIPIDS
● The most common are those
Lipids - largely nonpolar in nature. This is containing 12–18 carbons. In a fat
molecule, the fatty acids attach to
because they are hydrocarbons that include
each of the glycerol.
mostly nonpolar carbon–carbon or carbon–
hydrogen bonds.
 Example (Saturated)

● Stearic acid (animal fats)

● Palmitic Acid (common in meat)
● Butyric acid (butter)

During this ester bond formation, three water

molecules are released. We also call fats
triacylglycerols or triglycerides because of
their chemical structure. Some fatty acids
have common names that specify their
origin. For example, palmitic acid, a
Unsaturated Fatty Acid
saturated fatty acid, is derived from the palm
tree. ● hydrocarbon chain contains a double
bond
Arachidic acid is derived from Arachis
● Example
hypogea, the scientific name for groundnuts
● Oleic acid
or peanuts.
Most unsaturated fats are liquid at room
•Fatty acids may be saturated or
temperature.
unsaturated. In a fatty acid chain,
● oils
Saturated Fatty Acids
monounsaturated fat (e.g., olive oil) - one
○ only single bonds between
double bond in the molecule
neighboring carbons in the
hydrocarbon chain polyunsaturated fat (e.g., canola oil) if there
○ saturated with hydrogen is more than one double bond
○ hydrogen atoms attached to
the carbon skeleton are
maximized.
•When a fatty acid has no double bonds, it is ● alcohol classification (sterols).
a saturated fatty acid -not possible to add
more hydrogen to the chain's carbon atoms Most Common Steroid - Cholesterol

Long straight fatty acids with single bonds The liver synthesizes cholesterol
generally pack tightly and are solid at room
temperature. ● precursor to
● as testosterone and estradiol, which
Unsaturated fats or oils are gonads and endocrine glands
secrete.
● usually of plant origin ● to Vitamin D.
● contain cis unsaturated fatty acids. ● of bile salts, which help emulsifying
● Cis and trans indicate the fats and their subsequent absorption
configuration of the molecule around by cells.
the double bond. ● Sterols (cholesterol in animal cells,
● Cis Fat phytosterol in plants) are
● If hydrogens are present in the same components of the plasma
plane membrane of cells and are found
● Trans Fat within the phospholipid bilayer.
● If the hydrogen atoms are on two
different planes Most Abundant Organic Molecules-
PROTEINS
Kink - a bend (cis double bond)
PROTEINS
● prevents the fatty acids from packing
tightly, keeping them liquid at room ● have the most diverse range of
temperature functions of all macromolecules.
● Proteins may be structural,
WAXES regulatory, contractile, or protective.
● They may serve in
Wax covers some aquatic birds' feathers and ● transport,
some plants' leaf surfaces. ● storage, or membranes;
● or they may be toxins or enzymes.
● hydrophobic nature, they prevent ● Each cell in a living system may
water from sticking on the surface. contain thousands of proteins, each
● Long fatty acid chains esterified to with a unique function
long-chain alcohols comprise waxes. ● amino acid polymers arranged in a
linear sequence.
STEROIDS
TYPES AND FUNCTIONS OF PROTEINS
Steroids have a fused ring structure.
Enzymes
● hydrophobic and insoluble in water.
● All steroids have four linked carbon ● are catalysts in biochemical reactions
rings and several of them, like (like digestion)
cholesterol, have a short tail.
 ● usually complex or conjugated
proteins.
● Each enzyme is specific for the
substrate (a reactant that binds to an
enzyme) upon which it acts.
● The enzyme may help in
● breakdown,
● rearrangement,
● synthesis reactions

Catabolic Enzymes
Amino acids
● enzymes that break down their
substrates ● monomers that comprise proteins
● Each has the same fundamental
Anabolic Enzymes structure,
● consists of a central carbon atom,
● build more complex molecules from ● or the alpha (α) carbon, bonded to an
their substrates amino group (NH2), a carboxyl group
(COOH), and to a hydrogen atom.
Catalytic Enzymes
● Every has another atom or group of
● enzymes that affect the rate of atoms bonded to the central atom
reaction known as the R group
● Note that all enzymes increase the
reaction rate and, therefore, are
organic catalysts.
● An example of an enzyme is
● salivary amylase, which hydrolyzes
its substrate amylose, a component
of starch.

Hormones

● chemical-signaling molecules,
● usually small proteins or steroids,
secreted by endocrine cells that act
to control or regulate
● specific physiological processes,
● growth
Amino Acids
● development
● metabolism
● contain both amino group and
● reproduction
carboxyl-acid-group in their basic
● For example, insulin is a protein
structure.
hormone that helps regulate the
blood glucose level.
 ● 20 common amino acids present in
proteins.
● Nine of these are essential amino
acids in humans because the human
body cannot produce them and we
obtain them from our diet. For each
amino acid, the R group (or side
chain) is different.
NUCLEIC ACID- MOST IMPORTANT
MACROMOLECULES
Nucleic acids for the continuity of life.
● they carry the cell's genetic blueprint
● carry instructions for its functioning
DNA AND RNA
The two main types of nucleic acids are
● deoxyribonucleic acid (DNA)
● ribonucleic acid (RNA).
● DNA is the genetic material in all
living organisms, ranging from single-
celled bacteria to multicellular
mammals. It is in the nucleus of
eukaryotes and in the organelles,
chloroplasts, and mitochondria.
● In prokaryotes, the DNA is not
enclosed in a membranous envelope.
The cell's entire genetic content is its
genome, and the study of genomes is
genomics. In eukaryotic cells but not in
prokaryotes, DNA forms a complex with
histone proteins to form chromatin, the
substance of eukaryotic chromosomes.
A chromosome may contain tens of
thousands of genes.
Many genes contain the information to make
protein products. Other genes code for RNA
products. DNA controls all of the cellular
activities by turning the genes “on” or “off.”
•The other type of nucleic acid, RNA, is
mostly involved in protein synthesis. The
DNA molecules never leave the nucleus but
instead use an intermediary to communicate
with the rest of the cell. This intermediary is
the messenger RNA (mRNA). Other types of
RNA—like rRNA, tRNA, and microRNA—are
involved in protein synthesis and its
regulation.
The three major types of RNA are
○ mRNA (messenger RNA) : it
provides the template for
protein synthesis during
translation
○ tRNA (transfer RNA) : it
brings aminoacids and reads
the genetic code during
translation
○ rRNA (ribosomal RNA) : it
plays a structural and
catalytic role during
translation
Nucleotides
 ● DNA and RNA are comprised of
monomers

Polynucleotides

The nucleotides combine with each other to

form DNA or RNA.

Three components comprise each

nucleotide:

● a nitrogenous base,
● a pentose (five-carbon) sugar, and
● a phosphate group
● Each nitrogenous base in a
nucleotide is attached to a sugar
molecule, which is attached to one or
more phosphate groups.

The nitrogenous bases, important

components of nucleotides,

● are organic molecules

● they contain carbon and nitrogen
● contain an amino group that has the
potential of binding an extra
hydrogen, and thus decreasing the
hydrogen ion concentration in its
environment, making it more basic.
● Each nucleotide in DNA contains one
of four possible nitrogenous bases:
● adenine (A),
● guanine (G)
● cytosine (C),
● and thymine (T)

Purines - two carbon-nitrogen rings II. ENZYMES

● adenine Enzymes
● guanine
● a substance that acts as a catalyst in
Pyrimidines - single carbon-nitrogen ring living organisms, regulating the rate
at which chemical reactions proceed
● cytosine
without itself being altered in the
● thymine
process.
● uracil
 ● Without enzymes, many of these amino acid sequence
reactions would not take place at a determines the characteristic
perceptible rate. folding patterns of the
● Enzymes catalyze all aspects of cell protein’s structure, which is
metabolism. essential to enzyme
● This includes the digestion of food, in specificity. If the enzyme is
which large nutrient molecules are subjected to changes, such
broken down into smaller molecules; as fluctuations in temperature
● the conservation and transformation or pH, the protein structure
of chemical energy; may lose its integrity
● the construction of cellular (denature) and its enzymatic
macromolecules from smaller ability. Denaturation is
precursors. sometimes, but not always,
● deficiency of a particular enzyme. reversible.
● albinism and
● phenylketonuria NOMENCLATURE

Enzymes also have valuable industrial and •An enzyme will interact with substrate, to
medical applications. catalyze a certain kind of reaction.

● in medicine include killing disease- ○ suffix “-ase” to the substrate’s

causing microorganisms, promoting name (as in urease, which
wound healing, and diagnosing catalyzes the breakdown of
certain diseases. urea).
○ There are six principal
CHEMICAL NATURE OF ENZYMES categories and their
reactions:
•All enzymes were once thought to be ○ (1) oxidoreductases, which
proteins, but since the 1980s the catalytic are involved in electron
ability of certain nucleic acids, transfer;
○ (2) transferases, which
○ ribozymes (or catalytic transfer a chemical group
RNAs), has been from one substance to
demonstrated, refuting this another; (3) hydrolases,
axiom. Because so little is yet which cleave the substrate by
known about the enzymatic uptake of a water molecule
functioning of RNA, this (hydrolysis); (4) lyases, which
discussion will focus primarily form double bonds by adding
on protein enzymes. or removing a chemical
group; (5) isomerases, which
•A large protein enzyme molecule
transfer a group within a
○ is composed of one or more molecule to form an isomer;
amino acid chains called and (6) ligases, or
polypeptide chains. The synthetases, which couple
the formation of various
 chemical bonds to the
breakdown of a amino acids
pyrophosphate bond in
adenosine triphosphate or a
similar nucleotide.
MECHANISMS OF ENZYME ACTION
● In most chemical reactions, an
energy barrier prevents complex
molecules such as proteins and
nucleic acids from spontaneously
degrading, and so is necessary for
the preservation of life.
● When metabolic changes are
required in a cell, however, certain of
these complex molecules must be
broken down, and this energy barrier
must be surmounted.
● Heat could provide the additional
needed energy (called activation
energy), but the rise in temperature
would kill the cell.
● The alternative is to lower the
activation energy level through the
use of a catalyst. This is the role that
enzymes play. They react with the
substrate to form an intermediate
complex—a “transition state”—that
requires less energy for the reaction
to proceed.
● The unstable intermediate compound
quickly breaks down to form reaction
products, and the unchanged
enzyme is free to react with other
substrate molecules.
1. Active site binds to the
substrate.
2. The active site is a groove or
pocket formed by the folding
pattern of the protein.
3. three-dimensional structure,
together with
4. the chemical
5. electrical properties of the
6. cofactors within the active
site, permits only a particular
substrate to bind to the site,
thus determining the
enzyme’s specificity.
Enzymes are not always found uniformly
within a cell; often they are
compartmentalized in the nucleus, on the cell
membrane, or in subcellular structures. The
rates of enzyme synthesis and activity are
further influenced by hormones,
neurosecretions, and other chemicals that
affect the cell’s internal environment.
REDOX REACTIONS
Oxidation - loss of electrons from a
substance; Oxidation Reactions - addition of
oxygen or the more electronegative element
or removal of hydrogen or the more
electropositive element from a substance.
Reduction Reactions - gain of electrons.
○ Any substance that gains
electrons during a chemical
reaction gets reduced.
○ addition of hydrogen or a
more electropositive element
or the removal of a more
electronegative element or
oxygen from a substance.
OXIDIZING AND REDUCING AGENT
Oxidizing Agent
○ The substance (atom, ion and
molecule) that gains electrons
and is thereby reduced to a
low valency state
 ○ Electron-accepting species
which tend to undergo a
reduction in redox reactions
Reducing Agent
○ The substance that loses
electrons and is thereby
oxidized to a higher valency
state
○ An electron-donating species
which tends to hand over
electrons can be referred to
as a reducing agent.
•In the illustration provided below, it can be
observed that the reactant, an electron, was
removed from reactant A, and this reactant is
oxidized. Similarly, reactant B was handed
an electron and was, therefore, reduced.
Oxidation
● The loss of electrons and the
corresponding increase in the
oxidation state of a given reactant.
Reduction
● The gain of electrons and the
corresponding decrease in the
oxidation state of a reactant
● any redox reaction can be broken
down into two half-reactions, namely,
the oxidation half-reaction and the
reduction half-reaction.
The driving force
● derived from reduction-oxidation
reactions.
● Enzymes play a significant role in
connecting the series of redox
reactions ultimately involving
oxygen.” (Punekar, 2018)
FACTORS AFFECTING ENZYME
ACTIVITY
There are several factors that affect the
speed of an enzyme’s action
● concentration of the enzyme
● concentration of the substrate
● temperature
● hydrogen ion concentration (pH)
● presence of inhibitors
FACTOR 1: CONCENTRATION OF
ENZYMES
As the concentration of the enzyme is
increased, the velocity of the reaction
proportionately increases. This property is
used for determining the activities of serum
enzymes during the diagnosis of diseases.
FACTOR 2: CONCENTRATION OF
SUBSTRATE
•In the presence of a given amount of
enzyme, the rate of enzymatic reaction
increases as the substrate concentration
increases until a limiting rate is reached, after
which further increase in the substrate
concentration produces no significant
change in the reaction rate.
Enzyme molecules
○ saturated with substrate.
○ excess substrate molecules
cannot react until the
substrate already bound to
the enzymes has reacted and
been released (or been
released without reacting).
FACTOR 3: TEMPERATURE
•The protein nature of the enzymes
○ extremely sensitive to thermal
changes.
○ occurs within a narrow range
of temperatures
Optimal Temperature
○ each enzyme has a certain
temperature which ranges
between 37 to 40C°.
•The enzyme activity gradually lowers as the
temperature rises more than the optimal
temperature until it reaches a certain
temperature at which the enzyme activity
stops completely due to the change of its
natural composition.
•On the other hand, if the temperature lowers
below the optimal temperature, the enzyme
activity lowers until the enzyme reaches a
minimum temperature at which the enzyme
activity is the least. The enzyme activity
stops completely at 0C°, but if the
temperature rises again, then the enzyme
gets reactivated once more.
FACTOR 4: pH
•The potential of hydrogen (pH) is the best
measurement for determining the
concentration of hydrogen ion (H+)in a
solution.
○ It also determines whether
the liquid is acidic, basic or
neutral.
○ Acids pH - below 7
○ Bases/ Alkalines - above 7
○ Liquids with pH 7 are neutral
and equal the acidity of pure
water at 25 C°.
○ pH indicators - determiner of
pH
•Enzymes are protein substances
○ contain acidic carboxylic
groups (COOH–) and basic
amino groups (NH2). So, the
enzymes are affected by
changing the pH value.
○ Optimal pH. Each enzyme
has a pH value that it works at
with maximum efficiency. If
the pH is lower or higher than
the optimal pH, the enzyme
activity decreases until it
stops working.
○ For example, pepsin works at
a low pH, i.e, it is highly acidic,
while trypsin works at a high
pH, i.e, it is basic. Most
enzymes work at neutral pH
7.4.
○ Neutral pH 7.4
FACTOR 5: ACTIVATORS
● Some of the enzymes require certain
inorganic metallic cations, like Mg2+,
Mn2+, Zn2+, Ca2+, Co2+, Cu2+,
Na+, K+ etc., for their optimum
activity. Rarely, anions are also
needed for enzyme activity, e.g. a
chloride ion (CI–) for amylase.
Lei