- Serves as fuel and building material

WEEK 1 - MACROMOLECULES S - Include both sugars and their

MACROMOLECULES ? polymers (starch, cellulose, etc.)
Large molecules composed of smaller molecules - Aldehyde - double bond OH
- Complex in their structures (terminal)
- Most macromolecules are polymers, built
- Ketone - within the structure
from monomers.
- C6H1206
4 MAJOR MACROMOLECULES (ORGANIC) ?
1. Carbohydrates - most abundant
macromolecule on earth.
2. Lipids - provides insulation and
production: energy source
3. Proteins - most abundant macromolecule
in the body.
4. Nucleic acids - genetic information.
POLYMERS ?
- Long molecules consisting of many
similar building blocks called monomers.
- Specific monomers make up each
macromolecule. HAWORTH PROJECTION: ?
- Eg. Amino acids are the monomers for CARBOHYDRATE CYCLIC RING ?
proteins. - Carbohydrates also appear in cyclic rings
instead of linear molecules.
SYNTHESIS AND BREAKDOWN OF POLYMERS ? - Carbonyl group (aldehyde and ketone)
- Monomers form larger molecules by can react with a hydroxyl group (-OH
condensation reactions called dehydration
group).
Synthesis.
- Polymers can be disassembled by Hydrolysis
- Hydrolysis - addition of water molecules
- Dehydration synthesis - removal of water

CLASSES OF CARBOHYDRATES ?
MONOSACCHARIDES s
- contain a single polyhydroxy aldehyde or
ketone unit
- Saccharo - greek for sugar
- Eg. glucose, fructose

WEEK 2 - CARBOHYDRATES S
WHAT IS CARBOHYDRATES? ?
- Polyhydroxy aldehydes or ketones, or
substances that yield such
compounds on hydrolysis
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 - Simplest of the carbohydrates
carbohydrates since they contain only
one polyhydroxy aldehyde or ketone unit.
- They are classified according to the
number of carbon atoms they contain.

No. of Carbons Class of

Monosaccharide

3 Triose
4 Tetrose
5 Pentose
6 Hexose
- The presence of an aldehyde is indicated
by the prefix aldo- and a ketone by the
prefix keto-

DISACCHARIDES s
- consist of two monosaccharide units
linked together by a covalent bond.
- Eg. sucrose

PHYSICAL PROPERTIES OF MONOSACCHARIDES

- Most monosaccharides have a sweet
taste
- Solid at room temperature
- Extremely soluble in water
- The presence of large numbers of OH
groups make the monosaccharides much
more water soluble than most molecules
of similar MW.
- Glucose can dissolve in minute amounts
of water to make a syrup (1g/ 1 ml H20)

IMPORTANT MONOSACCHARIDES

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 which may be either in straight or
branched chains
- 3 Kinds of Polysaccharides: Cellulose,
glycogen, starch

OLIGOSACCHARIDES s
- contain from 3-10 monosaccharide units
- Eg. raffinose

IMPORTANCE OF CARBOHYDRATES ?
- Compounds of tremendous biological
importance:
- provides energy for the body
- supply carbon for the synthesis of cell
components
- form of stored chemical energy
- form part of the structure of some cells
and tissues
- it is known as biomolecules because
- Fructooligosaccharides are oligosaccharides
they are associated with living organisms.
that occur naturally in plants such as onion,
chicory, garlic, asparagus, banana, artichoke,
OCCURRENCE OF CARBOHYDRATES ?
among many others.
● Almost 75% of dry plant material is
produced by photosynthesis.
● Most of the matter in plants, except
water, are carbohydrate material
● Examples of carbohydrates are
cellulose which are structural component
of the plants, starch the energy reservoir
in plants and glycogen (animal starch) found
in animal tissues and human body in smaller
quantities

POLYSACCHARIDES s
- contain very long chains of hundreds or
thousands of monosaccharide units,

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 - CHIRAL - distinguishable from its mirror
image; that is, it cannot be superimposed
onto it.
- ACHIRAL - when an object has a point of
symmetry.

BLOOD TYPES & OLIGOSACCHARIDES ?

Oligosaccharides are often found as a component
of glycoproteins or glycolipids. They are often
used as chemical markers on the outside of cells,
often for cell recognition. Oligosaccharides are
also responsible for determining blood type.
● Chiral molecules have the same
relationship to each other that your
left and right hands have when
reflected in a mirror.
● Any carbon atom which is connected to
four different groups will be chiral, and
will have two nonsuperimposable mirror
images; it is a chiral carbon or a center
CARBOHYDRATES & CHIRALITY ? of chirality (encircled in red).
● Carbohydrates, and other organic compound, ● If any of the two groups on the carbon
achiral. Chiral molecules are said to be are the same, the carbon atom cannot be
optically active. chiral.
● Molecules which rotate the plane of ● Many organic compounds, including
polarized light is optically active. carbohydrates, contain more than one
● A levorotatory (–) substance rotates polarized chiral carbon.
light to the left. [e.g., L- glucose; (-)-glucose
● A dextrorotatory (+) substance rotates
polarized light to the right. [E.g., d- glucose;
(+) -glucose]
● Most biologically important molecules are
chiral, and hence are optically active.
● Often, living systems contain only one of
all of the possible stereochemical
forms of a compound. In some cases,
one form of a molecule is beneficial, and
the enantiomer is a poison.
CHIRALITY ?
- is a property of asymmetry important
in several branches of science.
- Chirality is derived from the Greek (kheir),
"hand", a familiar chiral object.

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STEREOISOMERS ?
● compounds with the same chemical
formula but different structures.
STEREOCHEMISTRY OF CARBOHYDRATES S
● Glyceraldehyde, the simplest carbohydrate,
exists in two isomeric forms that are mirror
images of each other.
● These forms are stereoisomers of each other.
● Glyceraldehyde is a chiral molecule. The
two mirror image forms of glyceraldehyde
are enantiomers of each other.
● D-glucose, is the most commonly occurring
isomer of glucose in nature. Common source
of energy (Dextrose).
● L-glucose cannot be used as a source of
energy in cellular respiration. Used as
laxative in some cases.
SAPONIFIABLE LIPIDS
FISCHER PROJECTIONS S
● Fischer projections are a convenient way
to represent mirror image in two
dimensions.
● Place the carbonyl group at or near the top
and the last achiral CH2OH at the bottom.
NAMING ISOMERS S
● When there is more than one chiral in a
carbohydrate, look at the chiral carbon
farthest from the carbonyl group: if the
hydroxyl group points to right when the
carbonyl is “up” it is the D-isomer, and
when the hydroxyl group points to the left,
it is the L-isomer.
WEEK 3 - LIPIDS S
WHAT ARE LIPIDS? ?
- Lipids are nonpolar
- Can be dissolved in water
- Hydrophobic
- Waxy, greasy, oily
- Energy storage in a form of fats
- Used as insulation against cold
- insoluble in water but soluble in
non-polar solvent
- Among the other macromolecules,
LIPIDS DO NOT CONSIST POLYMER
2 CLASSIFICATIONS OF LIPIDS S
S
- Undergo saponification - the process of
hydrolysis under basic conditions (pH
level is greater than 7)
- Contains ester linkages & can be
hydrolyzed into smaller molecules.
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Esters - functional group - Should have methyl and acid end
Polar head lipids - water soluble - Kink - prevents fatty acids from packing
Non-polar lipids - water insoluble tightly.
- CH3 - methyl group
- C = OOH - carboxylic acid (functional
group)
Carbon chains vary in: length and saturation

NON-SAPONIFIABLE LIPIDS S
- Do not contain ester linkages therefore
they cannot be saponified.
- Eg. steroids and prostaglandins

TYPES OF SAPONIFIABLE LIPIDS S

Simple Lipids - esters of fatty acids with various
alcohols.
SATURATED FATTY ACIDS S
● Fats
- Single bond (do not contain double bond)
● Waxes
- Carbon chain filled with hydrogen atoms
● Triglycerides
- Triglyceride
Complex Lipids - esters of fatty acids containing
- Appear in “solid” in room temperature
groups in addition to alcohol and fatty acid.
- Shorter = lower melting point
● Phospholipids
- Longer = higher melting point
● Glycolipids
- Eg. animal lards (butter) & tropical oils
TRIGLYCERIDE E
(palm, coconut)
- Fats and oils
- 3 Fatty acids + Glycerol
- Building blocks of lipids
- Major storage form of fat in the body

UNSATURATED FATTY ACIDS S

- Have double bond
- Mabilis ma digest bcs they can easily
breakdown
- Carbon chains lacks hydrogen
● MONOUNSATURATED FAT
- Triglyceride contains fatty acids with 1
double bond.
FATTY ACIDS S
- More healthy
- Organic acid (chain of carbons w
- Eg. Canola & olive oil
hydrogens attached)
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 ● POLYUNSATURATED FAT
- More than 2 double bonds
- Tends to be liquid at room temperature
- They appear more liquid at room temp
bcs of the presence of double bonds.
- Contains high percent of fatty acid
- Eg. Corn, sunflower oils, fish, safflower

HYDROGENATED FATTY ACIDS S

________________________________________
- Addition of hydrogen to unsaturated fat
- Effects stability and protects against
oxidation
- Shelf-stable
- Widely used by the food industry
- Eg. margarine, peanut butter, baked
goods and snack food

- Locate double bonds CIS VS TRANS FATTY ACIDS S

● OMEGA NUMBER - refers to the position CIS- -
of double bond nearest the methyl (CH3) Cis double bonds causes bending
end of the carbon chain - More healthier than trans
Essentials fatty acids - Most double bonds
- Omega-3 fatty acid - linolenic - Hydrogen is on the same side of the
- Omega-6 fatty acid - linoleic carbon chain
- But when fat is partially hydrogenated,
some of the double bonds change from
cis to trans
- U-like formation
TRANS- -
- Bend
- More linear
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 - Hydrogen is located on the other side - Importance: sex hormones, vitamin D,
bile, adrenal hormones
- Bile aids digestion of lipids in the small
intestine.

________________________________________
PHOSPHOLIPIDS S
- 2 fatty acids + choline
- Phospholipids in foods: lecithin, egg
yolks, soybeans, peanuts, & wheat germ
- Part of cell membranes & acts as an
emulsifier (helps keep fats in solution)
WAXES S
- Simple lipids contain a fatty acid joined to
a long chain (12-32 carbons) alcohol
- Insoluble in water
- Not easily hydrolyzed as fats and oils
- Sebum - produces wax

FAT DIGESTION S
Hydrolysis → Triglycerides → Monoglycerides,
Fatty acids, Glycerol

- Lecithin works as an emulsifier

STEROLS S
- Consists of carbon rings (4 fused rings)
- Classified as lipids
- No C=C & solid at room temp
- Soluble in nonpolar solvents, but they are
non saponifiable bcs the components are
not held together by ester bonds FUNCTION OF FATS S
- Eg. cholesterol (most abundant steroid) 1. ENERGY - 9 KCALS/GM
60% of body’s energy
Stored as adipose tissue
2. INSULATION & PROTECTION
3. CELL MEMBRANE CONSTITUENTS
HEALTH EFFECTS S
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Excess fat intake contributes to:
1. Obesity
2. Diabetes
3. Cancer
4. Heart disease
HOW?
1. HIGH FAT DIETS = HIGH KCAL DIETS
2. HIGH SATURATED FAT INTAKE RAISES
BLOOD CHOLESTEROL
3. HIGH FAT INTAKES MAY PROMOTE
CANCER
DIETARY RECOMMENDATIONS
1. LIMIT TOTAL FAT INTAKE TO <30% OF KCALS
EXAMPLE: IF 2000 KCAL DIET, THEN
2000 X .30 = 600 KCALS/9 KCALS PER GRAM = 65
GMS OF PROTEIN
2. LIMIT CHOLESTEROL TO <300 MG/DAY
3. SATURATED & POLYUNSATURATED FATS EACH
<10% OF KCALS
- Proteins are important in cell signaling,
immune responses, cell adhesion, and
the cell cycle.
- Proteins are a necessary component in
animal diets.
● All proteins are polymers containing
chains of amino acids chemically bound
by amide (peptide) bonds.
● Most organisms use 20 naturally-
occurring amino acids to build proteins.
● The linear sequence of the amino acids in
S a protein is dictated by the sequence of
the nucleotides in an organisms’ genetic
code.
● alpha (a)- amino acids - the amino group
is attached to the first carbon in the chain
connected to the carboxyl carbon.

1. USE ALL FATS IN MODERATION

PROTEIN CHARACTERISTICS ?
*1 TSP FAT = 5 GM = 45 KCALS
PROTEIN SIZE -
2.BEWARE OF “HIDDEN FATS” – ADDED TO
● Very large polymers of amino acids with
CONVENIENCE FOODS, PROCESSED FOODS, & IN
molecular weights that vary from 6000
COOKING
amu to several million amu.
3.CHOOSE LEAN MEATS, SKINLESS POULTRY,
- Glucose(C6H12O6)=180 amu
NONFAT DAIRY PRODUCTS; LIMIT MEATS TO <7 OZ./DA
- Hemoglobin
4.CHOOSE FISH 2-3 TIMES/WEEK
(C2952H4664O832N812S8Fe4) = 65,000 amu
5.CHOOSE MONOUNSATURATED FATS – CANOLA, OLIV
PEANUT, OR SESAME OILS; AVOID HYDROGENATED OIL
6.LIMIT EGG YOLKS TO 3-4/WEEK
WEEK 4 - PROTEINS S
WHAT IS PROTEINS? ?
● Proteios - Greek word means primary or
of first importance.
● Biochemical molecules consisting of
polypeptides joined by peptide bonds
● Proteins are too large to pass through cell
between the amino acid and carboxyl
membranes.
groups of amino acid residues.
● Contained within the cells where they
● Proteins perform a number of vital
were formed unless the cell is damaged
functions:
by disease or trauma.
- Enzymes are proteins that act as
- Persistent large amounts of protein in the
biochemical catalysts.
urine are indicative of damaged kidney
- Many proteins have structural or
cells.
mechanical functions (e.g., actin and
- Heart attacks can also be confirmed by
myosin in muscles).
the presence of certain proteins in the
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 blood that are normally confined to cells
in heart tissue.
ACID BASE PROPERTIES OF PROTEINS - foreign substances. Another protective
● Proteins take the form of zwitterions.
They have characteristic isoelectric
points, and can behave as buffers in
solutions.
● The tendency for large molecules to
remain in solution or form stable
colloidal dispersions depends on the
repulsive forces acting between
molecules with like charges on their
surfaces.
- When proteins are at a pH in which there
is a net positive or negative charge, the
like charges cause the molecules to repel
one another, and they remain dispersed.
- When the pH is near the isoelectric point,
the net charge on the molecule is zero,
and the repulsion between proteins is
small. This causes the protein molecules
to clump and precipitate from solution.
Proteins perform crucial roles in all biological
processes.
1. CATALYTIC FUNCTION: Nearly all
reactions in living organisms are
catalyzed by proteins functioning as
enzymes. Without these catalysts,
biological reactions would proceed much
more slowly.
2. STRUCTURAL FUNCTION : In animals’
structural materials other than inorganic
components of the skeleton are proteins,
such as collagen (mechanical strength of
skin and bone) and keratin (hair, skin,
fingernails).
3. STORAGE FUNCTION: Some proteins
provide a way to store small molecules or
ions
- E.g. ovalbumin (used by embryos
developing in bird eggs), casein (a milk
protein) and gliadin (wheat seeds), and
ferritin (a liver protein which is
complexed with iron ions).
4. PROTECTIVE FUNCTION: Antibodies are
proteins that protect the body from
disease by combining with and
destroying viruses, bacteria, and other
function is blood clotting carried out by
thrombin and fibrinogen.
5. REGULATORY FUNCTION: Body processes
regulated by protein include growth
(growth hormone) and thyroid function
(thyrotropin).
6. NERVE IMPULSE TRANSMISSION: Some
proteins act as receptors for small
molecules that transmit impulses across
the synapses that separate nerve cells.
- Eg. rhodopsin in vision
7. MOVEMENT FUNCTION: The proteins
actin and myosin are important in muscle
activity, regulating the contraction of
muscle fibers.
8. TRANSPORT FUNCTION: Some proteins
bind small molecules or ions and
transport them through the body.
- Serum Albumin is a blood protein that
carries fatty acids between fat (adipose)
tissue and other organ.
- Hemoglobin carries oxygen from the
lungs to other body tissues.
- Transferrin is a carrier of iron in blood
plasma.
● A typical human cell contains 9000
different proteins; the human body
contains about 100,000 different
proteins.
PROTEIN STRUCTURE -
● Proteins can be classified on the basis of
their structural shapes:
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 1. FIBROUS PROTEINS - made up of long
rod-shaped or string like molecules that
can intertwine with one another and
form strong fibers. o Insolubleinwater
- Major components of connective tissue,
elastic tissue, hair, and skin (e.g.,
collagen, elastin, and keratin).
2. GLOBULAR PROTEINS - more spherical in
shape – dissolve in water or form stable
suspensions.
- Not found in structural tissue but are ● The a-helix is held in this shape by
transport proteins, or proteins that may hydrogen bonding interactions between
be moved easily through the body by the amide groups, with the side chains
circulatory system (e.g., hemoglobin and extending outward from the coil.
transferrin.)
● The structure of proteins is much more
complex than that of simple organic
molecules. ● The amount of a-helix coiling in proteins
● Many protein molecules consist of a is highly variable. In a keratin (hair),
chain of amino acids twisted and folded myosin (muscles), epidermis (skin), and
into a complex three-dimensional fibrin (blood clots), two or more helices
structure. coil together (supracoiling) to form
● The complex 3D structures of proteins cables.
impart unique features to proteins that ● Another secondary structure is the
allow them to function in diverse ways. b-pleated sheet, in which several protein
● There are four levels of organization in chains lie side by side, held by hydrogen
protein structure: primary, secondary, bonds between adjacent chains:
tertiary, and quaternary/
PRIMARY STRUCTURE -
● It is the linear sequence of the side
chains that are connected to the protein
backbone:
● The b-pleated sheet structure is less
common than the a-helix; it is found
extensively only in the protein of silk.
● Each protein has a unique sequence of
amino acid residues that cause it to fold
into a distinctive shape that allows the
protein to function properly. Primary
structure of human insulin:
SECONDARY STRUCTURE -
● Hydrogen bonding causes protein chains
to fold and align to produce orderly
patterns secondary structures. TERTIARY STRUCTURE -
● The a-helix is a single protein chain ● The tertiary structure of a protein refers
twisted to resemble a coiled helical to the bending and folding of the protein
spring. into a specific three-dimensional shape.
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 ● These structures result from four types of
interactions between the R side chains of
the amino acids residues:
1. DISULFIDE BRIDGES can form between
two cysteine residues that are close to
each other in the same chain, or between
cysteine residues in different chains.
These bridges hold the protein chain in a
loop or some other 3D shape.
2. SALT BRIDGES are attractions between
ions that result from the interactions of
the ionized side chains of acidic amino
acids (— COO-) and the side chains of
basic amino acids (— NH3+).
3. Hydrogen bonds can form between a
variety of side chains, especially those
that contain: Hydrogen bonding also
influences the secondary structure, but
here the hydrogen bonding is between R
groups, while in secondary structures it is
between the C=O and NH portions of the
backbone.
4. HYDROPHOBIC INTERACTIONS result
from the attraction of nonpolar groups,
or when they are forced together by their
mutual repulsion of the aqueous solvent.
These interactions are particularly
important between the benzene rings in
phenylalanine or tryptophan. This type of
interaction is relatively weak, but since it
acts over large surface areas, the net
effect is a strong interaction.
● The compact structure of globular
proteins in aqueous solution, in which
the nonpolar groups are pointed inward,
away from the water molecules.
salt bridges, hydrogen bonds, or
hydrophobic interactions forming a larger
protein complex.
- Each of the polypeptide subunits has its
own primary, secondary, and tertiary
structure.
- The arrangement of the subunits to form
a larger protein is the quaternary
structure of the protein.
PROTEIN COMPOSITION -
● Proteins can also be classified by
composition
● Simple proteins contain only amino acid
residues. Conjugated proteins also
contain other organic or inorganic
components, called prosthetic groups.
o Nucleoproteins — nucleic acids (viruses).
o Lipoproteins — lipids (fibrin in blood, serum
lipoproteins
o Glycoproteins — carbohydrates (gamma
globulin in blood, mucin in saliva)
o Phosphoproteins — phosphate groups (casein
in milk)
o Hemoproteins — heme (hemoglobin,
myoglobin, cytochromes)
o Metalloproteins — iron (ferritin, hemoglobin)
or zinc (alcohol dehydrogenase)
AMINO ACIDS -
● Classified by the polarity of the R group
side chains, and whether they are acidic
or basic:
- Neutral,nonpolar
- Neutral, polar
- Basic, polar (contains additional amino
group).
- Acidic, polar (contains an additional
carboxylate group).

● All of the amino acids are also known by

QUATERNARY STRUCTURE
● When two or more polypeptide chains
are held together by disulfide bridges,
a three letter and one-letter
abbreviations.
● Since the amino acids (except for glycine)
contain four different groups connected
to the a-carbon, they are chiral, and exist
- in two enantiomeric forms:
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● The amino acids in living systems exist
primarily in the L form.
● Because amino acids contain both an
acidic and a basic functional group, an
internal acid-base reaction occurs,
forming an ion with both a positive and a
negative charge called a zwitterion:
AMINO ACIDS: ZWITTERIONS
● Lowering the pH of the solution causes
the zwitterion to pick up a proton.
● Increasing the pH of the solution causes
the zwitterion to lose a proton.
● Since at the Ph of the solution affects the
charge on the amino acid, at some pH,
the amino acid will form a zwitterion.
This is called the isoelectric point.
● Each amino acid (and protein) has a
characteristic isoelectric point; those
with neutral R groups are near a pH of 6,
those with basic R groups have higher
values, and those with acidic R groups
have lower values.
● Because amino acids can react with both
H30+ and OH-, solutions of amino acids
and proteins can act as buffers. (E.g.,
blood proteins to help regulate the pH of
blood).
OXIDATION REACTION
● Amino acids can undergo any of the
reactions characteristic of the functional
groups in the structure.
● Cysteine is the only amino acid that
contains a sulfhydryl (thiol, R-SH) group.
Thiols are easily oxidized to form
disulfide bonds (R-S-S-R). This allows
cysteine to dimerize to form cystine:
PEPTIDE FORMATION -
● Amides can be thought of as forming
from the reaction of an amine and a
carboxylic acid:
● In the same way, two amino acids can
- combine to form a dipeptide, held
together by a peptide bond:
PEPTIDES -
● Short chains are referred to as peptides,
chains of up to about 50 amino acids are
polypeptides, and chains of more than 50
amino acids are proteins. (The terms
protein and polypeptide are often used
interchangeably.)
● Amino acids in peptide chains are called
amino acid residues.
- The residue with a free amino group is
called the Nterminal residue, and is
written on the left end of the chain.
- The residue with a free carboxylate
group is called the C-terminal residue,
- and is written on the right end of the
chain.
● Peptides are named by starting at the N-
terminal end and listing the amino acid
residues from left to right.
● Large amino acid chains are unwieldy to
draw in their complete forms, so they are
usually represented by their three-letter
abbreviations, separated by dashes:
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- Gly-Ala (Gly = N-terminal, Ala =
C-terminal)
- Ala-Gly (Ala = N-terminal, Gly =
C-terminal)
● The tripeptide alanyl glycyl valine can be
written as Ala-GlyVal. (There are five
other arrangements of these amino acids
that are possible.)
● Insulin has 51 amino acids, with 1.55x106
different possible arrangements, but the
body produces only one.
OXYTOCIN & VASOPRESSIN
● More than 200 peptides have been
identified as being essential to the body’s
proper functioning.
● Vasopressin and oxytocin are
nonapeptide hormones secreted by the
pituitary gland. Six of the amino acid
residues are held in a loop by disulfide
bridges formed by the oxidation of two
cysteine residues.
● Even though the molecules are very
similar, their biological functions are
quite different:
- VASOPRESSIN is known as antidiuretic
hormone (ADH) because it reduces the
amount of urine formed, which causes
the body to conserve water. It also raises
blood pressure.
- OXYTOCIN causes the smooth muscles of
the uterus to contract, and is
administered to induce labor. It also
stimulates the smooth muscles of
mammary glands to stimulate milk
ejection.
ADRENOCORTICOTROPIC HORMONE
● Adrenocorticotropic hormone (ACTH) is
a 39-residue peptide produced in the
pituitary gland. It regulates the
production of steroid hormones in the
cortex of the adrenal gland.
- HEMOGLOBIN
-
● Hemoglobin is made of four subunits:
two identical alpha chains containing 141
AA’s and two identical beta chains
containing 146 AA’s. Each subunit
contains a heme group located in
crevices near the exterior of the
molecule.
● A hemoglobin molecule in a person
suffering from sickle cell anemia has a
one-amino acid difference in the sixth
position of the two b-chains of normal
HbA (a glutamate is replaced with a
valine).
● This changes the shape of red blood cells
that carry this mutation to a
characteristic sickle shape, which causes
the cells to clump together and wedge in
capillaries, particularly in the spleen, and
cause excruciating pain.
● Cells blocking capillaries are rapidly
destroyed, and the loss of these red
blood cells causes anemia.
-
PROTEIN HYDROLYSIS -
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● Amides can be hydrolyzed under acidic or produce substances that induce
basic conditions. immunity.
● The peptide bonds in proteins can be ● Proteins can also be denatured by
broken down under acidic or basic heavy-metal ions such as Hg2+, Ag+, and
conditions into smaller peptides, or all Pb2+ that interact with —SH and
the way to amino acids, depending on carboxylate groups.
the hydrolysis time, temperature and pH. - Organic materials containing Hg
(mercurochrome and merthiolate) were
common topical antiseptics.
- Heavy-metal poisoning is often treated
- The digestion of proteins involves with large doses of raw egg white and
hydrolysis reactions catalyzed by milk; the proteins in the egg and milk
digestive enzymes. bind to the metal ions, forming a
- Cellular proteins are constantly being precipitate, which is either vomited out
broken down as the body resynthesizes or pumped out.
molecules and tissues that it needs. PROTEIN REACTIVITY -
PROTEIN DENATURATION -
● Proteins are maintained in their native
state (their natural 3D conformation) by
stable secondary and tertiary structures,
and by aggregation of subunits into
quaternary structures.
● Denaturation is caused when the folded
native structures break down because of
extreme temps. or pH values, which
disrupt the stabilizing structures. The
structure becomes random and
WEEK 5 - ENZYMES S
disorganized.
ENZYMES ?
● are biological catalysts that speed up the
rate of the biochemical reaction.
● most enzymes are 3-D globular proteins
(tertiary and quaternary structure)
● are extremely efficient catalysts, and
● Most proteins are biologically active only some can increase reaction rates by
over a temperature range of 0C to 40C. 10^20 times that of the uncatalyzed
● Heat is often used to kill microorganisms reactions
and deactivate their toxins. The protein
toxin from Clostridium botulinum is
inactivated by being heated to 1000C for
a few minutes; heating also deactivates
the toxins that cause diphtheria and
tetanus.
● Heat denaturation is used to prepare
vaccines against some diseases. The
denatured toxin can no longer cause the
disease, but it can stimulate the body to

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 IMPORTANCE
● Enzymes play an important role in
Metabolism, Diagnosis, and Therapeutics.
● All biochemical reactions are
enzyme-catalyzed in the living organisms
● The level of enzymes in the blood are of
diagnostic importance (is a good
indicator in disease such as myocardial
infarction)
● Enzymes can be used therapeutically
such as digestive enzymes.
ROLES OF ENZYMES IN 3 MAJOR WAYS
● Enormous catalytic power
● Highly specific in the reactions they
catalyze
● Their activity as catalysts can be
regulated.
CATALYTIC EFFICIENCY -
● A comparison of free energy of
activation profiles for catalyzed and
uncatalyzed reactions. The free energy of
activation of the catalyzed reaction is
much less than that of the uncatalyzed
reaction.
● Catalysts increase the rate of chemical
reactions without being used up in the
process.
SPECIFICITY
● Enzymes are often very specific in the
type of reaction they catalyze, and even
the particular substance that will be
involved in the reaction.
- ● Strong acids catalyze the hydrolysis of
any amide or ester, and the dehydration
of any alcohol. The enzyme urease
catalyzes the hydrolysis of a single amide,
urea.
● Enzymes have varying degrees of
specificity for substrates
● Enzymes may recognize and catalyze:
- a single substrate
- a group of similar substrates
- a particular type of bond
-
REGULATION -
● The catalytic behavior of enzymes can be
regulated.
● The cell controls the rates of these
reactions and the amount of any given
product formed by regulating the action
of the enzymes.
STRUCTURE OF ENZYMES -
ACTIVE SITES -
● Enzyme molecules contain a special
pocket or cleft called the active sites.
● The active site of an enzyme is the
region that binds substrates, co-factors,
and prosthetic groups and contains
residue that helps to hold the substrate.
-
● A change in the shape of protein affects
the shape of the active site and function
of the enzyme.
● Can be further subdivided into:
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 CO-FACTORS
● is the nonprotein molecule which carries
out chemical reactions that can not be
performed by standard 20 amino acids.
● 2 TYPES: 1. Organic co-factors 2.
Inorganic co-factors
TYPES OF ORGANIC FACTORS ? ● It is First push to start a reaction.
● PROSTHETIC GROUP - is a nonprotein
component, tightly bound to apoenzyme
by covalent bonds.
- Ex: flavins, heme groups, biotin
● COENZYME - is a nonprotein component,
loosely bound to apoenzyme by
noncovalent bonds
- Ex: NAD+, vitamins or compound derived
from vitamins.
- SUBSTRATE -
● The reactant in biochemical reaction
● When a substrate binds to an enzyme it
forms an enzyme-substrate complex
ACTIVATION ENERGY OR -
ENERGY OF ACTIVATION -
● All chemical reactions require some
amount of energy to get them started.
O
R
● This energy is called ACTIVATION
ENERGY
MECHANISM OF ACTION OF ENZYME -
● Enzymes increase reaction rates by
decreasing the Activation energy:
● Enzyme-Substrate Interactions:
- Formation of Enzyme substrate complex
by:
￭ Lock-and-Key Model
￭ Induced Fit Model

● APOENZYME - anenzyme with its

co-factor removed. An enzyme without
its non protein moiety and is inactive.
● HOLOENZYME - an active enzyme with its
nonprotein component (small organic
molecules, metal ions)
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 LOCK- AND- KEY MODEL
● In the lock-and-key model of enzyme
action:
- The active site has a rigid shape.
- Only substrates with the matching shape
can fit.
- The substrate is a key that fits the lock of
the active site.
INDUCED FIT MODEL
● In the induced-fit model of enzyme
action:
- the active site is flexible, not rigid
- the shapes of the enzyme, active, site.
and substrate adjust to maximize the fit,
which improves catalysis
- there is a greater range of substrate
specificity.
ENVIRONMENTAL CONDITION -
● Extreme temperatures are the most
dangerous.
- High temps may denature (unfold) the
enzyme
- - pH ( most like 6 - 8 pH near neutral
- Substrate concentration
ENVIRONMENTAL FACTORS -
OPTIMUM TEMPERATURE - the temp at
which enzymatic reaction occurs fastest.
pH also affects the rate of enzyme-substrate
complexes.
- Most enzymes have an optimum pH of
around 7 (neutral)
- Some prefer acidic or basic conditions.
SUBSTRATE CONCENTRATION & -
-
REACTION RATE -
● The rate of reaction increases as
substrate concentration increases (at
constant enzyme conc.)
● Maximum activity occurs when the
enzyme is saturated (when all enzyme
are binding substrate)
REVERSIBLE COMPETITIVE INHIBITION -
● A competitive inhibitor:
- Has a structure like a substrate.
- Competes with the substrate for the
active site.
- Has its effect reversed by increasing
substrate concentration.
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 ● This classification is based on the type of
reactions catalyzed by the enzymes.
● There are 6 major classes.
● Each class is further divided into
subclasses, sub-sub-classes to describe
the huge number of different
enzyme-catalyzed reactions.

NONCOMPETITIVE INHIBITION -
● A noncompetitive inhibitor:
- Has a structure different than the
substrate.
- Distorts the shape of the enzyme, which
alters the shape of the active site.
- Prevents the binding of the substrate
- Cannot have its effect reversed by adding
more substrate.

ENZYMES SUBSTRATE -

NOMENCLATURE OF ENZYMES -
● An enzyme is named according to the
name of the substrate it catalyzes.
● Some enzymes were named before a
systematic way of the naming enzyme
was formed.
- Ex: pepsin, trypsin, rennin
● By adding the suffix -ASE at the end of
the name of the substrate.

CLASSIFICATION OF ENZYMES -
● A systematic classification of enzymes
ACTIVATION OF ZYMOGENS -
has been developed by the International
● Zymogens are a group of proteins that
Enzyme Commission.
display no catalytic activity but can be

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 transformed into active enzymes within
an organism.
● A zymogen is an inactive precursor of an
enzyme, especially those that catalyze
reactions involving the breakdown of
proteins.

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