Biochemistry Lecture Notes Cover Key Concepts for Health Sciences Students

By the end of this course the students
are expected to:

a. identify the structure of the
different functional groups
and biomolecules
(carbohydrates, proteins,
lipids, and nucleic acids)
b. correlate structure with the
biological functions of the
biomolecules
c. understand the importance
of transmission and
expression of genetic
information
BIOCHEMISTRY LECTURE d. Describe the pathways that

lead to the degeneration and
storage of metabolic fuel
COMPILED NOTES e. Explain derangement in

metabolic disorders in
relation to health , nutrition,
and disease
f. Apply principles of
biochemistry to the student
This course is intended primarily for health allied sciences students who need a working course
knowledge of the essentials in biochemistry as well as basic principles of organic chemistry.
Focus: Biochemistry as a science with clinical applications
TOPICS COVERED:
 Carbohydrates
 Enzymes
 Proteins
Prepared and compiled by:
SWU PHINMA  Lipids
COLLEGE OF
PHARMACY  Nucleic Acids
C.[Type text] Page 0
BIOCHEMISTRY INTRODUCTION MEDICINE
 Physiology
Etymology of BIOCHEMISTRY: BIO (life) Alchemy (Cast together)  Biochemistry helps one understand the biochemical changes and related physiological alteration in
the body.
 chemistry of life or study of the chemistry of living organism  Pathology
 Branch of chemistry that is concerned with the biological molecules of living organisms; its  Based on the symptoms described by the patient, physician can get clue on the biochemical change
and the associated disorder
structure, properties , functions and processes they undergo.
 It is studied through biochemical changes
 Study of the chemical substances found in living organism and chemical interactions of these  There are many disorders due to hormonal imbalance specially women and children. The formation of hormones
substances with each other (definition; H. Stephen Stoker) in the normal body function is taught in biochemistry by which the physician can understand the concerned
problem during treatment
Biochemistry is a field in which new discoveries are made almost daily about how cells manufacture the
molecules needed for life and how the chemical reactions by which life is maintained occur. DRUG FORMULATION
The knowledge explosion that has occurred in the field of biochemistry during the last decades of the
twentieth century and the beginning of the twenty-first is truly phenomenal.  Drug constitution
 Biochemistry gives an idea of the constitution of the drug, its chances of degradation with varying
Biology – living things temperature, etc. How modification in its chemistry helps improve efficiency, minimize side effects,
Physiology – branch of biology that deals with functions and activities of life or living matter (organs, tissues etc.
or cells)  Half-life/biochemical test
 This is a test done on biochemical drugs to know how long a drug is stable (shelf-life and expiration
date) when kept and so temperature.
B I O M O L E C U L E S: Chemical substances found within a living organism.  Drug storage
• Bioinorganic: Do not contain carbon  The storage condition required can be estimated by biochemical test. EXAMPLE: many enzymes,
• Water (70%) hormones are stored for dispensing. these get deteriorated over time due to temperature or
oxidation, contamination and also due to improper storage
• Inorganic salts (5%)
 Drug metabolism
• Bioorganic: Contain carbon
 It also gives an idea of how drug molecules are metabolized by many biochemical reactions in
• Proteins (15%) presence of enzymes. This helps to avoid drugs which have poor metabolism or those with excessive
• Lipids (8%) side effects from being prescribed or dispensed to the patient.
• Carbohydrates (2%)
Top 5 elements present in the human body: H, Ca, C, N, O

2nd top 5 elements present in the human body: Na, K, P, S, Cl
Trace elements that are required by the human body: Mg, V, Cr, Mn, Fe, Co, Cu, Zn, B, F, Si, Ge, Se, Br, I
IMPORTANCE OF BIOCHEMISTRY
NUTRITION
 Food Chemistry
 gives an idea of what we eat, it’s components like carbohydrates, proteins, fats, etc. and also the
possible physiological alteration due to their deficiency
 Nutritional values and limits
 the importance of vitamins, minerals, essential fatty acids, their contribution to health were known.
Physician can prescribe to limit usage of certain food like excess sugar for diabetes, excess oil for
heart and lung problem prone patients etc.
 Nutrition deficiency- In the present scenario many people rely in taking multivitamin and minerals for better
health: the function and role of the vitamins is described only by biochemistry
by: C.A.U, RPh Page 1

ALDOSE VS. KETOSE
CARBOHYDRATES
• Other name: __________________
• any of a large group of organic compounds occurring in foods and
living tissues and including sugars, starch, and cellulose.
• contain __________ and _______ in the same ratio as water (2:1)
with the general formula __________ or ____________.
• Is a polyhydroxy aldehyde (aldose), a polyhydroxy ketone (ketose),
or a compound that yields polyhydroxy aldehydes or polyhydroxy
ketones upon hydrolysis.
Give the 6 functions of Carbohydrates: CHIRALITY: Handedness in molecules

1. Importance:
 In human body chemistry, right-handed and left-handed forms of a molecule often elicit different
2. responses within the body.
 Sometimes both forms are biologically active, each form giving a different response; sometimes
3. both elicit the same response, but one form’s response is many times greater than that of the
other; and sometimes only one of the two forms is biochemically active.
4.  D- epinephrine is 20x greater than its response to L-epinephrine
 Building blocks of monosaccharides are right-handed ( D-glucose)
5.  Buildling blocks of proteins L-phenylalanine
6.
CLASSIFICATION OF CARBOHYDRATES AS TO MOLECULAR SIZE:

CLASSIFICATION SUGAR UNIT GIVE AT LEAST 1 EXAMPLE
How does carbohydrates broken down? Illustrate the trend from most
complex to simplest.
• CHIRAL CENTER - an atom in a molecule that has four different groups tetrahedrally bonded to it.
• CHIRAL MOLECULE- molecule whose mirror images are not superimposable
• ACHIRAL MOLECULE - molecule whose mirror images is superimposable
GUIDELINES FOR IDENTIFYING CHIRAL CENTERS

 A carbon atom involved in a multiple bond (double or triple bond) cannot be a chiral center since it
has fewer than four groups bonded to it. To have four groups present, all bonds about the chiral
center must be single bonds.
 A carbon atom that has two like groups bonded to it cannot be a chiral center since it does not
meet the requirement of four different groups.
 The commonly encountered entities --CH3 and --CH2 in a structural formula never involve chiral
centers because of the presence of two or more like hydrogen atoms.

 Carbon atoms in a ring system, if not involved in multiple bonding, can be chiral centers.
 Such carbon atoms have four bonds—two to neighboring atoms in the ring and two to substituents
on the ring.
 Chirality occurs when both (1) the two substituents are different and (2) the two “halves” of the
ring emanating from the chiral center are different.
DO NOW:
INSTRUCTION:
Isomerism
 Indicate whether the encircles carbon atom in each of the following molecules is  definition:
a chiral center or not (achiral) ______________________________________________________________________________
 Indicate how many possible chiral center is possible

STEREOISOMERISM DO NOW:
INSTRUCTION: Characterized the members of each of the following pairs of structure as: Enantiomers,
isomers that have the same molecular Diasteriomer, Niether enantiomer nor diasteriomer
and structural formulas but differ in the
orientation of atoms in space.
SUBTYPES OF STEREOISOMERISM:
• ENANTIOMERS
• “enantios” opposite
• stereoisomers whose
molecules are
nonsuperimposable
• Left & right-handed Pairs:
• DIASTEROMERS 1. A and B:___________________ 6. B and C: _______________________
• are stereoisomers whose 2. C and D:___________________ 6. C and E: _______________________
molecules are not mirror 3. D and G:___________________ 6. E and F: _______________________
images of each other. 4. A and C:___________________ 6. F and G: _______________________
5. A and E:___________________ 6. E and G: _______________________
FISCHER PROJECTION STRUCTURES OF MONOSACCHARIDES
optical
Carbon atoms Chiral carbons
isomers
Ruling
Aldohexose (6c)
 1st chiral carbon – OH alternating right and left
Aldopentose (5c)  2nd chiral carbon – OH alternating 2 rights and 2 lefts
Aldotetrose (4c)  3rd chiral carbon – OH alternating 4 rights and 4 lefts
 4th chiral carbon – OH alternating 8 rights and 8 left
Ketohexose (6c)
Ketopentose (5c)

Aldoses GUIDELINES:
1. Hemiacetal ring system:
viewed “edge on” oxygen ring atom
2. D or L isomer: position of
CH2OH group on the highest carbon
atom
3. a or B configuration
(anomers): determined the position of
the -OH on carbon 1 related CH2OH
group
4. Position of the remaining –OH
NOTES:
Ketoses

CLASSIFICATION: Base on MOLECULAR SIZE Pentoses of physiologic importance.
Sugar Where Found Biochemical Importance Clinical
MONOSACCHARIDE Significance
- is a carbohydrate that contains a __________ polyhydroxy aldehyde or polyhydroxy ketone unit. D-Ribose Nucleic acids Structural elements of nucleic acids and
- _________ be broken down into simpler units by hydrolysis reactions (DNA sugar) coenzymes, eg, ATP, NAD, NADP,
- Naturally occurring monosaccharides have from three to seven carbon atoms; five- and six-carbon flavoproteins. Ribose phosphates are
species are especially common. intermediates in pentose phosphate
- Pure monosaccharides are ___________, ___________, _____________________. pathway
Tabulation of biochemically important MONOSACCHARIDES
D-Ribulose Formed in metabolic Ribulose phosphate is an intermediate in
C atoms RCHO RCOR RCHO RCOR
processes. pentose phosphate pathway.
3 triose triulose glyceraldehyde dihydroxyacteone
(C3H6O3) D-Arabinose Gum arabic. Plum and Constituent of glycoproteins.
4 tetrose tetrulose -Erythrose -Erythroluse cherry gums.
(C4H8O4) -Threose D-Xylose (aka Wood gums, Constituent of glycoproteins.
5 pentose pentulose -Ribose -Ribulose wood sugar) proteoglycans,
(C5H10O5) -Arabinose glycosaminoglycans.
-Xylose -Xylulose D-Lyxose Heart muscle. A constituent of a lyxoflavin isolated from
-Lyxose human heart muscle.
6 hexose hexulose -Allose -Psicose
(C6H12O6) -Altrose -Fructose L-Xylulose Intermediate in uronic Found in urine in
-Glucose -Sorbose acid pathway. essential
-Mannose
pentosuria.
-Gulose
-Idose
-Galactose 5C Ribose
-Talose
D-Ribose
- a component of ribonucleic acids (RNAs) and energy-rich compounds such as adenosine triphosphate
3C D-Glyceraldehyde & Dihydroxyacetone (ATP).
- The compound 2-deoxy-D-ribose is also important in nucleic acid chemistry. This monosaccharide is a
• The simplest of the monosaccharides, these two trioses are important intermediates in the process of glycolysis,
a series of reactions whereby glucose is converted into two molecules of pyruvate. D-Glyceraldehyde is a chiral
component of DNA molecules.
molecule, but dihydroxyacetone is not.
- The prefix deoxy- means “_______________”;
the structures of ribose and 2-deoxyribose differ
D-glyceraldehyde Structure Dihydrocyacetone
in that the latter compound lacks an oxygen
Has chiral carbon or center Does not possess chiral carbon or atom at carbon 2.
center
L and D forms are possible L and D form is not possible

D- Ribose is a ___________. D-glucose, D-galactose, and D-fructose
Aldose Ketose are all ____________
If carbon 3 and its accompanying -H and -OH groups were eliminated

from the structure of D-glucose, the remaining structure would be
that of D-ribose

Hexoses of physiologic importance 6C Galactose
Sugar Source Importance Clinical Significance
D-Galactose
D-Glucose Fruit juices. Hydrolysis The “sugar” of the body. The sugar Present in the urine
-is synthesized from glucose in the _______________ for use in lactose (milk sugar), a disaccharide consisting
(Grape of starch, cane sugar, carried by the blood, and the (glycosuria)in diabetes
of a ____________ and _____________
sugar, maltose, and lactose. principal one used by the tissues mellitus owing to raised
- sometimes called brain sugar because it is a component of glycoproteins found in brain and nerve
dextrose, blood glucose
tissue.
blood sugar) (hyperglycemia).
- D-Galactose is also present in the chemical markers that distinguish various types of blood—A, B, AB, and O
D-Galactose and D-glucose are epimers (diastereomers that differ

D-Fructose Fruit juices. Honey. Can be changed to glucose in the Hereditary fructose
only in the configuration at one chiral center)
(levulose, Hydrolysis of cane liver and so used in the body. intolerance leads to
fruit sugar, sugar and of inulin fructose accumulation and
two compounds differ only in the configuration of the –OH group
dietary (from the Jerusalem hypoglycemia.
and -H group on carbon 4.
sugar) artichoke).
Epimers are diastereomers whose molecules differ only in the
D-Galactose Hydrolysis of lactose. - Can be changed to glucose in the Failure to metabolize leads configuration at one chiral center.
(brain sugar) (disaccharide liver and metabolized. Synthesized to galactosemia and
consisting of a glucose in the mammary gland to make the cataract
unit and a galactose lactose of milk. A constituent of 6C Fructose
unit) glycolipids and glycoproteins
(present in the brain) D-Fructose
- chemical markers that distinguish - D-Fructose is biochemically the most important ketohexose. It is also known as ____________and
various types ______________.
of blood—A, B, AB, and O - used as a ______________ not because it has fewer calories per gram than other sugars but
because less is needed for the same amount of sweetness.
D-Mannose Hydrolysis of plant A constituent of many

mannans and gums. glycoproteins. From the third to the sixth carbon, the structure of D-
fructose is identical to that of D-glucose. Differences at
carbons 1 and 2 are related to the presence of a ketone
group in fructose and of an aldehyde group in glucose.
6C Glucose
D-Glucose (Aka ___________, ___________, ____________) D- fructose Structure D-glucose

• Of all monosaccharides, D-glucose is the most abundant in nature and the most important from a
Hexose Hexose
human nutritional standpoint.
• D-Glucose ____________, _________. L-Glucose, on the other hand, __________, and the body
Ketose Aldose
cannot use it.
dextrose draws attention carbons 1 and 2 carbons 1 and 2 are
to the fact that the optically are related to the related to the presence of
active D-glucose, in presence of a an aldehyde group
aqueous solution, rotates
plane-polarized light to the ketone group in glucose. Identical
right. fructose. structure from C3-C6
Identical
blood sugar draws attention to the fact that blood contains dissolved glucose. The normal structure from
concentration of glucose in human blood is in the range of 70–100 mg/dL (1 dL = 100 mL). C3-C6

DISACCHARIDE Properties Reducing Reducing sugar Reducing sugar Non-reducing sugar
- carbohydrate that contains ____________________________________ sugar bec. 1 -has 3 isomeric (glucose ring can -No free hemiacetal or
unit of glucose form open to give an hemiketal moities
- ____________ bonded to each other
has a aldehyde or has free -The hemiacetal center
- crystalline, water-soluble substances hemiacetal hemiacetal glucose (anomeric carbon atom) of
- Example: Sucrose (table sugar) and lactose (milk sugar) carbon (C1) unit) each monosaccharides is
- Hydrolysis of a disaccharide produces _______ monosaccharide units. Forms: -form is sweeter involved in glycosidic
a-maltose than & more water linkage results to 2
Two monossacharides are bonded together by a glycosidic bond B-maltose soluble than -form. hemiacetal center
Open chain -form is present
form with long stored ice
cream producing a
gritty crystalized
texture.
Reaction Maltase Cellobiase Hydrolysis of lactose Sucrase use to break ,(1-
of causing by the enzyme 2) glycosidic linkage of
Enzymes hydrolysis (or lactase forms units glucose to form equimolar
in an acidic of --D-galactose & mic=xture of glucose and
condition) -D- glucose fructose
2
________________ is the bond in a disaccharide resulting from the reaction between the hemiacetal carbon D-Glucose
Maltose
atom -OH group of one monosaccharide and an -OH group on the other monosaccharide
- malt sugar, one-third as sweet as ___________, is produced whenever the polysaccharide starch
Tabulation of Common DISACCHARIDES
breaks down, as happens in plants when seeds germinate and in human beings during starch
Feature Maltose Cellobiose Lactose Sucrose digestion.
Common Malt sugar (1/3 Cellobiose Milk sugar Table sugar - It is a common ingredient in baby foods and is found in malted milk. Malt (germinated barley that
Names as sweet has been baked and ground) contains maltose.
as sucrose) - an interesting compound because of its use in alcohol production (fermentation).
Source Digestion by Intermediate in Milk. May occur in Juice of sugar cane (20% by
amylase or the hydrolysis of urine during mass) & sugar beets (17%
hydrolysis of polysaccharide pregnancy. by mass)
starch. cellulose Clinical significance: Clinical significance:
Germinating In lactase deficiency, In sucrase deficiency,
cereals and Nursing mother malabsorption leads malabsorption leads to
malt. =7-8% to diarrhea and diarrhea and flatulence.
Cow’s milk = 4-5% flatulence
Structural 2 Glucose units 2Glucose units --D-galactose & --D glucose &
Units - -D glucose --D-glucose & -D- glucose --D- fructose Maltose is a reducing sugar
& -D- glucose
- D-glucose
Glycosidic (1-4) (head to (1-4) (head to (1-4) (head to tail) ,(1-2) OH group of C2 of
Linkage tail) tail) Fructose(hemiacetal) + OH
group on C1 of D-glucose
(hemiacetal)
(head to head)

2
Cellobiose D-Fructose
D-Glucose Sucrose
D-Glucose
Like maltose, cellobiose contains two _____________ monosaccharide units. It differs from maltose in that
one of the D-glucose units—the one functioning as a hemiacetal—must have a or b configuration instead of Composed of a-D-glucose and b-D-fructose.
the a-configuration for maltose. This change in configuration results in a b(1 : 4) glycosidic linkage. table sugar, is the most abundant of all disaccharides and
occurs throughout the plant kingdom
The glycosidic linkage is not a (1 : 4) linkage, as was the case
for maltose, cellobiose, and lactose. It is instead an a, b(1 : 2)
glycosidic linkage. The - OH group on carbon 2 of D-fructose
(the hemiacetal carbon) reacts with the -OH group on
carbon 1 of D-glucose (the hemiacetal carbon).
Sucrase, the enzyme needed to break the a, b(1 : 2) linkage in sucrose, is

D-Galactose present in the human body. Sucrose hydrolysis (digestion) produces an equimolar mixture of glucose and
D-Glucose Lactose fructose called _______________.
When sucrose is cooked with acid-containing foods such as fruits or berries, partial hydrolysis takes place,
forming some invert sugar. Jams and jellies prepared in this manner are actually sweeter than the pure
milk sugar (major sugar found in milk) sucrose added to the original mixture because one-to-one mixtures of glucose and fructose taste sweeter
Uses: ingredient in ___________________ that are designed to than sucrose.
simulate mother’s milk.
-LACTOSE AS AN EXCIPIENT used as a filler or filler-binder. Changing Sugar Patterns:
-cost effectiveness; 1. H F C S / High-fructose corn syrup
-availability; - sweetener for food and beverages
-bland taste; A. HFCS42- _____________________________________
-low hygroscopicity; B. HFCS90- ______________________________________
-compatibility with active ingredients and other excipients; C. HFCS55- ______________________________________
-excellent physical and chemical stability; 2. Sugar substitutes of sucrose
- water solubility - saccharin- _________________________________________________________________
- sodium cyclamate - _________________________________________________________
Conditions associated with Lactose - aspartame (nutra sweet)- ____________________________________________________
1. __________________ - used to describe the condition where milk-drinking ability continues into adulthood. 3. Derivatives of sucrose
2. __________________- a condition in which people lack the enzyme lactase, which is needed to hydrolyze a. Sucralose - is synthesized from sucrose by substitution of three chlorine atoms for hydroxyl
lactose to galactose and glucose. groups.
Causes: - heatstable
 Genetic defect - __________ sweeter than sucrose
 Physiological decline w/ age - calorie free
 Injury to the mucosal lining of the intestines b. neotame- an ________ derivative. The same two amino acids are present as in aspartame. It
3. ______________- caused by the absence of one or more of the enzymes needed for the conversion of differs structurally from aspartame in that a 3,3-dimethylbutyl group is attached to the terminal -NH2
galactose to glucose. group of aspartame. This “bulky” attachment prevents the breakdown of neotame into its
In people with this condition, galactose and its toxic metabolic derivative galactitol (dulcitol) accumulate in component amino acids, as occurs for aspartame. Hence individuals with PKU can use neotame
the blood. without concern.
- can cause mental retardation in infants and even death - ____________ sweeter than sucrose

OLIGOSACCHARIDES Important parameters that distinguish various polysaccharides (or glycans) from each other are:
are carbohydrates that contain three to ten monosaccharide units bonded to each other via glycoside 1. The identity of the monosaccharide repeating unit(s) in the polymer chain.
linkages a. homopolysaccharide is a polysaccharide in which only one type of monosaccharide monomer is
Two naturally occurring oligosaccharides in onions, cabbage, broccoli, brussel sprouts, whole wheat, and all present.
types of beans: examples: starch, glucan, glycogen, cellulose, and chitin
a. _____________- trisaccharide, galactose, glucose, and fructose. b. heteropolysaccharide is a polysaccharide in which more than one (usually two) type of
b. _____________- tetrasaccharide , galactose, glucose, and fructose with additional galactose monosaccharide monomer is present.
Humans lack the digestive enzymes necessary to metabolize either raffinose or stachyose. Hence these examples: hyaluronic acid and heparin
oligosaccharides, when ingested in food, pass undigested into the large intestine causing discomfort. 2. The length of the polymer chain.
3. The type of glycosidic linkage between monomer units
c. Solanine, a toxin found in the __________ plant , is another example of an oligosaccharide-containing 4. The degree of branching of the polymer chain.
“complex” molecule.
- alkaloid and trisaccharides of Division of polysaccharides according to importance:
b-l-rhamnose, Storage Polysaccharides examples: ________________________________
b-d-glucose, Structural Polysaccharides examples: ______________________________
b-d-galactose Acidic Polysaccharides examples: __________________________________
Blood Types and Oligosaccharides
Biochemical markers - oligosaccharide molecules that are attached to the plasma membrane of red blood Storage Polysaccharides
cells is a polysaccharide that is a storage form for monosaccharides and is used as an energy source in cells.
Starch - a homopolysaccharide containing only glucose monosaccharide units.
The absence or presence of - It is the energy-storage polysaccharide in plants.
a fifth monosaccharide - aka ____________________
(attached to the second
galactose) determines blood
AMYLOSE AMYLOPECTIN
type. Type O blood lacks a
fifth monosaccharide unit. straight-chain glucose polymer, usually accounts for a branched glucose polymer, accounts for the remaining
Type A blood has N- 15%–20% of the starch 80%–85% of the starch.
acetylgalactosamine as a fifth - More water soluble because of increase in branching
unit. Type B blood has
galactose as a fifth unit. Type glucose units are connected by (1 : 4) glycosidic linkages. both (1 : 4) and (1 : 6)
AB blood contains both type
A and type B markers Glycogen
- is a branched polysaccharide containing only _______________ units.
- it is the glucose storage polysaccharide in humans and animals and sometimes referred to as animal
starch.
- Liver cells and muscle cells are the storage sites for glycogen in humans.
The glucose polymers amylose, amylopectin,and glycogen compare as follows in molecular size and degree
POLYSACCHARIDE of branching.
is a polymer that contains many monosaccharide units bonded to each other by glycosidic linkages.  Amylose: Up to 1000 glucose units; no branching
- _____________- an alternate name for a polysaccharide.  Amylopectin: Up to 100,000 glucose units;
are called complex carbohydrates, simple carbohydrates for mono & disaccharides. - branch points every 25–30 glucose units
Characteristic:  Glycogen: Up to 1,000,000 glucose units;
1. polysaccharides are not sweet and do not test positive in Tollens and Benedict’s solutions. - highly branch points every 8–12 glucose units
2. They have limited water solubility because of their size. However, the - OH groups present can These two opposing processes are called __________________ and ____________________, the formation
individually become hydrated by water molecules. The result is usually a thick colloidal suspension and decomposition of glycogen, respectively.
of the polysaccharide in water.
3. Polysaccharides, such as flour and cornstarch, are often used as thickening agents in sauces,
desserts, and gravy.

Structural Polysaccharides Glucagon
is a polysaccharide that serves as a structural element in plant cell walls and animal exoskeletons  Glucagon is a polypeptide hormone (29 amino acids) produced in the pancreas by alpha cells.
Cellulose – Gossypium hirsatum  It is released when blood-glucose levels are low.
-the structural component of plant cell walls,  Its principal function is to increase blood-glucose concentrations by speeding up the conversion of
-is the most abundant naturally occurring polysaccharide. glycogen to glucose (glycogenolysis) and gluconeogenesis in the liver. Thus glucagon’s effects are
-the “woody” portions of plants—stems, stalks, and trunks—have particularly high concentrations of this opposite those of insulin.
fibrous, water-insoluble substance.
- Like amylose(a-1:4), cellulose (b-1:4)is an unbranched glucose polymer Epinephrine
Chitin
 Epinephrine , also called adrenaline, is released by the adrenal glands in response to anger, fear, or
The 2nd most abundant naturally occurring polysaccharide, next to cellulose . Its function is to give rigidity to
excitement.
the exoskeletons of crabs, lobsters, shrimp, insects, and other arthropods. It also has been found in the cell
 Its function is similar to that of glucagon— stimulation of glycogenolysis, the release of glucose
walls of fungi.
from glycogen.
- contains galacturonic acid which is not found in cellulose
 Its primary target is muscle cells, where energy is needed for quick action.
 It also functions in lipid metabolism.
Acidic Polysaccharides
 polysaccharide with a disaccharide repeating unit in which one of the disaccharide components is an
amino sugar and one or both disaccharide components has a negative charge due to a sulfate group or
a carboxyl group.
 are heteropolysaccharides; two different monosaccharides are present in an alternating pattern
Hyaluronic Acid
 contains alternating residues of N-acetyl-b-Dglucosamine (NAG) and D-Glucuronate.
USES:
 Highly viscous hyaluronic acid solutions serve as ______________ in the fluid of joints,
 are also associated with the jelly-like consistency of the vitreous humor of the eye. (The Greek word
hyalos means “_________”; hyaluronic acid solutions have a glass-like appearance.)
Heparin
 small highly-sulfated polysaccharide with only 15–90 disaccharide residues per chain
USE:
 blood anticoagulant. It is naturally present in mast cells and is released at the site of tissue injury.
 It prevents the formation of clots in the blood and retards the growth of existing clots within the
blood. It does not, however, break down clots that have already formed.
 The source for pharmaceutical heparin is intestinal or lung tissue of slaughter-house animals (pigs
and cows).
Hormonal Control of Carbohydrate Metabolism

Insulin
 Insulin, a 51-amino-acid protein hormone produced by the beta cells of the pancreas.
 promotes the uptake and utilization of glucose by cells. Thus its function is to lower blood-glucose
levels.
 It is also involved in lipid metabolism.
 The release of insulin is triggered by high blood-glucose levels.
 The mechanism for insulin action involves insulin binding to protein receptors on the outer surfaces
of cells, which facilitates entry of glucose into the cells. Insulin also produces an increase in the
rates of glycogenesis, glycolysis, and fatty acid synthesis.
 Insulin is at the core of the metabolic disorder known as diabetes; either the body does not produce
enough insulin or body cells do not respond properly to the insulin that is produced.

ENZYMES TERMS DEFINITION
simple enzyme
Greek word en “___” and zyme “______”
Enzymes are biological catalyst that _____________________________________________ conjugated enzyme
Most of the enzymes are three dimensional globular proteins (tertiary and quaternary structure)
apoenzyme
Evaluate the statements below:
• All enzymes are proteins
• All proteins are enzymes cofactor
CHOICES:
A. 1st statement is correct C. Both statements are correct
B. 2nd statement is correct D. Neither of the statements are correct
prosthetic group
why?______________________________________________________________________________________________
BIOCHEMICAL IMPOTRTANCE of Enzymes holoenzyme
Biological catalyst
- They increase the rate of chemical reactions taking place within living cells without changing themselves. Coenzyme or
- As catalyst, enzymes are not consumed during the reaction but merely help the reaction occur more rapidly. cosubstrate
Specificity
- A given enzyme is very selective activator
- Both in the substances with which it interacts and in the reaction that it catalyzes
Substrate (S)
Regulate metabolism
- play key role in the degradation and synthesis of nutrients: ex. digestion
- presence and maintenance of a complete and balanced set of enzymes is essential for the breakdown of nutrients to supply
Product (P)
energy or to harness energy to power cell motility and activity
Synthesis of biomolecules metal-activated enzymes
- the assembly of those building blocks into proteins, DNA, membranes, cells, and tissues
metalloenzymes.
Enzyme and substrate interaction
ENZYME
PROSTHETIC GROUP
CONJUGATED ENZYME SIMPLE ENZYME
HOLOENZYME COFACTOR APOENZYME
ACTIVATOR COENZYME
 _________________ – is the nonprotein part of
the conjugated enzyme. It is generally either a small
organic molecule or an inorganic ion (usually a metal ion)
 _______________ are organic non-protein METAL ION
compound that binds with an enzyme to catalyze a
reaction. Just like enzymes can be reused and recycled
without changing reaction rate or effectiveness. METAL-ACTIVATED ENZYME
 ________________ are distinguished by their
tight, stable incorporation into a protein’s structure by
covalent or noncovalent forces
METALLOENZYME

COENZYMES NOMENCLATURE and CLASSIFICATION OF ENZYME
Vitamins Coenzyme Group transferred A. Based upon the substance they act upon (substrate)
 the suffix “ase” is added to the name of the substrate Except for:
Vit. B1 aldehydes 1. amylase acts on __________ Pepsin – in gastric juice (stomach)
Thiamin 2. maltase acts on ___________ Trypsin – in pancreatic juice (small intestine)
3. cellulase act on ____________ Ptyalin – in saliva
Vit. B2 flavin mononucleotide (FMN) 4. lipase acts on _______ Rennin – the milk curding enzyme
Riboflavin flavin adenine dinucleotide (FAD)
B. Based upon the reaction enhanced
Vit. B3 nicotinamide adenine dinucleotide (NAD1)  the suffix “ase” is added to the type of chemical reaction activated
Nicotinic acid nicotinamide adenine dinucleotide phosphate (NADP1) 1. Oxidase – __________________
2. decarboxylase - __________________
Vit. B5 acyl groups 3. transaminase - __________________
Pantothenic acid 4. hydrolase - __________________
except: urease – hydrolysis of urea
Vit. B6 pyridoxal-5-phosphate (PLP)
lactase – __________________
Pyridoxine pyridoxine-5’-phophate (PNP)
sucrase – __________________
pyridoxamine-5’-phosphate (PMP)
cellulase – __________________
Vit. B7 carbon dioxide (carboxyl group) 5. hydrase or dehydrase – reversible addition or removal of water
Biotin
C. Based upon the reaction they catalyze
Vit. B9 tetrahydrofolate (THF) 1. ___________________________________
Folic acid • Oxidation-Reduction reaction
Example: Lactate dehydrogenase
Vit. B12 Methylcobalamin (Cobalt as the prosthetic group metal ion) Phosphate dehydrogenase
Cyanocobalamin
METALLOENZYME
Metal ion Enzyme Function
Cu2+, Zn2+ Superoxide dismutase

“browning reaction” caused by phenolase (or polyphenoloxidase), a conjugated enzyme in which copper is present “
Zn2+ They oxidize a range of aliphatic and aromatic alcohols to their corresponding aldehydes and
ketones using NAD+ as a coenzyme. 2. _____________________________
 is an enzyme that catalyzes the transfer of a functional group other than hydrogen (ex. methyl, acyl, amino or
DNA polymerase phosphate groups) from one molecule to another.
Carboxypeptidase A is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C- Examples: transaminases and kinases
terminal) end of a protein or peptide
Mn2+ Pyruvate carboxylase
Arginase
Fe Hemoglobins
carry electrons between two segments of the electron-transport chain.

Cytochrome P450 enzymes play a role in the synthesis of many molecules including steroid
hormones, certain fats (cholesterol and other fatty acids), and acids used to digest fats (bile
acids). Additional cytochrome P450 enzymes metabolize external substances, such as
medications that are ingested, and internal substances, such as toxins that are formed within
cells.
Cu2+ hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains

3. _________________________ Main Classes and Subclasses of Enzymes
 an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the
bond to break
 Hydrolysis reactions are central to the process of digestion. Main Class Selected subclasses Type of Reaction Catalyzed
Examples:
 Carbohydrases - breaking of glycosidic bonds in oligo- and polysaccharides OXIDOREDUCTASES oxidases oxidation of a substrate
 Proteases- breaking of peptide linkages in proteins reductases reduction of a substrate
 lipases - breaking of ester linkages in triacylglycerols dehydrogenases introduction of double bond (oxidation) by formal removal of two H atoms
from substrate, the H being accepted by a coenzyme
TRANSFERASES Transaminases transfer of an amino group between substrates

Kinases transfer of a phosphate group between substrates
HYDROLASES Lipases hydrolysis of ester linkages in lipids

Proteases hydrolysis of amide linkages in proteins
Nucleases hydrolysis of sugar–phosphate ester bonds in nucleic acids
Carbohydrases hydrolysis of glycosidic bonds in carbohydrates
phosphatases hydrolysis of phosphate–ester bonds
LYASES dehydratases removal of H2O from a substrate

decarboxylases removal of CO2 from a substrate
4. ___________________________
deaminases removal of NH3 from a substrate
 is an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double hydratases addition of H2O to a substrate
bond in a manner that does not involve hydrolysis or oxidation.
Example: ISOMERASES Racemases conversion of D isomer to L isomer,or vice versa
 Dehydratase effects the removal Mutases transfer of a functional group from one position to another in the same
of the components of water from molecule
a double bond
 Hydratase effects the addition of LIGASES Synthetases formation of new bond between two substrates, with participation of ATP
the components of water to a Carboxylases formation of new bond between a substrate and CO2, with participation of
double bond ATP
5. ________________________
 an enzyme that catalyzes the
OVERVIEW: MECHANISM OF ENZYME ACTION
isomerization (rearrangement of atoms or
interconversion of optical, geometric, or
positional isomers) of a substrate in a reaction,
converting it into a molecule isomeric with
itself. There is only one reactant and one
product in reactions where isomerases are
operative.
6. ___________________________
• an enzyme that catalyzes the
bonding together of two Enzyme Active Site
molecules into one with the - the relatively small part of an enzyme’s structure that is
participation of ATP. involved in catalysis. Usually a “crevicelike” location the
• ATP involvement is required enzyme.
because such reactions are
generally energetically
unfavorable and they require the Enzyme-Substrate Complex
simultaneous input of energy - the intermediate reaction species that is formed when the
obtained by a hydrolysis reaction substrate bind to the active site of an enzyme.
in which ATP is converted to ADP

Models of enzyme action Extremophile
 is a microorganism that thrives in extreme environments, environments in which humans and most other forms
1. Lock-and-Key Model (Emil Fischer) of life could not survive.
 only a substrate whose shape and chemical nature are  _____________- optimal growth at pH levels of 3.0 or below
complementary to those of the active site can interact  _____________- optimal growth at pH levels of 9.0 or above
with the enzyme.  _____________- a salinity that exceeds 0.2 M NaCl needed for growth
 ___________________- a temperature between 80°C and 122°C needed to thrive
 _____________- a temperature of 15°C or lower needed for growth
 _____________- a high hydrostatic pressure needed for growth
EXTREMOZYME
2. Induced-Fit Model (Daniel F. Koshland)  is a microbial enzyme active at conditions that would inactivate human enzymes as well as enzymes present in
 is a result of the enzyme’s flexibility other types of higher organisms.
 the enzyme active site, although not exactly  cellulases, amylases, xylanases, proteases, pectinases, keratinases, lipases, esterases, catalases, peroxidases and
complementary in shape to that of the substrate, is flexible enough that it phytases
can adapt to the shape of the substrate.  USE:
detergent formulations
the petroleum industry during oil well drilling operations
Enzyme specificity Extremophile: H. pylori and Stomach Ulcers
 the extent to which an enzyme’s activity is restricted to a specific substrate, a specific group of substrates, a • Helicobacter pylori, commonly called H. pylori, is a bacterium that
specific type of chemical bond, or a specific type of chemical reaction can function in the highly acidic environment of the stomach
 Absolute specificity • causes more than 90% of duodenal ulcers and up to 80% of gastric
• enzyme will ___________________________________. ulcers.
• Ex. Catalase catalyzes the conversion of hydrogen peroxide (H2O2) to O2 and H2O. Hydrogen peroxide is • TREATMENT: acid-suppression or acid-neutralization medications
the only substrate it will accept PLUS
 Group specificity antibiotics(tetracycline, amoxicillin,metronidazole,clarithromycin,
• the enzyme will act only on molecules that have a ______________________, such as hydroxyl, amino, or and levofloxacin).
phosphate groups. • Transmission: fecal–oral or oral–oral routes.
• Examples:
• __________________- it cleaves amino acids, one at a time, from the carboxyl end of a peptide
chain.
• ______________- acts on ester bonds
• ______________-acts on peptide bonds
• ______________- acts on glycosidic bonds.
 Linkage specificity
• the enzyme will act on a particular type of ____________________, irrespective of the rest of the molecular
structure. This is the most general of the common specificities.
• Ex. Phosphatases hydrolyze phosphate-ester bonds in all types of phosphate esters a molecule closely resembling the a molecule that binds to a site on an a molecule that forms a covalent
 Stereochemical specificity substrate. Binds to the active site enzyme that is not the active site. The bond to a part of the active site,
• some enzymes are specific to only _________ isomer even if the compound is one type of molecule: and temporarily prevents normal substrate still occupies the active permanently preventing substrate
substrates form occupying it, thus site but the enzyme cannot catalyze the
• Ex. glucose oxidase catalyzes the oxidation of β-D-glucose but not α-D-glucose, and arginase catalyzes the
hydrolysis of L-arginine but not D-arginine. Maltase catalyzes the hydrolysis of α- but not β –glycosides. blocking the reaction. reaction due to the presence of the from occupying .
FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY
inhibitor .

Allosteric Enzymes Creatine kinase
- Greek allo, means “_______,” and stereos, means “____________.”  is an enzyme that is found primarily in _____________________ and in smaller fractions in the brain
- is an enzyme with two or more protein chains (quaternary TYPES OF CK
structure) and two kinds of binding sites (substrate and regulator)  muscle (CK-MM)
 brain (CK-BB)
Regulators- ______________________________________________  cardiac tissue (CK-MB) - important marker in the diagnosis of acute myocardial infarction (AMI)
_________________________________________________________
TROPONIN
Positive regulator _________________________________________  Description
________________________________________________________ • Troponin I and T are sensitive markers of cardiac injury.
• Troponin I is found solely in the ___________________, and
Negative regulator a noncompetitive inhibitor; decreases enzyme • Troponin T is found in both _______________________________________.
activity; changes to the active site are such that substrate is less  Clinical Significance
readily accepted. • Troponin levels begin to rise within 4 hours of onset of chest pain. Levels should be drawn on admission
and within 8 to 12 hours thereafter. Patients with elevated troponin levels are considered at high risk for a
significant cardiac event.
• Approximately 30% of patients with no elevation in CK-MB may demonstrate elevated troponin and thus be
diagnosed with a non-Q-wave myocardial infarction.
REASON FOR REGULATION: Waste of energy GASTROINTESTINAL TESTS
 A cell that continually produces large amounts of an enzyme for which substrate concentration is always very Alanine Aminotransferase/ serum glutamic pyruvic transaminase (SGPT).
low  liver tissue. It is also located in myocardial, muscle, and renal tissue
 A product of an enzyme-catalyzed reaction that is present in plentiful (more than needed) amounts.  considered a specific marker for liver disease
WAYS OF REGULATION Aspartate Aminotransferase/ serum glutamic oxaloacetic transaminase (SGOT)
(1) feedback control associated with allosteric enzymes  found in the liver. It is also present in the heart, kidney, pancreas, lungs, and skeletal muscle
(2) production of enzymes in an inactive form: proteolytic enzymes and zymogens  For diagnosis of liver disease
(3) covalent modification g-Glutamyl Transpeptidase
 an enzyme found in the liver, kidney, and pancreas. GGT levels are useful in the diagnosis and monitoring of
Feedback Control associated with Allosteric enzyme alcoholic liver disease
a process in which activation or inhibition of the first reaction in a reaction sequence is controlled by a product of the  Increased GGT may be seen in alcoholic liver disease, metastatic liver disease, obstructive jaundice,
reaction sequence cholelithiasis, and pancreatitis
Lactate Dehydrogenase
 enzyme involved in the interconversion of lactate and pyruvate.
 is found in many tissues, including heart, brain, liver, skeletal muscle, kidneys, lungs, and RBCs.
 LDH4 and LDH5 are present in liver tissue, and elevations may be seen in liver disease such as hepatitis and
cirrhosis.
 LDH1 and LDH2 may be useful in the diagnosis of myocardial infarction
proteolytic enzyme Lipase
 an enzyme that  enzyme that aids in the digestion of fat. It is primarily secreted by the pancreas.
________________________________________________________________________________.  useful in the diagnosis of pancreatitis and is considered a more specific marker for pancreatitis than amylase
zymogen or proenzyme Amylase
 is the _____________________ of a proteolytic enzyme.  enzyme that aids in digestion by breaking down complex carbohydrates into simple sugars.
EXAMPLES:  The majority of amylase is produced in the pancreas and salivary glands, and lesser amounts are secreted by the
 Pepsinogen ------- pepsin fallopian tubes, lungs, thyroid, and tonsils
 Tyrpsinogen -------trypsin  Serum amylase levels are most often used in the diagnosis of acute pancreatitis
 Chymotrypsinogen ------- chymotrypsin
 Angiotensinogen ------- angiotensin
BIOCHEMICAL IMPOTRTANCE: Enzymes

Important tool in diagnostic procedures (involving enzyme assay)
 assist to know damaged tissues
 assist the extent of tissue damage
 helps to monitor the course of the disease
 used as a therapeutic means of diagnosing a vast array of diseases

SERUM ENZYME MAJOR DIAGNOSTIC USE
Amylase Liver and pancreatic disease CONDITION ISOENZYME PATTERN
Myocardial infarction Moderate elevation of LDH1, slight elevation of LDH2

Acid phosphate Prostate cancer
Acute hepatitis Large elevation of LDH5, Moderate elevation of LDH4
Muscular dystrophy Elevation of LDH1-3

Alkaline phosphatase Liver and bone disease
Megaloblastic anemia Large elevation of LDH1
Creatine phosphokinase Myocardial infarction and muscle disorders Sickle cell anemia Moderate elevation of LDH1 and LDH2
Arthritis with joint infections Elevation of LDH5

Lactate dehydrogenase Myocardial infarction, leukemia, anemia
Renin Hypertension
Glutamic oxaloacetic transaminase Myocardial infarction

(SGOT)
Glutamic pyruvic transaminase Infectious hepatitis

(SGPT)
Trypsin Acute pancreatitis
Ceruplasmin Wilson’s disease

PROTEINS Nonpolar amino
Polar neutral Polar basic Polar acidic
acid
 Greek: Proteios means “__________________________________” • is an amino acid • is an amino acid • is an amino acid • is an amino acid
 are naturally occurring, unbranched polymer in which the monomer units are amino acids that contains: that contains: that contains: that contains :
 Are large biomolecules, or macromolecules, consisting of one or more long chain of amino • ____________, • ____________, • ____________, • ____________,
acid residues. _____________, _____________, _____________, _____________,
and a _________ and a _________ and a _________ and a _________
 Structural: Is a peptide in which at least 40 amino acid residues are present ______________ ______________ ______________ ______________
EXAMPLES: • G,A,V,L,I,P,F,M,W • S,C,N,T,Q,Y • H,K,R • D,E
 hormones acting as __________________;
 enzymes ______________________;
 cell receptors acting as ‘_________________’; Non-polar amino acid
 antibodies _________________foreign invaders;
 membrane channels allowing specific molecules to ________ or __________ a cell;
Proteins make up the muscles for moving; let you grow hair, ligaments and fingernails; and let you see (the
lens of your eye is pure crystalized protein).
AMINO ACIDS: Glycine Alanine Valine Leucine Isoleucine

BUILDING BLOCK OF PROTEINS
_________________________- is an amino acid in which

the amino group and the carboxyl group are attached to the - 
carbon atom.
Proline Phenylalanine Methionine Tryptophan
Except: Proline
NAMING AMINO ACIDS

AMINO HYDROPHOBIC SIDE CHAIN
ACIDS FUNCTIONAL GROUP
(9)
G H group
A Aliphatic R group (methyl)
V Aliphatic R group (isopropyl)
L Aliphatic R group (additional methylene group)
I Aliphatic R group (isobutyl group)
P Aliphatic R group (propyl)
F Aromatic Ring (Phenyl group/ alanine w/ phenyl substituent on the  -

carbon)
M Sulfur group (thioether)
W Aromatic Ring (indole ring -5 membered nitrogen ring fused w/ benzene ring)
CLASSIFICATION OF AMINO ACIDS

Polar Neutral Amino acids
Ketogenic
- L,K
serine cysteine Threonine Both Keto and Gluco

- Y, F, I, A,G,C,S,TW
Glucogenic
- V, P, M, N, Q, E, D, H, R
Asparagine Glutamine Tyrosine

Uses, Functions and Deficiency of Amino acids
Pola Basic Amino acids
AMINO USES/ FUNCTIONS DEFICIENCY
ACIDS
Trp  Necessary for the synthesis of neurotransmitter serotonin (5- Pellagra,

hydroxytryptamine). A natural relaxant, helps alleviate insomnia by
inducing normal sleep; reduces anxiety and depression.
 Can be metabolized to niacin if needed
 Used to synthesized melatonin (5-methoxy-N-acetyltryptamine)
Tyr  Precursor of dopamine, norepinephrine, epinephrine Hypothyroidism

Histidine Lysine Arginine
 Promotes healthy thyroid functioning
Polar Acidic Amino acids Val, Ile,  enhance energy, increase endurance, and aid in muscle tissue recovery MSUD (maple syrup
Leu and repair. urine disease)
 lowers elevated blood sugar levels and increases growth hormone
production.
Lys  precursor for L-carathine which is essential for healthy nervous system Retarded growth
function.
 for adequate absorption of calcium and bone development in children
Met  Is antioxidant. It helps in breakdown of fats and aids in reducing Liver

Aspartic acid Glutamic acid muscle degeneration. Helps lower cholesterol levels by increasing the Deterioration
liver's production of lecithin; reduces liver fat and protects the kidneys.
 principle supplier of sulfur, which inactivates free radicals. Is a natural
ESSENTIAL AMINO ACIDS NON-ESSENTIAL AMINO ACIDS chelating agent for heavy metals and helps detoxify the body of these
metals.
 Adequate methionine prevents disorders of the hair, skin and nails;
is a standard amino acid needed
for protein synthesis that must Synthesized by the body AMINO USES/ FUNCTIONS DEFICIENCY
be obtained from dietary C,A,N,D,E,Y,S, Q,G,P, ACIDS
sources because the human
body cannot synthesize it in Phe  Beneficial for healthy nervous system. It may be useful against
adequate amounts from other depression and suppressing appetite.
substances.  Used to produce dopamine and norepinephrine, chemicals that
R*,H,M,I,L,K,W,T,F,V

promote alertness, elevate mood, decrease pain, aid in memory and 3-methylhistidine Muscle proteins
learning, and reduce hunger and appetite. _________________ - found in the cell walls of
 D-phenylalanine - natural form. May improve rigidity, walking ε-N- Muscle proteins many bacteria
disabilities, speech difficulties and depression associated with trimethyllysine _______________- found in earthworms
Parkinson’s disease. _______- one of the neurotransmitters in the brain
 L-phenylalanine can be converted into L-tyrosine, which is in turn Thyroxine Thyroid gland _________- a constituent of the vitamin
converted into L-DOPA. L-DOPA is a precursor for dopamine, pantothenic acid
norepinephrine (noradrenalin), and epinephrine (adrenaline)
 DL-phenylalanine They are derived from the common amino acids and are produced by modification of the parent amino acid after the
protein is synthesized by the organism in a process called posttranslational modification. Hydroxyproline and
Ala  Removes toxic substances released from breakdown of muscle protein during intensive exercise
hydroxylysine differ from the parent amino acids in that they have hydroxyl groups on their side chains; they are found
only in a few connective-tissue proteins, such as collagen. Thyroxine differs from tyrosine in that it has an extra iodine-
containing aromatic group on the side chain; it is produced only in the thyroid gland, formed by posttranslational
Cys  antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants
modification of tyrosine residues in the protein thyroglobulin. Thyroxine is then released as a hormone by proteolysis of
such as vitamin E and selenium.
thyroglobulin.
Gln  Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules. Acid-base properties
Zwitterion = means double ion Is a molecule that has
a positive charge on one atom and a negative
Gly  Component of skin and is beneficial for wound healing. It acts as neurotransmitter charge on another atom but which has no net
charge.
Basic solution - NH3+ of the zwitterion loses a
proton and negatively charged species is formed.
His  Important for the synthesis of red and white blood cells.
Acidic solution - the zwitterion accepts a proton (H+)
 It is a precursor for histamine which is good for sexual arousal. Improve blood flow. to form a positively charged ion.
ISOELECTRIC POINT= the pH at which an amino acid
exists primarily in its zwitterion form. At the isoelectric point,
Thr It helps promote equilibrium in the central nervous system—aids in balancing state of emotion. almost all amino acid molecules in a solution (more than 99%) are
present in their zwitterion form.
Asp  Enhances stamina, aids in removal of toxins and ammonia from the body, and beneficial in the
synthesis of proteins involved in the immune system.
Pro  plays role in intracellular signaling.
Arg  plays role in blood vessel relaxation, stimulating and maintaining erection in men, production of
ejaculate, and removal of excess ammonia from the body.
Guidelines for amino acid form as function of solution pH follows:

 Low pH:
Uncommon amino acids derived from Posttranslational Modification o All acid groups are ___________ (-COOH).
o All amino groups are __________ (NH3 +)
AMINO ACIDS Source  High pH:
o All acid groups are _______________ (COO-).
4-hydroxyproline Collagen and gelatin o All amino groups are _____________ (-NH2).
 Neutral pH:
5-hydroxylysine Collagen and gelatin o All acid groups are _____________ (COO-).
o All amino groups are _____________(NH3+).
ε-N-methyllysine Muscle proteins

PROTEIN RELATED DISORDERS: Please research on the following disease
1. Kwashorkor and marasmus Neurotransmitters:
2. Amyloid disease relation to Alzheirmer’s disease  Enkephalins – pain killers (pentapeptide):
3. Prion disease: neurotransmitters or neuromodulators at many locations in the brain and spinal cord and are involved
-Creutzfeldt-Jakob disease and kuru disease with pain perception, movement,
-Scrapie mood, behavior, and neuroendocrine regulation; they are also found in nerve plexuses and exocrine glands
-Bovine spongiform encephalopathy of the gastrointestinal tract.
4. Hemoglobinopathies Antioxidants:
- Sickle cell anemia  Glutathione
- Hemoglobin C disease - regulator of oxidation-reduction reaction
- Hemoglobin SC disease - antioxidant, protecting cellular contents from oxidizing agents such as peroxides and superoxides (highly
- Thalasemmia reactive forms of oxygen often generated within the cell in response to bacterial invasion) with unusual
5. Collagenopathies features.
- Osteogenesis imperfecta I Glutathione - (Glu – Cys - Gly) (tripeptide)
- Osteogenesis imperfecta II Unusual features. The amino acid Glu, an acidic amino acid, is bonded to Cys, through the side-chain carboxyl group rather
than through its a- carbon carboxyl group.
6. Alpha-1 antitrypsin deficiency
PEPTIDE FORMATION BONDING IN PROTEINS
1. ________________ – the strongest bond
N – terminal end (left) 2. _______________ - is a covalent bond between two sulfur.
C – terminal end (right) Results from the oxidation of the –SH (sulfhydryl) groups of
Backbone (peptide bond & a-carbon –CH group) two cysteine molecules to form “cystine”
R- substituent 3. ________________ - result from the attraction of
electronegative atoms in the protein molecule. Weaker than
Peptide bond the peptide and disulfide bonds.
 a covalent bond (amide bond) between the carboxyl group of one amino acid and the amino group of another H-bond: can occur between amino acids with polar R groups.
amino acid. functional groups:
 Peptide – is an unbranched chain of amino acids, each joined to the next by a peptide bond. -OH; -NH2; -COOH; -CONH2
TYPES OF PEPTIDE: 4. ____________ or salt bridges - formed between groups which
 dipeptide – a compound containing two amino acids. are positively and negatively charge.
 Tripeptide – three amino acids joined together in a chain. - always involve the interaction between an acidic side chain
 Oligopeptide – refer to peptides with 10 to 20 amino acid residues. (R group) and a basic side chain (R group).
 Polypeptide – long unbranched chain of amino acids, each joined to the next by a peptide bond. 5. _______________ - formed by amino acids like leucine, valine,
Peptide Nomenclature phenylalanine, tryptophan, and proline which adhere each
IUPAC Rule: other forming a “micelle” and which do not mix well with water
1. The C-terminal amino acid residue keeps its full amino acid name. - result when two nonpolar side chains are close to each other.
2. All of the other amino acid residues have names that end in –yl. The –yl suffix replaces the –ine or ic acid ending
of the amino acid name, except for tryptophan (tryptophyl), cysteine (cysteinyl), glutamine (glutaminyl), and
asparagine (asparaginyl).
CLASSIFICATION OF PROTEINS
3. The amino acid naming sequence begins at the N-terminal amino acid residue. I.Based on the number of peptide chain
1. monomeric protein
V – F – C- Valylphenylalanylcysteine - is a protein in which only one peptide chain is present.
Cys- Ala-Gly-Val- Cysteinylalanylglycylvaline Example: myoglobin
2. multimeric protein
Biochemically important small peptides - is a protein in which more than one peptide chain is present.
- The peptide chains present in multimeric proteins are called protein subunits.
Hormones both produced by the pituitary gland:
1. Oxytocin Example: insulin
▹ regulates uterine contraction and lactation, plays II.Based on chemical composition
a role in stimulating the flow of milk in a nursing 1. Simple protein is a protein in which only amino acid residues are present.
mother. A. Albumins
2.Vasopressin (ADH) Examples:
▹ regulates the excretion of water by the kidneys; a. Serum albumin (blood)
▹ Enhances reabsorption of free water b. Lactalbumin (milk)
▹ plays a role in the control of blood pressure by regulating contraction of smooth muscle c. Ovalbumin (eggwhite)

Properties:
 Soluble in water and dilute neutral salt solution 2. Conjugated protein is a protein that has one or more non-amino acid entities present in its structure in addition
 Coagulated by heat and precipitated by full saturation with (NH4)2SO4 but not w/ NaCl to one or more peptide chains.
except with the presence of acid. • prosthetic group is a non-amino acid group present in a conjugated protein. These non-amino acid
B. Globulins components, which may be organic or inorganic.
Examples:
a. Ovoglobulin (eggwhite)
b. Edestin (hempseed)
c. Legumin (peas)
d. Myosinogen (muscles)
e. Serum globulin (blood)
Properties:
 Soluble in neutral dilute salt solutions but not in water. (Neutral salts refers refer to salts of
strong acids and bases as NaCl, MgSO4 and (NH4)2SO4.)
 Coagulated by heat and can be precipitated from their solutions by half saturation with
(NH4)2SO4 and complete saturation with NaCl.
C. Glutelins
Examples:
a. Glutenin (wheat)
b. Oryzenin (rice) A. Nucleoprotein
Properties: Examples:
 Soluble in dilute acids and alkalies but insoluble in neutral solvents. a. Ribosomes (site for protein synthesis in cells)
D. Prolamines b. Viruses (self-replicating, infectious complex)
Examples: c. Chromatin
a. Gliadin (wheat) d. Products from glandular tissues
b. Zein (corn) e. Germ of grains
c. Hordein (barley) Properties:
 Prosthetic group: Nucleic acids
Properties:  Combination of histones and protamins with nucleic acids
 Insoluble in ordinary solvent (water, dilute salt solutions, dilute acid and alkalies) but soluble in  Soluble in dilute solutions of NaCl
70% alcohol at about neutral point.  Precipitated by acidification
 Not coagulable by heat. B. Glycoproteins (more proteins less carbohydrates)
Examples:
E. Histones a. Mucin aka mucoproteins – more carbs less proteins (saliva, mucous secretion of the nose)
Examples: b. Tendomucoid (tendons)
a. Globin (hemoglobin) c. Osseomucoid (bones)
b. Thymus histones d. gamma globulin (antibody)
c. Scobrone of Mackerel e. Interferon (antiviral protection)
Properties: f. Simple proteins like globulins and albumins
 Soluble in water, dilute acids and alkalies but not in ammonia. Properties:
 Not readily coagulated by heat  Prosthetic group: carbohydrates
 Strongly basic and occur in the tissues in the form of salt combinations with acid substances like the heme  Use: Utilize for lubricating purposes in view of their slimy nature
of the hemoglobin  Use: Help in protecting the membranes of the GIT against digestion since they are not digested
F. Protamines by the enzymes of GIT.
Examples: Salmin (salmon sperm) C. Phosphoproteins
Properties: Examples:
 Contain smaller number of amino acids a. Casein (milk)
 Soluble in water and dilute acids and alkalies b. Vitellin (egg yolk)
 Not coagulated by heat Properties: Prosthetic group: H3PO4
G. Scleroproteins (Albuminoids)
Examples: D. Chromoproteins/ Hemoproteins
a. Keratin (epidermal tissues) Examples:
b. Elastins (Ligaments) a. Hemoglobin (blood -carrier of O2 in blood )
c. Collagen (hides, bones and cartillage) b. Myoglobin (oxygen binder in muscles)
Properties: Insoluble in water and neutral solvents c. Cytochromes

d. Rhodopsin 2.2. Peptides
Properties: Prosthetic group: hematin or heme unit  Are combinations of two or more amino acids, the carboxyl group of one being united with the
E. Lipoproteins amino group of the other.
Examples:  Present properties like peptones
a. Lecithin  Ex. di, tri,tera,penta etc.
b. Cephalin
c. low-density lipoprotein (LDL) – lipid carrier III. Level of structural organization
d. high-density lipoprotein (HDL) – lipid carrier A. PRIMARY
Properties:  Sequence of amino acids in a protein – that is, the order in which the amino acids are connected to each
 Prosthetic group: Lipids/ fatty substance other
 Occurrence: Blood serum, brain tissues, cell nuclei, egg yolk and milk  Also involves the order of attachment of the amino acids to each other through covalent peptide bonds.
D. Metalloproteins  These bonds are formed between the carboxyl group of one amino acid with the amino group of another.
Examples:  “peptide bond planarity” is the zigzag arrangement
a. iron–ferritin (storage complex for iron)  MYOGLOBIN: The primary structure of human myoglobin. This diagram gives only the sequence of the
b. zinc–alcohol dehydrogenase (enzyme in alcohol oxidation) amino acids present and conveys no information about the actual three dimensional shape of the protein.
Properties: Prosthetic group: metal ion B. SECONDARY
3. Derived proteins. These include substances formed from simple conjugated proteins.  Core of many proteins is the  sheet
A. Primary Protein derivatives – proteins which have undergone slight intramolecular rearrangement  Form rigid structures with the H-bond
through the hydrolytic action of certain physical and chemical agents.  Can be of 2 types
- synonymous w/ denatured proteins a. Anti-parallel – run in an opposite direction of its neighbor
1. Proteans b. Parallel – run in the same direction with longer looping sections between them
Examples: C. TERTIARY
 Myosan from myosin  The overall three-dimensional shape of a protein that results from the interactions between amino
 Edestan from edestin acids side chains (R groups) that are widely separated from each other within a peptide chain.
Properties: Are insoluble substances resulting from the preliminary  Four types of stabilizing interactions contribute to the tertiary structure of a protein:
actions of water, dilute acids or enzymes covalent disulfide bonds
2. Metaproteins electrostatic attractions (salt bridges)
Examples: Hydrogen bonds
a. Acid metaproteins (acid albuminate) hydrophobic attractions
b. Alkali metaproteins (alkali albuminate) D. QUATERNARY
Properties  Is the organization among the various peptide chains in a multimeric protein.
 Are product of further hydrolysis  The three-dimensional shape of a protein consisting of two or more independent peptide chains,
 Soluble in weak acids and alkalies neutral salt solution which results from noncovalent interactions between R groups
 Insoluble in neutral salt solutions  For example, the human hemoglobin molecule is a tetramer made up of two alpha and two beta
3. Coagulated proteins polypeptide chains.
Examples: Cooked egg albumin and Cooked meat  This is also when the protein associates with non-proteic groups. For example, carbohydrates can be
Properties : Insoluble products resulting from either the action of heat, alcohol, ultraviolet added to form a glycoprotein.
rays or even simple mechanical shaking  Bonds:
B. Secondary Protein derivatives  Electrostatic
 Product of more extensive hydrolysis  H-bond
 Mixtures of fragments of original proteins varying in composition and size  Hydrophobic
 Exhibit certain common properties such as solubility in water and non-coagulability by heat.
1. Primary proteoses
Properties
 Soluble in water, precipitated by conc.HNO3 and by half saturation with (NH4)2SO4 or ZnSO4.
 Not coagulated by heat
2. Secondary proteoses
Properties
 Precipitated only by complete saturation with (NH4)2SO4 but nit with picric acid and HNO3 .
2.1. Peptones
Properties
 Soluble in water
 Not coagulated by heat
 Not precipitated by saturation with (NH4)2SO4 but by certain alkaloidal reagents, such
as,phosphotingstic and tannic acids.

IV. GROSS STRUCTURE
1. Fibrous 3. MEMBRANEOUS
 Protein whose molecules have an  is a protein that is found associated with a membrane system of a cell.
Fibrous Occurrence and Functions  Soluble in aqueous media
elongated shape with one dimension much
Proteins  Have been crystallized and have definite molecular weights
longer than the others.
(insoluble)  Can be denatured
 Properties:
 Tend to have simple, regular and
Keratins found in wool, feathers,

linear structures.
Largely insoluble in ordinary aqueous
hooves, silk, and BASED ON FUNCTIONS
fingernails • CATALYTIC: Proteins with the role of biochemical catalyst are called enzymes.
media
Enzymes participate in almost all of the metabolic reactions that occur in cells.
 Molecular weights are high Collagens found in tendons, bone, The chemistry of human genetics, is very dependent on the presence of
 Functions is for structural and support and other connective enzymes.
tissue
2. GLOBULAR
• DEFENSE: also called immunoglobulins or antibodies w/c are central functioning of the
 Protein whose molecules have peptide Elastins found in blood vessels body’s immune system
chains that are folded into spherical or and ligaments They bind to foreign substances, such as bacteria and viruses, to help combat
globular shapes.
invasion of the body by foreign particles.
 The folding in such that most of amino Myosins found in muscle tissue
acids with hydrophobic side chains
Fibrin found in blood clots • TRANSPORT: - proteins bind to particular small biomolecules and transport them to other
(nonpolar R groups) are in the interior of
locations in the body and then release the small molecules as needed at the
the molecules and most of the hydrophilic
destination location.
side chains (polar) are on the outside of the molecule.
Examples:
 Properties:
hemoglobin - carries oxygen from the lungs to other organs and tissues.
 Soluble in aqeous media
Transferrin - which carries iron from the liver to the bone marrow.
 Have been crystallized and have definite molecular weights
High- and low-density lipoproteins - are carriers of cholesterol in the bloodstream
 Can be denatured
• MESSENGER: transmit signals to coordinate biochemical processes between different
Globular Proteins (soluble) Occurrence and Functions cells, tissues, and organs
insulin
Insulin glucagon
Human growth hormone
Myoglobin
• CONTRACTILE: are necessary for all forms of movement
Hemoglobin Actin and myosin
Sperm can “swim” because of long flagella made up of contractile proteins.
Transferrin
• STRUCTURAL: confer stiffness and rigidity to otherwise fluid-like biochemical systems
Immuno globulins
Collagen - component of cartilage,
Keratin - gives mechanical strength as well as protective covering to hair,
fingernails, feathers, hooves, and some animal shells.
Characteristics FIBROUS GLOBULAR
• STORAGE: These proteins bind (and store) small molecules for future use
Water-solubility During degradation of hemoglobin the iron atoms present are released and
become part of ferritin, an iron-storage protein, which saves the iron for use in
Secondary structure
the biosynthesis of new hemoglobin molecules.
Function generally have structural functions that provide involved in metabolic Myoglobin - an oxygen-storage protein present in muscle; the oxygen so stored
support chemistry, performing functions such as is a reserve oxygen source for working muscle.
and external protection, catalysis, transport, and regulation.
• REGULATORY: often found “embedded” in the exterior surface of cell membranes.
Kind of proteins Act as sites at which messenger molecules, including messenger proteins such
as insulin, can bind and thereby initiate the effect that the messenger “carries.”
Presence in human body
Are often the molecules that bind to enzymes (catalytic proteins), thereby
Mass composition turning them “on” and “off” and thus controlling enzymatic action.

• TRANSMEMBRANE: help control the movement of small molecules and ions
through the cell membrane
• NUTRIENT: These proteins are particularly important in the early stages of life, from
embryo to infant.
Casein - milk
Ovalbumin - found in egg white (>50% present)
• BUFFER: These proteins are part of the system by which the acid-base balance within body
fluids is maintained
Hemoglobin has a buffering role in addition to being an oxygen carrier.
Transmembrane proteins regulate the movement of ions in and out of cells, ensuring that ion
concentrations are those needed for correct acidity/alkalinity.
• FLUID BALANCE: These proteins help maintain fluid balance between blood and
surrounding tissue
Albumin and globulin
 Found in the capillary beds of the circulatory system. When increased blood pressure generated
by a pumping heart forces water and nutrients out of the capillaries, these proteins remain
behind (since they are too big to cross cellular membranes). As their concentration increases
(due to less fluid being present), osmotic pressure “forces” draw water back into the capillaries,
which is necessary for fluid balance to be maintained.

LIPIDS BASED ON FUNCTIONS
1. Energy-storage lipids
CLASSIFICATION OF LIPIDS
a. Triacylglycerols
 an organic compound found in living organisms that is insoluble (or only sparingly soluble) in water
i. Fats
but soluble in nonpolar organic solvents.
ii. Oils
 are a heterogeneous group of compounds, including fats, oils, steroids, waxes, and related
2. Membrane lipids
compounds,
a. Phospholipids
 which are related more by their physical than by their chemical properties.
i. Glycerophospholipids
 Common property of being
1. Lecithins
(1) relatively insoluble in water
2. Cephalins
(2)soluble in nonpolar or organic solvents ii. Sphingophospholipids
1. Sphingomyelins
GENERAL FUNCTIONS OF LIPIDS b. sphingoglycolipids
i. They are efficient energy sources. i. Cerebrosides
Body lipids are reservoir of potential chemical energy. Lipids can be stored in the body in ii. Gangliosides
almost unlimited amount in contrast to carbohydrates. Furthermore, lipids have a high c. Cholesterol
calorific value (calories per gram) which is twice as great as carbohydrate. Large amount 3. Emulsification lipids
of energy is stored as lipid than as carbohydrates a. Bile acids
ii. Serve as thermal insulators. i. Cholic acids
The subcutaneous lipids serve as insulating materials against atmospheric heat and cold ii. Deoxycholic acids
and protect internal organs. 4. Messenger lipids
Nonpolar lipids act as electrical insulators, allowing rapid propagation of depolarization a. steroid hormones
waves along myelinated nerves. i. Sex Hormones
iii. They are structural components of the cell membrane. 1. Estrogens
Lipids which form the major constituent of biomembranes are responsible for membrane 2. Androgens
integrity and regulation of membrane permeability. 3. Progestins
Lipids present in inner mitochondrial membrane actively participate in electron ii. Adrenocorticoids
transport chain. 1. Mineralocorticoids
Combinations of lipid and protein (lipoproteins) are important cellular constituents, 2. Glucocorticoids
occurring both in the cell membrane and in the mitochondria, and serving also as the b. Eicosanoids
means of transporting lipids in the blood. i. Prostaglandins
iv. Serve as precursors for hormones (steroid hormones). ii. Thromboxanes
Lipids serve as metabolic regulators of steroid hormones and prostaglandins. iii. Leukotrienes
v. They also dissolve the vitamins, which are fat soluble and assist their digestion. BASED UPON WHETHER OR NOT SAPONIFICATION OCCURS
They serve also as a source of fat soluble vitamins (Vitamin A, D, E and K) and essential 1. Saponifiable lipids - is a lipid that undergoes hydrolysis in basic solution to yield two or more smaller
fatty acids. (Linoleic, Linolenic and Arachidonic acid). product molecules.
vi. Polyunsaturated fatty acids help in lowering blood cholesterol. a. Triacylglycerols
vii. Squalamine, a steroid, is a potential antibiotic and antifungal agent. b. Glycerophospholipids
c. sphingophospholipids,
PHYSICAL PROPERTIES OF LIPIDS d. sphingoglycolipids
1. WATER SOLUBILITY e. waxes
Solubility decreases with increasing carbon chain length 2. Nonsaponifiable lipids - does not undergo hydrolysis in basic solution. Such lipids cannot be broken up into
2. MELTING POINT smaller component parts using hydrolysis.
Degree of unsaturation : Increase unsaturation = decrease in melting point a. Cholesterol
b. Steroid hormones
c. Bile acids
d. Eicosanoids

FATTY ACIDS: SATURATED FATTY ACIDS
 building blocks of lipids FATTY ACID FORMULA No. of C OCCURENCE
 are naturally occurring monocarboxylic acid. Acetic acid CH3COOH 2 Vinegar
CHARACTERIZATION OF FATTY ACIDS BASED ON CARBON CHAIN LENGTH Propionic acid CH3CH2COOH 3 An end product of carbohydrate fermentation by
1. long-chain fatty acids (C12 to C26) rumen Organisms
2. medium-chain fatty acids (C8 and C10) Butyric acid C3H7COOH 4 Glycerides in butter
3. short-chain fatty acids (C4 and C6) Caproic acid C5H11COOH 6 Goat and Cow butter; Coconut fat
Caprylic acid C7H15COOH 8 Goat and Cow butter; Coconut fat; Human Fat
CLASSIFICATION OF FATTY ACIDS: Capric acid C9H19COOH 10 Goat and Cow butter; Coconut fat; Fat of spice bush
I. Based on the degree of unsaturation Lauric acid C11H23COOH 12 Spermaceti, cinnamon, palm kernel oil, coconut oils,
1. Saturated fatty acid – aka BAD FAT laurels, butter
 is a fatty acid with a carbon chain in which all carbon–carbon bonds are single bonds.
Myristic acid C13H27COOH 14 Nutmeg, palm kernel, coconut oils, myrtles, butter
 Dietary effect is an increase in heart disease risk.
Palmitic acid C15H31COOH 16 Animal and vegetable fats; spermaceti; beeswax
2. Monounsaturated fatty acids – aka GOOD FAT
Stearic acid C17H35COOH 18 Animal and vegetable fats
 is a fatty acid with a carbon chain in which one carbon–carbon double bond is present.
 Dietary effect is a decrease in heart disease risk.
3. Polyunsaturated fatty acids – aka GOOD-BAD FAT UNSATURATED FATTY ACIDS
 is a fatty acid with a carbon chain in which two or more carbon–carbon double bonds are FATTY ACID No. of C & of OCCURENCE
present. double bonds
 Dietary effect is “mixed”; Monoenoic acids (one double bond)
o As GOOD FAT- decrease heart disease risk Palmitoleic 16:1Δ9 In nearly all fats
o As BAD FAT – increase cancer risk ω7
II. Based on the configuration of Double Bond Oleic acid 18:1Δ9 Animal and Vegetal fats and oil
 cis – ω9
o Naturally occurring fatty acids generally contain cis double bonds. (associated with GOOD Elaidic acid 18:1Δ9 Hydrogenated and ruminant fats.
FAT) ω9
 trans – Dienoic acids (two double bonds)
o Hydrogenation converts some cis double bonds to trans double bonds. Linoleic Acid 18:2Δ9,12 Linseed oil, Corn, peanut, cottonseed, soybean,
o Trans fatty acids have effects on blood chemistry similar to those of saturated fatty ω6 and many plant oils.
acids.(Associated with BAD FAT) Trienoic acids (three double bonds)
III. Base on Location of Double Bond (Aka ESSENTIAL FATTY ACIDS) Gamma-Linolenic acid 18:3Δ6,9,12 Linseed oil, Some plants, eg, oil of evening
 OMEGA- 3 FATTY ACIDS ω6 primrose, borage oil; minor fatty acid in animals.
o First double bond is three carbons away from the CH3 end of the carbon chain. α-Linolenic acid 18:3Δ9,12,15 Frequently found with linoleic acid but
o LINOLENIC ACID (18:3) is the primary member of this family and a precursor for EPA and ω3 particularly in linseed oil.
DHA. Tetraenoic acids (four double bonds)
o OTHER MEMBER: Arachidonic acid 20:4Δ5,8,11,14 Lipids of the liver and brain; eggyolk. Found in
 EPA and DHA – important constituents of the communication membranes of the ω6 animal fats and in peanut oil; important
brain and are necessary for normal brain development and are also active in the component of phospholipids in animals
retina of the eye. Pentaenoic acids (five double bonds)
 OMEGA-6 FATTY ACIDS Timnodonic 20:5Δ5,8,11,14,17 Important component of fish
o First double bond is six carbons away from the CH3 end of the carbon chain. oils, eg, cod liver, mackerel,
o LINOLEIC ACID (18:2) is the primary member of this family and a precursor for arachidonic menhaden, salmon oils.
acid Hexaenoic acids (six double bonds)
o OTHER MEMBER Cervonic 22:6Δ4,7,10,13,16,19 Fish oils, phospholipids in brain.
 Arachidonic acid - the major starting material for eicosanoids ω3
Unsaturated Fatty Acids and Double-Bond Position (SHORT HAND NOTATION)
 Delta designation (Δ)
 Omega designation (ω)

LIPIDS ARE CLASSIFIED AS SIMPLE OR COMPLEX 2 TYPES OF TRIACYLGLYCEROL
I. Simple lipids: Esters of fatty acids with various alcohols.  Simple Triacylglycerol
a. Fats: Esters of fatty acids with glycerol. Oils are fats in the liquid state. o Is a triester formed from the esterification of glycerol with three identical fatty acids
b. Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols. molecule.
II. Complex or compound lipids: Esters of fatty acids containing groups in addition to an alcohol and a fatty  Mixed Triacylglycerol
acid. o A triester formed from the esterification of glycerol with more than one kind of fatty acid
molecules.
a. Phospholipids: Lipids containing, in
addition to fatty acids and an alcohol, a EXAMPLES OF TRIACYLGLYCEROL
phosphoric acid residue. They frequently
have nitrogen containing bases and other FEATURE FATS OIL/ FIXED OIL
substituents. PHYSICAL STATE Solid or semisolid at Liquid at room temp
room temp
BIOCHEMISTRY Complex lipids N
SOURCE Obtained from animal sources Obtained from plants
b. Glycolipids: contain carbohydrate and nitrogenous base
PREDOMINANT Saturated compounds predominates Mono and polyunsaturated
i. Glycosphingolipids- Lipids containing a fatty acid, sphingosine, and carbohydrate.
FATTY ACIDS compounds predominates
c. Other complex lipids: Lipids such as sulfolipids and aminolipids. Lipoproteins may also be placed in this
STRUCTURE “Linearity” of fatty acids causing the “Bends” chain causing the molecule
category.
molecule to be closely packed incapable of close packing
III. Precursor and Derived lipids: Products of hydrolysis of I and II but still exhibiting the general physical
MELTING POINT Higher Lower
characteristics of lipids
a. Saturated and unsaturated fatty acids FA
b. Mono and di-glycerides FEATURE SATURATED FATS UNSATURATED FATS
c. Alcohols Type of bonds Consist of SINGLE bond Consist of at least 1 DOUBLE bond
i. Straight chain – products of hydrolysis of waxes Recommended Not more than 10% of total calories per Not more than 30% of total calories per
ii. Alcohols containing b-ionone ring – Vitamin A and some carotenols consumption day day
iii. Sterols Health Effects Excessive consumption is not good MUFAs reduces heart disease risk
d. Miscellaneous because of their association with heart PUFAs – reduce heart risk but promote
i. Aliphatic hydrocarbons diseases. risk of some types of cancer
ii. Squalene – hydrocarbons in shark liver and human Cholesterol Saturated fats increase Low Density Unsaturated fats increase High-
iii. Carotenoids Lipoproteins (LDL or bad cholesterol) & Density Lipoprotein (HDL or good
iv. Vitamins D,E,K Very Low Density Lipoproteins (VLDL's) cholesterol) and decrease Low Density
Lipoproteins (LDL or bad cholesterol).
CLASSIFICATION OF LIPIDS: based on FUNCTIONS Sources of HDL include onions and
I. ENERGY STORAGE LIPIDS Omega-3 fatty acids like flax oil, fish,
ADIPOCYTE – specialized cells that function as the storage site for Triacylglycerl (TAG). foods rich in fiber like grains.
TRIACYGLYCEROL (TAG) OR TRIACYLGLYCERIDE Commonly found in Butter, coconut oil, whole milk, Avocado, soybean oil, canola oil and
 Most abundant type of lipids present in the body and are the main storage form of fatty acids, and butter, margarine, cheese, fried foods, & olive oil, sunflower oil, fish oils
they account for greater than 90% of dietary fat intake frozen dinners walnuts, Shelf Life long lasting and do
 More efficient at storing energy than glycogen, large quantities can be packed in very small volume. not spoil quickly spoil quickly
 Lipid formed through esterification of 3 fatty acid with glycerol Melting Point High Low
 FAT – substitute term Physical state at room Solid (Trans Fats & Saturated Fats) Liquid (Monounsaturated &
temperature Polyunsaturated Fats- Omega 3's &
ESTERIFICATION REACTION: 9's)
Carboxylic acid + alcohol ------- ester + H2O Rancidity Low High
Example: Examples Hydrogenated Oils, Butter, Processed Olive Oil, linoleic acid, alpha-linolenic
Glycerol + stearic acid ----------- triacylglerol + H2O Meats acid
S

TERMINOLOGIES FOR FAT SUBSTITUTE B. SPHINGOLIPIDS (as SPHINGOGLYCOLIPIDS)
Fat free means less than 0.5g of fat per serving COMPOSITION:
Low fat means 3g or less fat per 50g serving  contains both a fatty acid and a carbohydrate component attached
Reduce fat or less fat means at least 25% less fat per serving than the regular food to a sphingosine molecule.
Calorie free means less than 0.5 kilo calories per serving Globosides
cytolipins
II. MEMBRANE LIPIDS
A. PHOSPHOLIPIDS COMPOSITION 1. Cerebrosides
 one or more fatty acids  simplest sphingoglycolipids, contain a single monosaccharide unit—either glucose or
 a phosphate group galactose,
 a platform molecule to which the fatty acid(s) and the phosphate group are attached  one fatty acid and sphingosine, but no phosphoric acid and glycerol.
 alcohol that is attached to the phosphate group.  occur primarily in the brain (7% of dry mass).
 Phosphatidic acid- parent compound  also present in the myelin sheath of nerves.
1. Glycerophospholipids 2. Gangliosides
COMPOSITION:  More complex sphingoglycolipids, contain a branched chain of up to seven monosaccharide
 two fatty acids  contain sphingosine, long chain fatty acids, hexoses (usually galactose or glucose) and
 phosphate group esterified to a glycerol molecule neuramic acid
 an alcohol esterified to the phosphate group  residues.occur in the gray matter of the brain as well as in the myelin sheath.
GLYCEROPHOSP HOLIPIDs 3. Globosides
AMINO ALCOHOL IONIC GROUP GLYCEROPHOSPHOLIPIDS OR
GLYCEROPHOSPHATIDES C. CHOLESTEROL
CHOLINE Quaternary ammonium group Phosphatidylcholine aka Lecithin  C27 steroid molecule that is a component of cell membranes and a precursor for other steroid-
ETHANOL AMINE (+) ion group Phosphatidylethanolamine Aka Cephalins based lipids.
SERINE 2 ionic group Phosphatidylserine Aka Cephalins  most abundant steroid in the human body
ORDES  steroid alcohol
PHOSPHATIDYLCHOLINE (lecithins)  can be isolated from plants, animals, and human beings
 the most abundant phospholipids of the cell membrane  LIMITED WATER SOLUBILITY: due to the lack of a large polar head group. The –OH group on carbon
 represents a large proportion of the body’s store of choline. 3 is considered the head of the molecule.
 Choline is important in nervous transmission, as acetylcholine, and as a store of labile
methyl groups. STEROID - is a lipid whose structure is based on a fused ring system that involves three 6-membered rings
 Dipalmitoyl lecithin - is a very effective surface active agent and a major constituent of and one 5-membered ring. This steroid fused-ring system, which is called the steroid nucleus,
the surfactant preventing adherence, due to surface tension, of the inner surfaces of the
lungs. Its absence from the lungs of premature infants causes respiratory distress
syndrome
PHOSPHATIDYLSERINE (CEPHALINS)
 Lipids associated with blood clotting
2. Sphingophospholipids
COMPOSITION:
 one fatty acid
 one phosphate group attached to a sphingosine molecule
 an alcohol attached to the phosphate group.
SPHINGOMYELIN - Sphingophospholipids in which the alcohol esterified to the phosphate group is OTHER SIGNIFICANCE: Within the human body
choline.  found in cell membranes (up to 25% by mass)
 are found in all cell membranes and are important structural components of the  in nerve tissue, in brain tissue (about 10% by dry mass)
myelin sheath, the protective and insulating coating that surrounds nerves.  Every 100 mL of human blood plasma contains about 50 mg of free cholesterol and about 170 mg of
cholesterol esterified with various fatty acids.

SOURCES OF CHOLESTEROL PASSIVE DIFFUSION aka PASSIVE TRANSPORT
o Dietary intake  90% drugs are transported across biologic membranes
o Biosynthesis in the liver and to a lesser extent in the intestines  Movement of drug if there is a concentration gradient , meaning, drug concentration on one side of
LIPOPROTEIN : Protein carrier system the membrane is higher than that of the other side
1. LDL - carry cholesterol from the liver to various cells or tissues of the body  No energy expenditure
 a major cholesterol transport protein which comprises 60% to 70% of total serum cholesterol  Drugs must be unionized, nonpolar and lipophilic
 is considered the “bad” cholesterol, and has been linked to atherosclerosis  First order kinetics
2. HDL - carry excess cholesterol from body tissues back to the liver for degradation to bile acids  Non-saturable process
 Are responsible for transport of 20% to 30% of serum cholesterol.  Consistent with Fick’s law of diffusion
 It is considered the “good” cholesterol, and elevated HDL levels are associated with a decreased  Examples of molecules that crosses this manner: O2, N2, H2O, CO2,urea, and ethanol
risk for CHD or Chronic Heart Disease
3. VLDL – transport triacylglycerols from the liver to adipose tissue FACILITATED DIFFUSION
4. CHYLOMICRONS – transport dietary triavylglycerols from the intestines to the liver and adipose tissue  The drug binds with an intrinsic factor carrier like vitamin B12
 It passes through the membrane but no energy expenditure
DISEASE ASSOCIATED WITH CHOLESTEROL:  Transfer is downhill and fast
 Atherosclerosis - a form of cardiovascular disease characterized by the buildup of plaque along the  Saturable process. The rate limiting step is the number of intrinsic factor
inner walls of arteries.  Examples of molecules that crosses this manner: Glucose, chloride ion, and bicarbonate ion
 Plaque - is a mound of lipid material mixed with smooth muscle cells and calcium. Much of the lipid
material in plaque is cholesterol. ACTIVE TRANSPORT
 Carier mediated
CELL MEMBRANE  Permeability is dependent on the number of carriers
 is a lipid-based structure that separates a cell’s aqueous-based interior from the aqueous  5-10% of drugs are transported this way, usually small MW drugs with structures similar to food
environment surrounding the cell. (peptides,nucleosides,nucleotides) so permeability is affected by the presence of food due to
 LIPID BILAYER- is a two-layer-thick structure of carrier competition of nutrients
phospholipids and glycolipids in which the  Saturable process. The rate limiting step is the number of carriers
nonpolar tails of the lipids are in the middle of  Zero order kinetics
the structure and the polar heads are on the  Can go against concentration gradient
outside surfaces of the structure.  Expends energy
o 6 to 9 nanometers thick.  Examples of molecules & drugs that crosses this manner:
o 3 distinct parts to the bilayer: o Sodium, potassium, and hydronium ions
 the exterior polar “heads,” o Centrally active amino acid-like drugs, methyldopa,gabapentin
 the interior polar “heads,” o Oral B-lactams antibiotics like amoxicillin and cephalexin
 and the central nonpolar o ACE inhibitors like enalapril
“tails o Folic acid
OTHERS:
2 TYPES OF MEMBRANE PROTEINS ENDOCYTOSIS
1. Integral membrane protein- is a membrane protein that penetrates the cell membrane  Drug particles are engulfed by the cell
2. Peripheral membrane protein- is a nonpenetrating membrane protein located on the surface of the cell  Examples: Vitamin A,D,E,K
membrane.  2 TYPES:
TRANSPORT MECHANISM ACROSS THE CELL: o Pinocytosis, in which the fluid material is engulfed (CELL DRINKING)
o Phagocytosis, in which large sized solid material is engulfed. (CELL EATING)
III. EMULSIFICATION LIPIDS: Bile Acids

BILE - a fluid containing emulsifying agents that is secreted by the liver, stored in the gallbladder, and
released into the small intestine during digestion.
BILE ACID - a cholesterol derivative that functions as a lipid-emulsifying agent in the aqueous environment of
the digestive tract
o Secreted in the duodenal papillae

o 3 ways Synthesization
 Parasympathetic stimulation of the vagus nerves GALLSTONE: Formation
causing the liver to contract and synthesize bile to  increased secretion of cholesterol
be stored in the gallbladder to release bile acids  decrease in the size of the bile pool
 Stimulation of the duodenum to secrete secretin,
a hormone that allows contraction of liver to
produce bile
 Stimulation of the duodenum to secrete
cholecystokinin to directly contract the
gallbladder to release bile acids.
EMULSIFIER - is a substance that can disperse an stabilize water-
insoluble substances as colloidal particles in an aqueous solution IV. MESSENGER LIPIDS:
 Regulatory lipids that act in the tissue where they are
FUNCTIONS OF BILE ACIDS:  synthesized or at other locations after transport via the
1. EMULSIFIER: it functions to emulsify fats and aids in the digestion  blood stream.
and absorption in the small intestine. They lower surface tension and  HORMONE (Aka chemical messenger)
thus can emulsify fats. o is a biochemical substance, produced by a ductless gland, that has a messenger function.
2. Helps neutralize acids in the stomach o It serves as a means of communication between various tissues.
3. They also activate lipases. o carry information and instructions from one group of cells to another.
I. STEROID HORMONES
Three respects of difference between cholesterol and bile acids: a. Sex Hormones - which control reproduction and secondary sex characteristics
1. They are tri- or dihydroxy cholesterol derivatives. i. Estrogen
2. The carbon 17 side chain of cholesterol has been oxidized to a ii. Progestins
carboxylic acid. iii. Androgen
3. The oxidized acid side chain is bonded to an amino acid (either b. Adrenoicorticoids
glycine or taurine) through an amide linkage. i. Mineralocorticoids
Average bile acid composition in normal human adult bile: ii. Glucocorticoids
 38% - cholic acid derivatives, II. EICOCANOIDS
 34% - 7-deoxycholic acid derivatives a. Prostaglandins
 28% - 12-deoxycholic acid derivatives b. Thromboxanes
c. Leukotrienes
I.STEROID HORMONE: is a hormone that is a cholesterol derivative

A. SEX HORMONE: which control reproduction and secondary sex characteristics
i.ESTROGEN: the female sex hormones
a.Sources:
 WOMEN: ovaries and adrenal cortex
 MEN: testes and adrenal gland
 either glycine or taurine attached to
b.Function in WOMEN:
the side-chain carboxyl group via an
 for the development of female secondary sex characteristics at the onset of puberty
amide linkage
 for regulation of the menstrual cycle
 The presence of this amino acid
 stimulate the development of the mammary glands during pregnancy
attachment increases
 induce estrus (heat) in animals
 both the polarity of the bile acid and
c.TYPES OF ESTROGEN
its water solubility.
1. Estradiol - the most commonly measured type of estrogen for nonpregnant women. The amount
of estradiol in a woman's blood varies throughout her menstrual cycle. After menopause, estradiol
production drops to a very low but constant level.

2. Estriol - levels usually are only measured during pregnancy. Estriol is produced in large amounts HIGH ESTROGEN IN MEN
by the placenta, the tissue that links the fetus to the mother. It can be detected as early as the 9th  Infertility
week of pregnancy, and its levels increase until delivery. Estriol can also be measured in urine.  Erectile dysfunction
 Gynecomastia
3. Estrone- may be measured in women who have gone through menopause to determine their
estrogen levels. It also may be measured in men or women who might have cancer of the ovaries, ii.PROGESTINS - the pregnancy hormones
testicles,or adrenal glands. a. Sources: synthesized : ovaries and the placenta
b. Function:
Estrogen & Pregnancy  Prepare the lining of the uterus for implantation of the fertilized ovum.
During the reproductive years, the pituitary gland in the brain generates hormones that cause a  They also suppress ovulation.
new egg to be released from its follicle each month. As the follicle develops, it produces estrogen, which  properly regulate the menstrual cycle and treat unusual stopping of the menstrual periods
causes the lining of the uterus to thicken. (amenorrhea)
Progesterone production increases after ovulation in the middle of a woman's cycle to prepare the  To prevent estrogen from thickening the lining of the uterus (endometrial hyperplasia) in women
lining to receive and nourish a fertilized egg so it can develop into a fetus. If fertilization does not occur, with HRT (hormone replacement therapy)
estrogen and progesterone levels drop sharply, the lining of the uterus breaks down and menstruation  To treat pain that is related to endometriosis
occurs. If fertilization does occur, estrogen and progesterone work together to prevent additional ovulation  To treat loss of appetite and severe weight or muscle loss in patients with AIDS or cancer
during pregnancy. Birth control pills (oral contraceptives) take advantage of this effect by regulating
hormone levels. They also result in the production of a very thin uterine lining, called the endometrium, ORAL CONTRACEPTIVE PILLS
which is unreceptive to a fertilized egg. Plus, they thicken the cervical mucus to prevent sperm from entering
 May contain estrogen and
the cervix and fertilizing an egg.
progesterone combination
or progestins alone
Other Roles of Estrogen
 used to suppress ovulation
 Bone. Estrogen produced by the ovaries helps prevent bone loss and works together with calcium,
as a method of birth control
vitamin D and other hormones and minerals to build bones. Thus preventing osteoporosis.
relieve menstrual cramps
 Vagina and Urinary Tract. When estrogen levels are low, as in menopause, the vagina can become
and some perimenopausal
drier and the vaginal walls thinner, making sex painful.
symptoms
 regulate menstrual cycles in
Other uses of Estrogen
women with polycystic
 Estrogen Therapy to treat certain conditions:
ovarian syndrome (PCOS)
 For delayed onset of puberty menopausal symptoms such as hot flashes and symptomatic
vaginal atrophy. Vaginal atrophy is a condition in which low estrogen levels cause a woman's
iii.ANDROGEN - the male sex
vagina to narrow, lose flexibility and take longer to lubricate.
hormones
 Female hypogonadism, a condition in which the ovaries produce little or no hormones, as well
I.Sources:
as premature ovarian failure, can also cause vaginal dryness, breast atrophy and lower sex
 MEN: testes and adrenal
drive
cortex
 to prevent osteoporosis and to improve women's overall health.
 WOMEN: androgens are
HIGH ESTROGEN IN WOMEN
produced in the ovaries,
 swelling and tenderness in the breasts
adrenal glands and fat cells
 irregular menstrual periods II. Function:
 headaches in Men:
 mood swings  development of male
 fibrocystic developments in the breast secondary sex characteristics.
 weight gain  promote muscle growth
 hair loss in women:
 cold hands or feet  stimulation of hair growth in pubic area and under arm during puberty
 feeling tired or lacking energy  precursor in the synthesis of estrogen
 difficulty with memory  key role to prevent bone loss and send desire for satisfaction
 trouble sleeping

III.TYPES OF ANDROGEN B. GLUCOCORTICOIDS - control glucose metabolism and
 TESTOSTERONE counteract inflammation.
 ANDROSTENEDIONE a. CORTISOL- the major glucocorticoid hormone and is
Other androgens produced in humans by the zona fasciculata of the adrenal
 dihydrotestosterone (DHT), cortex within the adrenal gland.
 dehydroepiandrosterone (DHEA)  It is released in response to stress and low blood-
 DHEA sulfate (DHEA-S) glucose concentration.
HIGH ANDROGEN:  It functions to increase blood sugar through
 VIRILIZING EFFECTS gluconeogenesis, to suppress the immune system,
 ACNE and to aid in themetabolism of fat, protein,and
 HIRSUTISM carbohydrates. It also decreases bone formation.
 SCALP BALDING  Cortisol and its synthetic ketone derivative
Additional effects in women:  cortisone exert powerful anti-inflammatory effects
PCOS – polycystic ovarian syndrome in the body.
o IRREGULAR MENSTRUATION
o WEIGHT GAIN
o INFERTILITY  cortisone and prednisolone, are used as prescription drugs to control inflammatory diseases such
o DIABETES – due to problem using insulin or as rheumatoid arthritis.
o insulin resistance
ANABOLIC STEROIDS or ANABOLIC-ANDROGENIC STEROIDS II.EICOSANOIDS:
 Are used to build up muscle strength and enhance endurance  is an oxygenated C20 fatty acid derivative that functions as a messenger lipid.
 ANDROGENIC EFFECT - masculinizing effect  metabolic precursor for most eicosanoids is arachidonic acid, the 20:4 fatty acid.
 ANABOLIC EFFECT – muscle building  are hormonelike molecules rather than true hormones because they are not transported in the
Common Side Effects That May Occur with Anabolic Steroid Use bloodstream to their site of action as true hormones are.
 Severe acne, oily skin and hair
 Hair loss The physiological effects of eicosanoids include medication of:
 Kidney disease 1. The inflammatory response, a normal response to tissue damage
 Heart disease such as heart attack and stroke 2. The production of pain and fever
 Altered mood, irritability, increased aggression, depression or suicidal tendencies 3. The regulation of blood pressure
 Alterations in cholesterol and other blood lipids 4. The induction of blood clotting
 High blood pressure 5. The control of reproductive functions, such as induction of labor
 Gynecomastia (abnormal development of mammary glands in men causing breast enlargement) 6. The regulation of the sleep/wake cycle
 Shrinking of testicles
MAJOR TYPE OF EICOSANOIDS:
 Azoospermia (absence of sperm in semen)
I. PROSTAGLANDINS - is a messenger lipid that is a C20-fatty-acid derivative that contains a cyclopentane ring
 Menstrual irregularities in women
and oxygen-containing functional groups.
 Infertility
 Regulatory functions:
 Excess facial or body hair deeper voice in women
o including raising body temperature,
 Stunted growth and height in teens o inhibiting the secretion of gastric juices,
 Risk of viral or bacterial infections due to unsterile injections o increasing the secretion of a protective mucus layer into the stomach,
 Suicidal attitudes o relaxing and contracting smooth muscle,
o directing water and electrolyte balance,
II.ADRENOCORTICOID HORMONES: o Intensifying pain, and enhancing inflammation responses.
A. MINERALOCORTICOIDS - control the balance of Na+ and K+ ions in cells and body fluids  Note: Aspirin reduces inflammation and fever because it inactivates enzymes needed for
a. ALDOSTERONE prostaglandin synthesis.
 main mineralocorticoid, is necessary for regulation of salt and water in the body.
 acts on the kidneys to provide active reabsorption of sodium and an associated passive II. THOMBOXANES - is a messenger lipid that is a C20- fatty-acid derivative that contains a cyclic ether ring
reabsorption of water, as well as, the active secretion of potassium in the principle cells of the and oxygen-containing functional groups.
cortical collecting tubule. This in turn results in an increase of blood pressure and blood volume.

 are produced by blood platelets and promote platelet aggregation. EXAMPLES OF WAXES:
 FUNCTIONS 1. CARNAUBA WAX
o to promote the formation of blood clots.  obtained from a species of Brazilian palm tree
 is a particularly hard wax whose uses involve high-gloss finishes: automobile wax, boat wax, floor
III. LEUKOTRIENES - is a messenger lipid that is a C20- fatty-acid derivative that contains three conjugated wax, and shoe wax.
double bonds and hydroxy groups. 2. LANOLIN
 found in leukocytes (white blood cells).  a mixture of waxes obtained from sheep wool,
 FUNCTIONS  used as a base for skin creams and ointments intended to enhance retention of water (which
o Various inflammatory and hypersensitivity (allergy) responses softens the skin).
3. PARAFFIN
 Mineral waxes
 resist moisture and chemicals and have no odor or taste.
 They serve as a waterproof coating for such paper products as milk cartons and waxed paper.
4. BEESWAX
 a blend of biological and mineral waxes
 sometimes a component of candle wax
PROTECTIVE COATING LIPIDS: BIOLOGICAL WAXES

BIOLOGICAL WAX
 is a lipid that is a monoester of a long-chain fatty acid and a long chain alcohol
 are monoesters, unlike fats and oils which are triesters.
 fatty acids found in biological waxes generally are saturated and contain from 14 to 36 carbon
atoms.
WAX
 is a pliable, water-repelling substance used particularly in protecting surfaces and producing
polished surfaces
 esters of high molecular weight, monohydric alcohols and high molecular weight fatty acids.
MINERAL WAX
 is a mixture of long-chain alkanes obtained from the processing of petroleum.

NUCLEIC ACID TYPES OF DNA
FEATURES A-DNA B-DNA Z-DNA

Helix turn Right Right Left
- Is an unbranched polymer in which the repeating monomer units are nucleotides. Major grove Narrow and Wide and Flat
- What is the most remarkable property of living cells? Deep Deep
It is the ability to produce exact replicas of themselves! Minor grove Wide and Narrow and Narrow
shallow deep and deep
Note: For the definition of terms, refer to your assignment Number of base pairs 11.6 10 12
per helical turn
FRIEDRICH MIESCHER Coined DNA
(1844–1895) molecule as
three-
Swiss physiologist, dimensional
discovered nucleic double helix
acids in 1869 while structure
studying the nuclei of
JAMES DEWEY WATSON and FRANCIS CRICK
white blood cells
Types of NUCLEIC ACIDS
• DNA - is a nucleotide polymer in which each of the monomers contains deoxyribose, a phosphate group, and
one of the heterocyclic bases adenine, cytosine, guanine, or thymine
• RNA - is a nucleotide polymer in which each of the monomers contains ribose, a phosphate group, and one of
the heterocyclic bases adenine, cytosine, guanine, or uracil.
FEATURES/STRUCTURE DNA RNA
TYPE OF STRAND Double helix Single strand

LENGTH OF STRANDS Longer Shorter
DNA is found in the nucleus, with a small RNA forms in the nucleolus, and then moves to NUCLEOTIDE -Building blocks of N.A.
LOCATION amount of DNA also present in specialized regions of the cytoplasm depending on 3 COMPONENT SUBUNIT
mitochondria. the type of RNA formed.
1. Phosphate
DNA replicates and stores and transfers RNA converts the genetic information contained - Derived from H3PO4(Phosphoric acid)
genetic information. It is a blueprint for all within DNA to a format used to build proteins, and - HPO4-2 (In blood pH conditions, loses 2 H+ ions)
PRIMARY FUNCTION
genetic information contained within an then moves it to ribosomal protein factories.
2. Sugar
organism
The sugar in DNA is deoxyribose, which RNA contains ribose sugar molecules, without the
SUGAR UNIT contains one less hydroxyl group than RNA’s hydroxyl modifications of deoxyribose.
ribose.
The bases in DNA are Adenine (‘A’), RNA shares Adenine (‘A’), Guanine (‘G’) and
Thymine (‘T’), Guanine (‘G’) and Cytosine (‘C’) with DNA, but contains Uracil RNA- Pentose Ribose DNA- Pentose Deoxyribose
NITROGENOUS
Cytosine (‘C’). (‘U’) rather than Thymine. 3. NitrogenousBase (5 N-bases)
BASES and pairing
Adenine and Thymine pair (A-T) Adenine and Uracil pair (A-U) - They contian an amine functional group
Cytosine and Guanine pair (C-G) Cytosine and Guanine pair (C-G)
 A – DNA  hnRNA
Pyrimidine Purine
MAJOR TYPES  B – DNA  snRNA
(6-membered ring) (Bicyclic Fused, w/ five-six membered ring)
(Briefly describe  Z – DNA  mRNA
each)  rRNA
 tRNA

CENTRAL DOGMA
Naming Nucleosides and Nucleotides
DNA REPLICATION
the biochemical process by which DNA molecules produce exact duplicates of themselves
Primary Nucleic Acid

Structure
is the sequence in
which nucleotides
are linked together
in a nucleic acid.
Primary Nucleic Acid Structure ANTIMETABOLITES

Human DNA - are a class of anticancer drugs that interfere with DNA
 30% Adenine & 30% Thymine; 20% Cytosine and 20% Guanine replication because their structures are similar to
 5’ 3’ and 3’ 5’ molecules required for normal DNA replication.
1. 6-Mercaptopurine (6-MP): structurally resembles adenine
 Two strands of double helix are “antiparallel”
 They are in opposite directions
 Bases from each strand are “complementary bases” 2. Thioguanine: As was the case with
 BASE PARING Most favorable base pairs:
6-MP, the close structural resemblance
Incorrectly pair: A=T G=C
between thioguanine and guanine leads to the incorporation of thioguanine,
Purine + Purine= OVERLAP What if?
rather than guanine, into nucleotides.
Pyrimidine + Pyrimidine= TOO SMALL AND FAR T&G  only 1 H-bond
Correctly pair: Purine (small) + Pyrimidine (big) C&A  only 1 H-bond

3. 5-Fluorouracil: Uracil is a base found in RNA rather than
DNA. However, its structure is close enough to that of
thymine (which is methyluracil) that it can pass for
thymine.
4. Methotrexate: It is a structural analog of folic acid

(folate). A derivative of folic acid is needed in one of the
early steps of nucleotide synthesis. Methotrexate inhibits GENETIC CODE
the conversion of folic acid to this needed derivative, which
shuts down DNA synthesis.
DNA TRANSCRIPTION
ANTICODON
POST-TRANSCRIPTION: Formation of mRNA

DNA TRANSLATION Antibiotic Protein Synthesis Inhibitors
Protein Synthesis 1. Erythromycin: binds to the larger bacterial ribosome subunit, blocking the exit of a growing
is the process by which mRNA codons are deciphered and a particular protein molecule is
peptide chain.
synthesized
STEPS:
2. Terramycin: blocks the A-site location on the ribosome, preventing the attachment of amino-acid
1. Activation carrying tRNAs.
2. Initiation 3. Streptomycin (see accompanying structural diagram): binds to the smaller bacterial ribosome
3. Elongation subunit causing a shape change, which in turn causes a misreading of mRNA information.
4. Termination 4. Neomycin: binds to the smaller bacterial ribosome subunit in a manner similar to streptomycin.
5. Chloramphenicol: binds to the ribosome and interferes with the formation of peptide bonds
1. ACTIVATION between amino acids.
2. INITIATION
MUTATION
is an error in base sequence in a gene that is
reproduced during DNA replication.
MUTAGEN
is a substance or agent that causes a change in the
structure of a gene.
3. ELONGATION: Translocation
SILENT MUTATION
code for the same amino acid (a "synonymous substitution"). A silent mutation does not
4. TERMINATION affect the functioning of the protein. A single nucleotide can change, but the new codon specifies the
same amino acid, resulting in an unmutated protein.
UAG This type of change is called synonymous change since the old and new codon code for the same
UAA amino acid.
UGA

MISSENSE MUTATION DELETION MUTATION
This type of mutation is a change in one DNA base pair that results in the substitution of one amino changes the number of DNA bases by
acid for another in the protein made by a gene. removing a piece of DNA. Small deletions may remove
one or a few base pairs within a gene, while larger
 CONSERVATIVE result in an amino deletions can remove an entire gene or several
acid change. However, the neighboring genes. The deleted DNA may alter the
properties of the amino acid remain function of the resulting protein(s).
the same (e.g., hydrophobic,
hydrophilic, etc.).
 NON-CONSERVATIVE result in an
amino acid change that has
different properties than the wild
type. The protein may lose its
function, which can result in a DUPLICATION MUTATION
disease in the organism. EX. sickle consists of a piece of DNA that is abnormally copied one or more
cell anemia (valine to glutamic acid) times. This type of mutation may alter the function of the resulting
protein.
NONSENSE MUTATION
FRAMESHIFT MUTATION
is also a change in one DNA base pair.  This type of mutation occurs when the
Instead of substituting one amino acid for addition or loss of DNA bases changes a gene's reading
another, however, the altered DNA sequence frame.
prematurely signals the cell to stop building a  A reading frame consists of groups of 3 bases
protein. This type of mutation results in a that each code for one amino acid.
shortened protein that may function  A frameshift mutation shifts the grouping of
improperly or not at all. these bases and changes the code for amino acids.
 The resulting protein is usually nonfunctional.
Insertions, deletions, and duplications can all be
frameshift mutations.
INSERTION MUTATION
changes the number of DNA bases in a REPEAT EXPANSION MUTATION
gene by adding a piece of DNA. As a result, the  Nucleotide repeats are short DNA sequences
protein made by the gene may not function that are repeated a number of times in a
properly. row. For example, a trinucleotide repeat is
made up of 3-base-pair sequences, and a
tetranucleotide repeat is made up of 4-base-
pair sequences.
 A repeat expansion is a mutation that
increases the number of times that the short

DNA sequence is repeated. This type of mutation can cause the resulting protein to function
improperly.
OTHER RELATED TOPICS:

 Virus
 Vaccine
 Genetic engineering
 Recombinant DNA polymerase chain reaction (PCR)
 Polymerase chain reaction is a method for rapidly producing
multiple
copies of a DNA nucleotide sequence
VIRUS
A small particle that contains DNA or RNA (but not both)
surrounded by a coat of protein and that cannot reproduce
without the aid of a host cell.
VACCINE is a preparation containing an inactive or weakened

form of a virus or An electron microscope image of an inflnuenza virus.
bacterium.
GENETIC ENGINEERING
is the process whereby an organism is intentionally
changed at the molecular (DNA) level so that it exhibits
different traits “Real dreams are NOT those that come at night when we
sleep.
Recombinant DNA (rDNA)
It is those that come when we don’t sleep while achieving
is DNA that contains genetic material from two
different organisms. it”
Recombinant DNA is made by inserting
a gene obtained from DNA of one
organism into the DNA from another
kind of organism.

Biochemistry Lecture Notes Cover Key Concepts for Health Sciences Students

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By the end of this course the students

are expected to:

BIOCHEMISTRY LECTURE d. Describe the pathways that

COMPILED NOTES e. Explain derangement in

Top 5 elements present in the human body: H, Ca, C, N, O

by: C.A.U, RPh Page 1

Give the 6 functions of Carbohydrates: CHIRALITY: Handedness in molecules

CLASSIFICATION OF CARBOHYDRATES AS TO MOLECULAR SIZE:

GUIDELINES FOR IDENTIFYING CHIRAL CENTERS

by: C.A.U, RPh Page 2

by: C.A.U, RPh Page 3

FISCHER PROJECTION STRUCTURES OF MONOSACCHARIDES

by: C.A.U, RPh Page 4

by: C.A.U, RPh Page 5

L and D forms are possible L and D form is not possible

If carbon 3 and its accompanying -H and -OH groups were eliminated

by: C.A.U, RPh Page 6

D-Galactose and D-glucose are epimers (diastereomers that differ

D-Mannose Hydrolysis of plant A constituent of many

D-Glucose (Aka ___________, ___________, ____________) D- fructose Structure D-glucose

by: C.A.U, RPh Page 7

by: C.A.U, RPh Page 8

Sucrase, the enzyme needed to break the a, b(1 : 2) linkage in sucrose, is

by: C.A.U, RPh Page 9

by: C.A.U, RPh Page 10

Hormonal Control of Carbohydrate Metabolism

by: C.A.U, RPh Page 11

HOLOENZYME COFACTOR APOENZYME

by: C.A.U, RPh Page 12

Cu2+, Zn2+ Superoxide dismutase

Mn2+ Pyruvate carboxylase

carry electrons between two segments of the electron-transport chain.

by: C.A.U, RPh Page 13

TRANSFERASES Transaminases transfer of an amino group between substrates

HYDROLASES Lipases hydrolysis of ester linkages in lipids

LYASES dehydratases removal of H2O from a substrate

by: C.A.U, RPh Page 14

by: C.A.U, RPh Page 15

BIOCHEMICAL IMPOTRTANCE: Enzymes

by: C.A.U, RPh Page 16

Amylase Liver and pancreatic disease CONDITION ISOENZYME PATTERN

Myocardial infarction Moderate elevation of LDH1, slight elevation of LDH2

Muscular dystrophy Elevation of LDH1-3

Arthritis with joint infections Elevation of LDH5

Glutamic oxaloacetic transaminase Myocardial infarction

Glutamic pyruvic transaminase Infectious hepatitis

Trypsin Acute pancreatitis

Ceruplasmin Wilson’s disease

by: C.A.U, RPh Page 17

AMINO ACIDS: Glycine Alanine Valine Leucine Isoleucine

_________________________- is an amino acid in which

NAMING AMINO ACIDS

A Aliphatic R group (methyl)

V Aliphatic R group (isopropyl)

L Aliphatic R group (additional methylene group)

I Aliphatic R group (isobutyl group)

P Aliphatic R group (propyl)

F Aromatic Ring (Phenyl group/ alanine w/ phenyl substituent on the  -

M Sulfur group (thioether)

by: C.A.U, RPh Page 18

serine cysteine Threonine Both Keto and Gluco

Asparagine Glutamine Tyrosine

D-Glucose (Aka _____, _, ________) D- fructose Structure D-glucose