BIOCHEMISTRY REVIEW NOTES

Claire E. Palma, RPh

I. INTRODUCTION
Biochemistry
 Is the study of molecular basis of life.
 Is the study of chemical processes in living organism, including, but not limited to, living matter.
 It is concerned with the structure and chemical processes of biomolecules found in or produced by
organisms.
 BIOMOLECULES: Carbohydrates, proteins, lipids and nucleic acids

CELL
It is a functional basic unit of life
Discovered by Robert Hooke
A highly organized unit with specialized structure called organelles
UNICELLULAR MULTICELLULAR
- Simple organism consists of single - Composed of an estimate of 100 trillion
cells - Ex. HUMANS
- Ex. BACTERIA
*** Largest cell known: UNFERTILIZED OSTRICH EGG CELLS
PROKARYOTES EUKARYOTES
- Do not have true nucleus or - Have a defined nucleus and internal
internal membrane structure organelles surrounded by membranes
- Ex. Bacteria and Archea - Ex. Yeasts, fungi, plants, and animals
PROKARYOATIC CELL EUKARYOTIC CELL
- Capsule Animal cell Plant cell
- Cell wall
- Cell - VACUOLE
- Plasma membrane
membrane - Chloroplast
- Cytoplasm
- Cytoplasm - Cytoplasm
- Ribosomes
- Mitochondrion - Mitochondrion
- Plasmid
- Lysosome - Cell membrane
- Pili
- Golgi body - Nuclear
- Bacterial flagellum
- Endoplasmic envelope
- Nucleoid
reticulum - Nucleolus
(rough and - Nucleus
smooth) - Endoplasmic
- Nucleus reticulum
- Cytoskeleton - Golgi apparatus
- cell wall
THE ORGANELLES
1. PLASMA/CELL MEMBRANE
- A double layer of lipids and phosphorus with protein molecules = phosphobilipid layer.
- Separates cell contents from surroundings. A barrier for extra & intracellular substances.
o Extra: Na+, Ca ++ & Cl-.
o Intra: K+, enzymes & glycogen.
- provides mechanical strength and shape to the cell
- actively involved in selecting which molecules can enter or exit the cell = SEMIPERMEABLE MEMBRANE

MOVEMENTs through the membrane:

1. Lipid soluble molecules pass readily by dissolving in the lipid portion of the membrane.
2. Small molecules and ions pass though channels.
3. Large molecules & nonlipid-soluble transport by carrier molecules & vesicles
 These movements are:
 Diffusion
 Osmosis
 Filtration
 Mediated transport (facilitated diffusion, active transport, secondary active transport)
 Endocytosis (phagocytosis & pinocytosis)
  Exocytosis

2. CYTOPLASM
i. The living material surrounding the nucleus enclosed within the cell membrane
ii. Contains the organelles & cytosol
iii. Cytosol – the fluid portion of the cytoplasm.
3. NUCLEUS
i. Contains the genetic material, and the machinery for converting that information into
protein molecules,
ii. known as the control center of the cell
iii. Nucleolus – inner part of the nucleus, is the site of ribosomal RNA synthesis & ribosomal
subunit assembly.
iv. consist of the nucleoplasm that is bounded by the nuclear envelope
v. nucleoplasm= network of chromatin fibers composed of DNA and histones
4. ROUGH ENDOPLASMIC RETICULUM
i. Rough appearance due to ribosomes attached to it.
ii. A site of protein synthesis for incorporation into membrane and cellular organelles & for
export to the outside of the cell.
5. SMOOTH ENDOPLASMIC RETICULUM
i. Site for lipid & steroid synthesis.
ii. Also a site for metabolism of carbohydrate & drug detoxification
6. GOLGI APPARATUS/COMPLEX
i. Involved in packaging and secretion for cell products (such as proteins & lipids)
ii. Transport of substances into the cell wall.
iii. Major site of new membrane synthesis & participates in formation of lysosomes &
peroxisomes.
7. LYSOSOMES
i. Contains enzymes that digests vesicles formed from endocytosis which are intra &
extracellular substances that must be removed.
ii. Hydrolases enzyme catalyse hydrolysis of proteins, carbohydrates, nucleic acids & lipids.
8. PEROXISOMES
1. contain oxidative enzymes for break down of lipid (lipid oxidation)
2. most noted for their involvement in the generation and breakdown of toxic
molecules known as peroxides to water anD oxygen.
9. MITOCHONDRIA
i. Powerhouse of the cell, because it is the site of ATP production by cellular respiration,
which is the major energy source for various chemical reactions.
10. RIBOSOMES
i. Site of biosynthesis of proteins
ii. composed of a variety of proteins and a type of RNA called rRNA.
iii. With 2 subunits, the smaller subunit that binds to mRNA and the larger subunit that binds
to tRNA and amino acids.
iv. rRNA come together to form whole ribosomes when protein synthesis is initiated.
11. CYTOSKELETON
 a highly structured network of proteinaceous filaments
 responsible for maintenance of overall cell shape and facilitation of cell movements, intracellular
transport,
and cell division.
 components: microtubules,
microfilaments
& intermediate fibers
12. CENTRIOLES
i. Microtubule formation site
ii. Involved in organization of the mitotic spindle.
iii. Becomes the centrosome that build mitotic spindle that interact with chromosomes during
mitosis.
13. CILIA, FLAGELLA, & MICROVILLI
i. Cilia – move substances over surfaces of cells
 ii. Flagella – longer compared to cilia & used to propels the cell.
iii. Microvilli – increases the surface area of a cell
PROTEINS

Monomer: amino acids

2nd most abundant molecule in the cells
elemental composition: Carbon (C), Hydrogen (H), Nitrogen (N), Oxygen (O), some also contain Sulfur (S)
ALL PROTEINS are polymers of only 20 amino acids

AMINO ACIDS
 An organic compound that contains both amino (-NH2) and carboxyl (-COOH) groups attached to the same
Carbon atom.

 The position of carbon atom is Alpha

(a)
 R = side chain – vary in size, shape,
charge, functional groups present,
hydrogen bonding ability, and chemical
reactivity.
 Many protein also contain derived amino acid (formed by enzymatic modification of a common amino
acid after it has been incorporated into a protein).
 >700 amino acids are known
 Based on common R groups, there are 20 standard amino acids
 All amino acids have a chiral center except Glycine
FUNCTIONS OF A.A:
1. Chemical messengers = as neurotransmitters
*neurotransmitters are substances released from one nerve cell that influence the function
of the second nerve or muscle cell)
 Glycine
 Gamma-amino butyric acid (der. of glutamate)
 Serotonin & melatonin (der. of tryptophan)
2. Metabolic intermediates
 Arginine, citrulline, ornithine – components of urea cycle
3. Hormones ( chemical signal molecules produced in one cell that regulate the functions of other
cells.
 Thyroxine (der. of tyrosine) - hormone in thyroid gland
 Indole acetic acid – hormone in plants
4. Precursor of complex N-containing molecules
 Nitrogenous base in nucleotides
 Heme
 Chlorophyll

THE AMINO ACIDS AND THEIR ABBREVIATIONS

Amino Acid 3 letters 1 letter Amino Acid 3 letters 1 letter

Alanine Ala A Methionine Met M
Cystine Cys C Asparagine Asn N
Aspartate Asp D Proline Pro P
Glutamate Glu E Glutamine Gln Q
Phenylalanine Phe F Arginine Arg R
Glycine Gly G Serine Ser S
Histidine His H Threonine Thr T
Isoleucine Ile I Valine Val V
Lysine Lys K Tryptophan Trp W
Leucine Leu L Tyrosine Tyr Y

TYPES OF STANDARD AMINO ACIDS

  Neutral Non-polar: R groups (hydrocarbon) are non-polar, interact poorly with water. Aliphatic & Aromatic
HC side chains.
 Neutral Polar: R groups are polar, easily interact with water, but contain neutral side chains
 Polar acidic: Contain Carboxylic group as part of the side chains
 Polar basic: Contain amino group as part of the side chain

NON-POLAR AMINO ACIDS

POLAR AMINO ACIDS

SIDE CHAINS OF AMINO ACIDS OR THE R GROUPS

 MONOCARBOXYLIC – MONOAMINO  Heterocyclic
groups  Proline – α-imino
 Alkyl side groups  Carboxamine groups
 Glycine – H (hydrogen side  Asparagine - carbonyl group and
chain) an amide group with 1
 Alanine – CH3 – (methyl) methylene carbon
 Valine – isopropyl  Glutamine - carbonyl group and
 Leucine – isobutyl an amide group with 2
 Isoleucine – isobutyl methylene carbon
 Aromatic groups (attached by –CH2 –)  MONOAMINO – DICARBOXYLIC groups
 Phenylalanine – benzene ring  Aspartate – with methylene
 Tyrosine – phenol carbon
 Tryptophan – indole  Glutamate – with 2 methylene
 Sulfur containing carbons
 Cysteine – thiolmethyl  DIAMINO – MONOCARBOXYLIC groups
 Methionine – methyl ethyl  Lysine – N-butyl amine
thiol  Arginine – guanidino with 3
 Hydroxy-alcohol containing methylene carbon
 Serine – hydroxymethyl  Histidine – imidazole
 Threonine – ethanol

Essential Non
Essential
Histidine Alanine
Isoleucine Asparagine
Leucine Aspartic
Acid
 Proteins Functions

Lysine Cysteine
Threonine Glutamine Insulin enzyme for sugar metabolism
Tryptophan Glycine Hemoglobin oxygen transport in blood
Phenylalanine Glutamic
Acid Collagen Provides support in the connecective
tissues
Methionine Proline
Valine Serine Keratin Hair and skin
Arginine Tyrosine Anti bodies part of immune system in blood
Actin & Muscle contraction and movement
2 types of isomers: Myosin
• Constitutional Isomers – have the
same molecular formula but differ in the way their atoms are connected
• Stereoisomers – a.k.a. Configurational Isomers. Atoms are connected in the same way, but
arranged differently in space
• Types of stereoisomers:
• D-isomers – are found in monosaccharide and some bacteria's
• L-isomers – are found in naturally occurring proteins and amino acids.
• Enantiomers – are mirror images of each other that are non-superimposed images
Isoelectric point – pH at which the concentration of Zwitter ion is maximum
• Different amino acids have different isoelectric points
• At isoelectric point – amino acids are not attracted towards an applied electric field their net
charge is zero.
• Amino acids are less soluble at this pH
• Zwitter ions crystallize relatively easy
BUFFER- a solution that resists change in pH following the addition of an acid or base. A buffer can be created by
mixing a weak acid (HA) with its conjugate base (A-) or weak acid and its salt.
AMINO ACID REACTIONS:
1. Peptide bond formation - Peptide bonds are amide linkages (RCONH2) formed by dehyration reaction or
removal of water molecule.
a. Every peptide has an N-terminal end and a C-terminal end: H3N+ -aa-aa-aa-aa-aa-aa-aa- COO-.
Naming starts from the N-terminal where all amino acids suffixes are changed to –yl (ex. Glycine –
Glycyl) up to C-terminal where the name of last amino acid attached to C-terminal is retained. For
example, a tripeptide composed of an N-terminal valine, a glycine, and a C-terminal leucine is
called valylglycylleucine.
2. Disulfide bridge formation - Disulfide bridges help stabilize many polypeptides and proteins.
Cysteine Oxidation – oxidation of two Cysteine molecules to form Cystine
When 2 Cysteine residues form a bond it is referred to as a disulfide bond
3. Separation of Proteins on Basis of Charge
 Electrophoresis – protein dissolved in a buffer solution at a particular pH is placed in an electric
field. Charged proteins migrate towards the oppositely charged poles. Anode & cathode
 Ion-exchange – column chromatography is used for preparative separation of proteins by
charge. Ion-exchange resin consist of insoluble material that contain charged groups. (-) & (+)
charged resin.
 Ultracentrifugation – a protein subjected to centrifugal force moves in the direction of the
force at a velocity dependent on its mass.
 Molecular Exclusion Chromatography – a porous gel in the form of small insoluble beads is
commonly used to separate proteins by size in column chromatography.
• Small proteins penetrate the pores of the gel
• Large proteins, which are excluded from the pores
CLASSIFICATION OF PROTEINS BASED ON CHEMICAL COMPOSITION
• Simple proteins – a protein in which only amino acid residues are present.
• More than one protein subunit may be present but all subunits contain only amino acids.
• Conjugated proteins – a protein that has one or more non-amino acid entities (prosthetic groups)
present in its structure.
• One or more polypeptide chains may be present.
• Non-amino acid components – may be organic or inorganic – prosthetic groups
• Metaloproteins contain a specific metal as a prosthethic group
• Apoproteins – a protein without its prosthetic groups
 • Holoprotein – a protein molecule combined with its prosthetic group.
• APOPROTEIN + PROSTHETIC GROUP= HOLOPROTEIN
STRUCTURAL ORGANIZATION OF PROTEINS
1. PRIMARY STRUCTURE - is the sequence of amino acids comprising the molecule; connected by PEPTIDE
BOND
2. SECONDARY STRUCTURE - refers to the spatial arrangement of amino acids residues that are adjacent in
the primary structure. One peptide bond form a hydrogen bond to another peptide bond.
Globular proteins – compactly folded and coiled
Fibrous proteins – more filamentous or elongated
a. Types of Secondary Structure
i. α-helix - is a rigid, rodlike structure that forms when a polypeptide chain twists into a right
handed helical conformation
ii. β-pleated sheet - The primary structure is extended instead of tightly winding into a helix.
They are stabilized by hydrogen bonds.
SUPERSECONDARY STRUCTURE
• βaβ unit – two parallel β-pleated sheets are connected by an a-helix segment
• Β-meander pattern – two antiparallel β-sheets by amino acids and glycines to effect an abrupt
change in direction. Aka reverse or β-turns.
• aa-units – two successive a-helices separated by a loop.
• β-barrel – arrangements are formed when various β-sheet configuration fold back on
themselves.
• Greek key – antiparallel β-sheet doubles back on itself
3. TERTIARY STRUCTURE - The overall three-dimensional arrangement of all atoms in a protein. Refers both
to the folding of domains and final arrangement of domains in the polypeptide.
Domains – are the fundamental functional and three-dimensional structural units of a polypeptide
INTERACTION THAT STABILIZE TERTIARY STRUCTURE
• Disulfide bond – covalent, strong, between two cysteine groups.
• Electrostatic interactions – salt bridge between charged side chains of acidic and basic amino
acids.
• Hydrogen bonding –between polar acidic and/or basic R groups
• Hydrophobic interactions – between non-polar side chains
4. QUATERNARY STRUCTURE - highest level of protein organization.
Proteins with Quaternary structure are often referred to as oligomeric proteins.
Oligomers
a. refers to multisubunit proteins in which some or all subunits are identical.
b. Oligomers are composed of protomers.
c. Protomers refers to a single subunit or a group of subunits.
CLASSIFICATIONS OF PROTEINS ACCORDING TO STRUCTURE
• Globular proteins
• Compact spherical molecules that are usually water soluble.
• Can undergo denaturation
• Function as enzymes and intracellular signaling molecules.
• E.g. Hemoglobin, myoglobin
• MYOGLOBIN - A hemeprotein present in heart and skeletal muscle. Has a higher affinity for
oxygen than hemoglobin. First protein to have its three dimensional structure revealed.
Monomer – single peptide chain with one heme u
• HEMOGLOBIN - A hemeprotein present in red blood cells. Its main function is to transport
oxygen from the lungs to the capillaries of the tissues. Hemoglobin can transport up to 4
oxygen molecules. Tetramer (four peptide chains) – each subunit has a heme group.

• Fibrous proteins
• Are long, rod shaped molecules that are insoluble in water and physically tough
• Contains large amounts of regular secondary structure
• Low solubility in water
• Function: For structure and support.
• E.g. Collagen myosin, keratin, and tropomyosin
• COLLAGEN - Most abundant protein in the human body (30% of total body protein). Most
abundant protein in vertebrates. Glycine constitutes approximately one-third of the amino
acid residues of collagen. Vitamin C is needed in the synthesis of collagen.
 • Alpha-KERATIN - Class of proteins found in hair, wool, skin, horns, and fingernails. Provide
protective coating for organs. Hydrogen bonds and disulfide bridges are the principal
interactions between profilament subunits.
• SILK-FIBROIN - Also known as B-keratin. Consists mostly of small amino acid residues. e.g.
Glycine, serine or alanine. Insects and spiders produce silk that contain silk fibroin.
• ELASTIN - Is a connective tissue protein with rubber-like properties. Usually present in the
lungs, the walls of large arteries and elastic ligaments. Elastin is rich in proline and lysine
amino acid residues.
DISEASES ASSOCIATED WITH PROTEINS:
1. KWASHIORKOR – protein deficiency. Symptoms: Edema, Irritability, Anorexia, Ulcerating dermatoses,
Enlarged liver with fatty infiltrates
2. MARASMUS – energy deficiency (severe deficiency of proteins and carbohydrates). Symptoms:
Extensive tissue and muscle wasting, Variable edema, Dry skin, Loose skin folds over buttocks and
armpit, Drastic loss of adipose tissues, Patients are often irritable and voraciously hungry
COLLAGEN DISEASES:
1. EHLERS-DANLOS SYNDROME - inheritable defects in the metabolism of fibrillar collagen molecules. Most
clinically important mutations are found in the gene for type III collagen.
2. OSTEOGENESIS IMPERFECTA – aka Brittle bone syndrome. Mutations in the Type I Collagen
Two types :Type I also known as: Osteogenesis imperfecta tarda and Type II also known as:
Osteogenesis imperfecta congenita
3. SCURVY – Vit C Deficiency resulting to decrease collagen synthesis. A.k.a. Barlow’s disease(in infants),
Moeller’s disease and Cheadle’s disease.
4. SICKLE CELL ANEMIA - A genetic disorder of the blood caused by a single nucleotide alteration in the B-
globin gene.
5. METHEMOGLOBINEMIA - Oxidation of the heme component of hemoglobin to the ferric state forms
methemoglobin, which cannot bind to oxygen. Characterized by chocolate cyanosis and chocolate
colored-blood
6. MAPLE SYRUP URINE DISEASE - A.k.a branched-chain ketoaciduria. Deficiency of the branched-chain
alpha-keto acid dehydrogenase complex, leading to a build up of the branched-chain amino acids (leucine,
isoleucine, and valine) and their toxic products in the blood and urine.

TESTS FOR PROTEINS: - Detect tyrosine,trytophan, phenylalanine( R

A. BIURET TEST group-aromatic ring)
- General test for proteins - POSITIVE RESULT: ORANGE YELLOW SOL’N
- Detect the presence of peptide linkages(- E. HOPKIN’S COLE TEST
CONH-) - It is specific for tryptophan(containing indole
- POSITIVE RESULT: PURPLE SOL’N group)
B. MILLON’S TEST - involves condensation of tryptophan to form
- Identify proteins containing phenol side a violet colored complex upon the reaction
chain(tyrosine) with glyoxylic acid (CHOCOOH) and conc.
- POSTIVE RESULT: BRICK RED PPT sulfuric acid
C. NINHYDRIN TEST - POSITIVE RESULT : VIOLET RING AT THE
- Detect α- amino acids JUNCTION
- Positive for proteins in which the amino F. TEST FOR SH GROUP
group is attached to the alpha carbon - detect sulfur containing amino acids
- POSITIVE RESULT: BLUE VIOLET SOL’N (cysteine & methionine)
D. XANTHOPROTEIC TEST - POSITIVE RESULT: BLACK PPT.

CARBOHYDRATES
- hydrates of carbon
- General formula: CnH2nOn or Cn(H2O)n
- polyhydroxyaldehydes & polyhydroxyketones and their derivatives
- most abundant biochemical
- raw materials for the synthesis of other biochemicals (components of nucleic acids: pentose sugars ribose
and deoxyribose)
- MONOSACCHARIDES : simple sugars, building blocks of carbohydrates; an be linked together by
glycosidic bonds to form larger structures
 - SIMPLEST ALDOSE: glyceraldehyde
- SIMPLEST KETOSE: dihydroxyacetone
- The most important monosaccharide from the standpoint of food are hexoses
- The most abundant monosaccharides found in living cells are the pentoses and hexoses
Examples:
2 C: diose (hydroxyacetaldehyde) Monosaccharides found in humans:
3 C: triose (Glyceraldehyde & 3 carbons: Glyceraldehyde
dihydroxyacetone) 4 carbons: Erythrose
4 C: tetrose (Erythrose) 5 carbons: Ribose
5 C: pentose (Ribose, deoxyribose, xylose, 6 carbons: Hexose
arabinose) 7 carbons: Sedoheptulose
6 C: hexose (fructose, glucose, galactose, 9 carbons: Neuraminic acid
mannose)
MONOSACCHARIDES STRUCTURE
EPIMERS- diastereomers that differ in the configuration at a single asymmetric carbon atom (nag iba lang ng
position ng substituents sa isang carbon lang, in contrast to anomers na nagkaiba sa 1 st carbon)
E.g. D-glucose and D- galactose at carbon 4, D-glucose and D-Mannose at carbon 2.
Optical isomers – isomers that can rotate plane polarized light in opposite directions (ang makaka-rotate lang
ang may chiral center). Glyceraldehyde is the reference compound for optical isomers. E.g. D-glyceraldehyde
FISCHER PROJECTIONS - Was devised by the German chemist Emil Fischer
In these structures the carbohydrate backbone is drawn vertically with the most highly oxidized carbon
usually shown at the top.
Whether D or L, is indicated by the direction of the hydroxyl group attached to the reference carbon.
HAWORTH STRUCTURE - Was developed by W.N. Haworth
Haworth structures more closely depict proper bond angles and lengths than do Fischer representations.
IMPORTANT MONOSACCHARIDES
 Glucose
D-glucose, also known as dextrose, or blood sugar.
Most common
 Fructose
D-fructose, or levoluse, is often referred to as fruit sugar because of its high content in fruit.
Fructose is twice as sweet as sucrose.
Food for diabetics and used in infant feeding.
 Galactose
Is necessary to synthesize a variety of biomolecules. E.g. Lactose, glycoproteins, phospholipids, glycolipids.
 Xylose
Wood sugar
A diagnostic agent to evaluate intestinal absorption as it is absorbed in the intestines.
 Ribose
The monosaccharides D-ribose and D-deoxyribose are important components of the nucleic acids.
They are present in these complex molecules in the form of a furanose ring.
REACTIONS OF MONOSACCHARIDES
 Mutarotation
Spontaneous process which involves the interconversion of a- and β- forms of monosaccharides when
dissolved in water(haworth structure or cyclic form: β- forms- nasa taas ang OH, a-forms- nasa baba ang
OH)
 Oxidation
Oxidation of an aldehyde group yields an aldonic acid,
Oxidation of a terminal CH2OH group (but not the aldehyde group) gives an uronic acid
Oxidation of both the aldehyde and CH2OH gives an aldaric acid.
Sugars that can be oxidized by weak oxidizing agents are called as reducing sugars
All monosaccharides are reducing sugars
REDUCING SUGARS - they are reducing agents in certain redox reactions because of the aldehyde group
Fehling’s solution or Benedict’s solution - Cu (II) sulfate reduced to Cu2O (brick red pricipitate)
 Reduction
Reduction of the aldehyde and ketone groups of monosaccharides yields the sugar alcohols. (recall:
alcohol oxidation yields aldehyde. Aldehyde reduction results to formation of alcohol “baliktadin”)E.g.
Reduction of D-glucose, for example yields D-glucitol, also known as D-sorbitol.
 Isomerization
 Monosaccharides could undergo several types of isomerization. E.g. Epimerization, aldose-ketose
interconversion
 Esterification
Carbohydrates can be converted to esters by reactions with acids. Esterification often dramatically
changes a sugar’s chemical and physical properties. (again, draw the reaction: alcohol (present in
carbohydrates) plus carboxylic acid results to formation of esters plus water
 Glycoside formation
 Hemiacetals react with alcohol to form acetals. The new linkage is called a glycoside linkage, and
the compound is called glycoside.
DISACCHARIDES: Consists of two monosaccharides joined by an O-glycosidic bond (ether bond, R-O-R or
monosaccharide connected to O then another monosaccharide), which is formed when a hydroxyl group of one
sugar reacts with the anomeric carbon of the other.
 Lactose
Disaccharide found in milk (milk sugar).
B(1,4) glycosidic linkage between Glucose and Galactose
Reducing sugar
 Maltose
Malt sugar, is an intermediate product of starch hydrolysis.
a(1,4) glycosidic linkage between 2 D-glucose
 Cellobiose
A degradation product of cellulose
a B(1,4) glycosidic bond between 2 D-glucose
 Sucrose
Contains both a-glucose and B-fructose residues linked by alpha, beta (1,2) glycosidic bond
nonreducing sugar
OLIGOSACCHARIDES: Composed of 3 – 12 monosaccharide units.
POLYSACCHARIDES: Also known as glycans.
Used for storage and structure
Two classes of Polysaccharides
Homopolysaccharide - Contain only a single type of monomer
Heteropolysaccharide – Contain two or more different kinds of polymers.
HOMOPOLYSACCHARIDES:
 Starch
The energy reservoir of plant cells. Is a significant source of carbohydrate in the human diet.
Contains two types of glucose polymer:
Amylose – unbranched chains of d-glucose that are linked with a(1,4) glycosidic bonds
Amylopectin- is a branched polymer containing a(1,4) and a(1,6) glycosidic linkages. The a(1,6)
branch points may occur every 24-30 glucose units.
 Glycogen
Is the main storage polysaccharide of animal cells.
Glycogen is a polymer of (a1-4) linkage subunits of glucose with (a1-6) linked branches (every
8-12)
Glycogen is more extensively branched and more compact than starch.
 Dextran
Are bacterial and yeast polysaccharides.
Made up of a(1,6) linked poly-D-glucose; all have a(1-3) branches, and some also have a(1-
2) or a(1-4) branches.
Dental plaque , formed by bacteria growing on the surface of teeth, is rich on dextrans.
 Cellulose
A polymer of D-glucopyranose residues linked by B(1,4) glycosidic bonds.
The most important structural polysaccharide of plants.
 Chitin
Linear homopolysaccharide composed of N-acetylglucosamine residues in B-linkages.
The only chemical difference from cellulose is the replacement of the hydroxyl group at C-2
with an acetylated amino group.
Principal component of the hard exoskeletons of nearly a million species of arthropods
(insects, lobsters, and crabs)
Second most abundant polysaccharide, next to cellulose.
Most abundant organic substance on earth
 HETEROPOLYSACCHARIDES
Are high molecular weight carbohydrate molecules that contain more than one kind of
monosaccharide.
Heteropolysaccharides provide extracellular support for organisms of all kingdoms.
 Peptidoglycan
Bacterial and Algal Cell Walls Contain Structural Heteropolysaccharides
the rigid component of bacterial cell walls is a heteropolymer of alternating B-(1,4)-linked N-
acetylglucosamine and N-acetylmuramic acid residues.
 Glycosaminoglycans
are a family of linear polymers composed of repeating disaccharide units. One of the two
monosaccharides is always either N-acetylglucosamine or N-acetyl-galactosamine; the other is
in most cases a uronic acid, usually D-glucuronic or L-iduronic.
 Hyaluronic acid form clear, highly viscous solutions that serve as lubricants in the
synovial fluid of joints and give the vitreous humor of the vertebrate eye its jellylike
consistency. Hyaluronate is also an essential component of the extracellular matrix
of cartilage and tendons, to which it contributes tensile strength and elasticity as a
result of its strong interactions with other components of the matrix.
 Chondroitin sulfate contributes to the tensile strength of cartilage, tendons,
ligaments, and the walls of the aorta.
 Dermatan sulfate contributes to the pliability of skin and is also present in blood
vessels and heart valves.
 Keratan sulfates are present in cornea, cartilage, bone, and a variety of horny
structures formed of dead cells: horn, hair, hoofs, nails, and claws.
 Heparin is a natural anticoagulant made in mast cells and released into the blood,
where it inhibits blood coagulation by binding to the protein antithrombin.
GLYCOCONJUGATES
Compounds that result from the covalent linkages of a carbohydrate molecules to both proteins and
lipids.
 Proteoglycans
contains GAG chains linked to a protein molecule by N- and O-glycoside linkages.
contribute support and elasticity to tissues
 Glycoproteins
protein that are covalently linked to a carbohydrate through N- or O-linkages.
do not contain uronic acids, sulfate groups, and disaccharide repeating units compared with your
proteoglycans.
 Glycolipids and lipopolysaccharides
components of the plasma membrane with covalently attached oligosaccharide chains exposed on
the cell’s outer surface.
CARBOHYDATE-ASSOCIATED DISEASES
 Lactose intolerance
Also known as lactase deficiency or hypolactasia
inability to digest and metabolize lactose
Caused by a lack of lactase, the enzyme required to break down lactose in the digestive system.
Symptoms: abdominal pain, bloating, flatulence, diarrhea, nausea and acid reflux
 Glycogen storage disease
Also known as glycogenosis and dextrinosis
result of defects in the processing of glycogen synthesis or breakdown within muscles, liver, and other cell
types.
Two classes: genetic and acquired
 Galactosemia
rare genetic metabolic disorder that affects an individual’s ability to metabolize the sugar galactose
properly.
Long term complication: Speech deficits, ataxia, dementia, diminished bone density, cataract.
 G6PD deficiency
an X-linked recessive hereditary disease by abnormally low levels of glucose-6-phosphate dehydrogenase.
Manifestation: neonatal jaundice, kernicterus, hemolytic crisis, acute renal failure.
 Diabetes mellitus
group of metabolic diseases in which a person has high blood sugar, either because the body does not
produce enough insulin, or because cells do not respond to the insulin that is produced.
 Symptoms: polyuria, polydipsia, and polyphagia
ENZYMES
- Complex biological molecules
- Primarily or entirely made up of proteins (most are globular proteins)
- Undergoes denaturation
- Behaves as biological catalyst (the most effective catalyst known)
BASIC requirement for ENZYME ACTIVITY
• Body Temperature
• pH Near 7
• Aqueous solution (soluble in water, glycerol & diluted alcohol.
• Modest amount of salts
Vitamins Coenzymes Reaction Deficiency
Vitamin B1 (Thiamine) Thiamine pyrophosphate Transketolation & Beri-beri, peripheral
oxidative decarboxylation neuropathies, muscle
cramps, numbness &
Wernicke’s korsakoff’s
syndrome

Vitamin B2 (RIBOFLAVIN) Flavin mononucleotide & Redox reaction rare, asstd with other B-
flavin adenine complex def
dinucleotide

Vitamin B3 Nicotinamide – adenine Redox reaction Pellagra

(NIACIN/NICOTINAMIDE dinucleotide
Nicotinamide – adenine
dinucleotide phosphate

Vitamin B6 (PYRIDOXINE Pyridoxal phosphate Decarboxylations & Anemia

transanimation

Vitamin B5 Coenzyme A (CoA) Activated carbonyl emotional instability,

(PANTOTHENIC ACID) groups, acyl transferase burning sensation in
as acyl carrier in fatty acid extremities
metabolism

Vitamin B9 (FOLIC ACID Tetrahydrofolate H & C transfers Megaloblastic anemia,

OR FOLATE) birth defects

Vitamin B7 (BIOTIN) Biotin/Biocytin (prosthetic carboxylations Dermatitis, alopecia

group)

Vitamin B12 Methylcobalamin & Isomerization & methyl Megaloblastic anemia

(CYANOCOBALAMIN deoxyadenosylcobalamine group transfer
Conversion of
homocysteine to
methionine

Vitamin C (ASCORBIC Antioxidant, scurvy

ACID hydroxylation

Vitamin A (RETINOIC Cofactor for protein For cellular nightblindness

ACID) rhodopsin differentiation & vision

Vitamin D Functions as hormone ricketts & osteomalacia

(CHOLECALCIFEROL) more than a cofactor for
enzyme

Vitamin E (TOCOPHEROL) Mainly as antioxidant hemolysis of RBC

 For free radical trappings

Vitamin K Cofactor in enzyme- haemorrhage, bleeding

(PHYTOMENADIONE) catalyzed reaction that
carboxylate particular
glutamate residues in
proteins involved in
blood-clotting cascade

SIX (6) MAJOR CLASSES OF ENZYMES:

1. Oxidoreductases
Catalyze oxidation-reduction reactions.
Subclasses: dehydrogenases, oxidases, oxygenases, reductases, peroxidases and hydroxylases
2. Transferases
Catalyze reactions that involve the transfer of groups from one molecule to another.
E.g. Transcarboxylases, transmethylases, and transaminases
3. Hydrolases
Catalyze reactions in which the cleavage of bonds is accomplished by adding water.
E.g. Esterases, phosphatases, and peptidases
4. Lyases
Catalyze reactions in which groups are removed to form a double bond or added to a double bond.
E.g. Decarboxylases, hydratases, deaminases, and synthases
5. Isomerases
Catalyze several types of intramolecular rearrangements.
E.g. Epimerases, mutases
6. Ligases
Catalyze bond formation between 2 substrate molecules coupled by hydrolysis
Process often utilizes high-energy bonds such as ATP
ENZYME-SUBSTRATE COMPLEX
MOA OF ENZYME ACTION:
1. The active site contains Functional Groups (directly participate in reaction)
2. As substrate binds, it induces a conformational changes  2 models of substrate binding to enzyme.
Lock & Key Model
Induced Fit Model
3. The activated ES form a transition state complex.
4. The TSC decomposes the products which dissociates from enzyme.
5. Enzyme returns to original form, binds another substrate & repeats the process.
REACTION ORDER:
defined as the sum of the exponents on the concentration terms in the rate expression.
First order – if the rate depends on the first power of the concentration of a single reactant and suggests
that the rate limiting step is a unimolecular reaction.
• Rate=k[A]1
Second order – depends on the concentration of the two reactants.
• Rate=k[A]1[B]1
Zero order – when the addition of a reactant does not alter the reaction rate.
• Rate=k[A]0
MICHAELIS MENTEN KINETICS

• Vmax = maximum velocity that the reaction can attain

• Km= is referred as the Michaelis constant
• S= substrate concentration
• The lower the value of the Km the greater the affinity of the enzyme for ES complex formation
• Km is [S] at Vmax/2 (Km is the substrate concentration at which the enzyme has half maximal velocity.
ENZYME INHIBITION
• Inhibition may be reversible or irreversible
• Irreversible inhibitors
• usually bond covalently to the enzyme
• The structure is not similar to the enzyme’s normal structure.
 • Increasing the concentration of substrate does not reverse the inhibition process.
• Permanently, the enzyme is inactivated.
• Reversible inhibitors – inhibitor can dissociate from the enzyme because it binds through noncovalent
bonds.
• Competitive Inhibition
• The structure of the competitive inhibitor resembles that of the enzyme’s normal
substrate
• Binds reversibly to an enzyme active site and the inhibitor remains unchanged
• Forms EI complex will be equivalent to ES complex.
• Noncompetitive Inhibition
• A noncompetitive enzyme inhibitor decreases enzyme activity by binding to a site on an
enzyme other than the active site
• Inhibitor binding alters the enzyme’s 3D config. & blocks the reaction.
• Causes a change in the structure of the enzyme and prevents enzyme activity
• Increasing the concentration of substrate does not completely overcome inhibition
• Suicide inhibitor
• Inhibitor is unreactive until enzyme attempts to use it as a substrate.
• At that point, compound binds covalently to the active site & inhibits the enzyme by permanently
killing itself.

LIPIDS
• Lipins or lipoids
• Esters of long chain fatty acids and alcohols, or closely related derivatives.
• Polymers of fatty acids.
• Are insoluble in water but soluble in non-polar solvents or solvents of low polarity
• Has an operational definition rather than structural definition.
• Functions:
• Store energy within fat cells
• As membrane components
• Serve as chemical messengers
• Acts as hormones, antioxidant, pigments or vital growth factors and vitamins
•

FATTY ACIDS
Fatty Acids are monocarboxylic acids that contain hydrocarbon chains of variable lengths
monomers of Lipids

SATURATED UNSATURATED
Solid at room temp (higher melting point) Liquid at room temp (lower melting point)
C – C single bonds. one or more double bonds
Fatty acids that can be synthesized are called nonessential fatty acids. While fatty acids that must be obtained
from the diet are called as essential fatty acids.
Ex. of essential fatty acids: Linoleic (omega-6 from vegetable oils) and linolenic acids (omega-3 from fish oils)

DERIVATIVES OF FATTY ACIDS

1. TRIACYLGLYCEROL - Also known as Triglycerides; are esters of glycerol with three fatty acid molecules;
referred to as neutral fats; 9kcal
Triacylglcerol mixtures are referred to as fats or oils.
Storage of energy: A specialized type of cell called adipocytes, found in adipose tissues stores
triacylglycerols.
As insulator: Fats provide insulation @ low temperature. It is a poor conductors of heat. It prevents heat
loss
• Reactions indergone by TAGs: Rancidity (due to oxidation), Hydrogenation (removal of double bond),
Saponification (formation of soap with alkali either NaOH or KOH)
• Trans fatty acids- are formed during hydrogenation (from unsaturated to saturated) when cis
double bonds are converted to trans double bonds. In the body it behaves like saturated fatty
acids (recall that trans and saturated are unhealthier)
2. WAXES - Are esters of long-chain saturated and unsaturated fatty acids with long chain alcohols.
Their melting points are generally higher than those of triacylglycerols.
Important waxes: Lanolin (from lamb’s wool), Carnauba wax (from a brazilian palm tree),
Spermaceti (from whales), and Bees wax
3. PHOSPHOLIPIDS - Are structural components of membranes and are considered as amphipathic molecules
They are considered as emulsifying agents and surface active agents.
2 TYPES of phospholipids:
• Phosphoglycerides aka Glycerophospholipids - are molecules that contain glycerol, fatty acids,
phosphate and an alcohol. Are the most numerous phospholipid found in cell membranes.
• Sphingomyelins differ from phosphoglycerides in that they contain sphingosine instead of glycerol.
• It is also classified as sphingolipids.
4. SPHINGOLIPIDS - Are important components of animal and plant membranes.
Contains a long chain amino alcohol. In animals this alcohol is primarily sphingosine. While in plants the
alcohol is known as phytosphingosine.
The core of each type of sphingolipid is ceramide, a fatty acid amide derivative of sphingosine.
• Most important glycolipids:
• Cerebrosides – a sphingolipid in which the head group is a monosaccharide.
• E.g. Galactocerebrosides(found in cell membranesof the brain)
• Sulfatides – sulfated cerebroside
• Gangliosides – are sphingolipids that possess oligosaccharide groups with one or
more N-acetylneuraminic acid (Neu5Ac), a sialic acid (often simply called “sialic acid”)
5. EICOSANOIDS - Considered as a fatty acid derivative. Are also known as autocrine regulators; diverse
group of extremely powerful hormone like molecules produces in mammalian tissues. Most eicosanoids
are derived from arachidonic acid (arachidonic acid is synthesized from linoleic acid).
E.g.
a. Prostaglandins – Antiplatelet aggregation, vasodilation, inflammation, pain, fever
b. Thromboxane – platelet aggregation, vasoconstriction
c. Leukotriene – inflammation, bronchoconstriction, vasoconstriction
6. ISOPRENOIDS - vast biomolecule that contain repeating five carbon structural units known as isoprene
units. Isoprenoids are not synthesized from isoprene. Instead, their biosynthetic pathways all begin with
the formation of isopentenyl pyrophosphate from acetyl-CoA
 Isoprenoids consists of:
a. Terpenes
b. Steroids
7. TERPENES - Are enormous group of molecules that are found largely in the essential oils of plants. They
are classified according to the number of isoprene residues. Examples:
a. Monoterpenes (geranium, 2)
b. Sesquiterpenes (Farnesene, 3)
c. Diterpene (Phytol, 4)
d. Triterpenes (Olive oil, Squaline, Yeast, 6),
e. Tetraterpenes ( Carotenoids, 8).
8. STEROIDS- complex derivatives of triterpenes; found in all eukaryotes and a small number of bacteria.
Composed of four fused rings. They are distinguished by the placement of carbon-carbon double bond
and varoius substituents.
STEROID NUCLEUS: consists of 3 cyclohexane rings, 1 cyclopentane ring and has no fatty acids.
E.g. Cholesterol (Animals), Stigmasterol ( Plants), Ergosterol (Fungi)
9. Steroid hormones - are chemical messengers in cells; are produced from cholesterol. Include sex
hormones such as androgens (testosterone) in males and estrogens (estradiol) in females.
10. LIPOPROTEIN -Is any protein that is covalently linked to lipid groups. Plasma lipoproteins transport lipid
molecules through the blood stream from one organ to another.
Lipoproteins are classified according to their density E.g.:
a. Chylomicron - (<0.95 g/cm3) transport dietary triacylglycerols and cholesteryl esters from the
intestines to the tissues.
b. VLDL (0.95 – 1.006 g/cm3) synthesized in the liver, transport lipids to tissues from the liver
to the tissues.
c. LDL (1.006 – 1.063 g/cm3) converted from VLDL. Also known as “Bad cholesterol”
a. HDL (1.063 – 1.210 g/cm3) also produced in the liver, scavenging excessive cholesterol from cell
membranes and transports them back to the liver converting them to bile acids. “Good
cholesterol”
DISEASES-ASSOCIATED TO LIPIDS

Disease Symptom Accumulating Sphingolipid Enzyme deficiency

Tay-Sachs disease Blindness, muscle Ganglioside Gm2 B-Hexosaminidase A

weakness, seizures,
mental retardation
Gaucher’s Mental retardation, Glucocerebroside B-glucosidase
disease liver and spleen
enlargement,
erosion of long
bones
Krabbe’s disease Demyelination, Galactocerebroside B-galactosidase
mental retardation
Niemann Pick Mental retardation Sphingomyelin Sphingomyelinase
disease

NUCLEIC ACIDS
• Biomolecules that store and transmits genetic information in cells
• Were first found in the nuclei of cells.
• Function: storage and expression of genetic information.
• Types of nucleic acids:
 Deoxyribonucleic acid (DNA)
 Ribonucleic acid (RNA)
• Made up of nucleotides
NUCLEOTIDES
Nitrogeneous Bases Pentose Sugars Phosphate group
 Purine Deoxyribose

Ribose

Pyrimidine

NUCLEOSIDE: N bases plus sugar; lacks phosphate group

 Important Bonds:
 An ester bond forms between a phosphate group and a ribose group. This forms the back
bone of a strand.
 A glycosidic bond forms between a ribose group and a nitrogen base group.
 Phosphodiester bond forms between nucleotides to form nucleic acids.

Base Sugar Nucleotide Name

DNA Nucleotide deoxyribose deoxyadenosine 5’- dAMP
Adenine deoxyribose monophosphate dGMP
Guanine deoxyribose deoxyguanosine 5’– dCMP
Cytosine deoxyribose monophosphate dTMP
Thymine deoxycytosine 5’-
monophosphate
deoxythymine 5’-
monophosphate
RNA Nucleotide ribose adenosine 5’- AMP
Adenine ribose monophosphate GMP
Guanine ribose guanosine 5’- CMP
Cytosine ribose monophosphate UMP
Uracil cytidine 5’-
monophosphate
uridine 5’-
monophosphate

CLASSIFICATION OF NUCLEIC ACIDS BASED ON STRUCTURE

1. PRIMARY STRUCTURE: The primary structure of a nucleic acid is the nucleotide sequence
The nucleotides in nucleic acids are joined by phosphodiester bonds
The 3’-OH group of the sugar in one nucleotide forms an ester bond to the phosphate group on the 5’-
carbon of the sugar of the next nucleotide. (ANG DINRAWING NATIN SA BOARD)
2. SECONDARY STRUCTURE: DNA Double Helix – The Watson-Crick Model
In DNA there are two strands of nucleotides that wind together in a double helix
- the strands run in opposite directions; the bases are arranged in step-like pairs
- the base pairs are held together by hydrogen bonding (C and G, 3 H bonds; A and T, A and U, 2 H bonds)
The pairing of the bases from the two strands is very specific
The 2 strands of DNA are arranged antiparallel to one another: viewed from left to Right the left strands is
aligned 5’ to 3’,while the right strand is aligned 3’ to 5’
The complementary base pairs are A-T and G-C
- two hydrogen bonds form between A and T
 - three hydrogen bonds form between G and C
3. TERTIARY STRUCTURE: the complex folding of large chromosomes within eukaryotic chromatin and
bacterial nucleoids is generally considered tertiary structure
• Histone – is the primary protein component of the CHROMATIN
• Nucleosome – a nucleoprotein, formed when a DNA wraps into a histone
• Chromatin – repeating units of nucleosome.
STRUCTURAL FORMS OF DNA
 Two structural variants that have been well characterized in crystal structures are the A and Z
forms.
 The B-form is the most common; found under physiologic condition.
 The A-form is favored in many solutions that are relatively devoid of water.
 The Z-form is considerably slimmer than B-DNA, is left handed spiral.
CENTRAL DOGMA

The flow of information from DNA to RNA to protein.

DNA is the repository & directs its own replication; it is
transcribed into RNA; mRNA is translated into a polypeptide
gene product.

.
1. REPLICATION – DNA synthesis
o 2 strands of DNA double helix separates, 2 daughter molecules are produced (semiconservative
replication)
o As they separates, it forms a “v” formation where the active synthesis occurs – the replication
fork.
o Replication is bidirectional
o DNA helicase – unwinds the DNA double helix
o Topoisomerases – unwinds the supercoils.
o DNA polymerase works on 5’ 3’ direction only.
o Leading (5’  3’)& Lagging strands (3’  5’)
o Okazaki fragments – fragments of lagging strands
o DNA Ligase – joins lagging strand together
o  now DNA polymerase can work on this continuous strand.
2. TRANSCRIPTION
The genetic master plan of an organism is contained in the sequence of nucleotides of DNA. However, it is
through the RNA that the master plan is expressed.
The copying process, during which a DNA strand serves as a template, is called transcription. Protein
synthesis begins with transcription, the process whereby DNA produces mRNA.
Classes of RNA:
 rRNA – Ribosomal RNA are components of ribosomes, the complexes that carry out the
synthesis of proteins.
 mRNA – Messenger RNA are intermediaries, carrying genetic information from one or a few
genes to a ribosome.
 tRNA – Transfer RNA are adapter molecules that faithfully translate the information in mRNA
into a specific sequence of amino acids.
A. INITIATION - requires binding protein transcription factors & RNA polymerase to promoter sites at the
beginning of the gene; it makes a complementary RNA copy of the DNA template strand & recognize
the end of the sequence (terminal site)
B. ELONGATION - requires local unwinding of the DNA helix by RNA Polymerase followed by synthesis of
a 5’ 3’ RNA transcript coded for the DNA template read in the 3, 5’ direction
C. TERMINATION - requires a termination signal sequence that results in release of RNA polymerase &
new synthesized transcript from DNA
3. TRANSLATION - a process when mRNA carries coded information to ribosomes. The ribosomes "read" this
information and use it for protein synthesis.Translation occurs in the cell’s ribosomes, which contain
rRNA. The information necessary for translation travels from the cell nucleus to the ribosomes via
messenger RNA (mRNA). The mRNA binds to the smaller ribosomal body, and tRNA brings amino acids to
it.
tRNA has two important sites:
a. One is for the attachment of a specific amino acid
 b. the other is the recognition site, which contains an anticodon (a sequence of three bases that
match a codon on the mRNA).
THE GENETIC CODE
Codon – a three letter word, that contains the information necessary for the synthesis of proteins.
The 3 letters are composed of 3 consecutive ribonucluetide.
The 4 ribonucleotide can be formed into these three letter word in 64 ways.
START CODON: AUG
STOP CODONS: UAG, UAA, and UGA
MUTATION - An error in base sequence reproduced during DNA replication. Errors in genetic information is
passed on during transcription. The altered information can cause changes in amino acid sequence during protein
synthesis and thereby after protein function.
Silent mutation
 There is a change but the protein still codes for the same amino acid. There is no manifestation to
the individual
 E.g. UCA to UCU
Missense mutation
 A different codon is produced therefore it codes for a different amino acid
 E.g. UCA (serine) to CCA (proline)
Nonsense mutation
 A stop codon is produced thereby also stopping protein synthesis
 E.g. UCA to UAA (stop)
MUTAGENS
Mutations are caused by mutagens
A mutagen is a substance or agent that causes a change in the structure of a gene:
 Radiation and chemical agents are two important types of mutagens
 Ultraviolet, X rays, radioactivity and cosmic radiation are mutagenic cause of cancers
 Chemical agents can also have mutagenic effects
 E.g. HNO2 can convert to uracil
 Nitrates, nitrites, and nitrosamines – can form nitrous acid in cells
Under normal conditions mutations are repaired by repair enzymes
GENETIC DISORDERS: Disease caused by abnormalities in genes or in chromosomes
Either hereditary or results of Mutations
1. SINGLE GENE DISORDER -where genetic disorders are the result of a single mutated gene they can be
passed on to subsequent generations
a. Autosomal Dominant Disorders - only one mutated copy of the gene is needed for a person to be
affected. Each affected person usually has one affected parent. Ex. Neurofibromatosis.
b. Autosomal Recessive Disorders Two copies of the gene must be mutated for a person to be
affected. An affected person usually has unaffected parents who each carry a single copy of the
mutated gene (and are referred to as carriers). Ex. Sickled – cell anemia
c. X-Linked dominant Disorders - Caused by mutations in genes on the X chromosome. One copy of
the affected gene is needed. Males are more severely affected, it can be fatal so females have
them. Not fatal for males with XXY. Daughters are carriers. Ex. SCID/Bubble Boy disease.
d. X-Linked recessive Disorders - also caused by mutations in genes on the X chromosome. Two
copies of the affected gene is needed. Usually males are affected, It can be expressed in females if
two copies are present, females are just carriers. Ex. Hemophilia
e. Y-linked disorders - caused by mutations on the Y chromosome. Only males can get them, and all
of the sons of an affected father are affected. Since the Y chromosome is very small, Y-linked
disorders only cause infertility
2. MULTIFACTORIAL AND POLYGENIC DISORDERS
Effects of multiple genes + lifestyle + environment
Examples:
 Heart attacks, Diabetes, Hypertension. Obesity, Cancers