Proteins​ - macronutrients composed of Grams/da Grams/day

amino acids y for (acceptable %

- Essential nutrients found in average of calories
animal and plant foods body from protein)
- Originates from the Greek weight
(g/kg body
word ​proteios​ (​first quality​) weight)

0-6 mos. 9 g/day Not

(1.5 g/kg) determinable
[adequate
intake]

7-12 mos. 11 g/day Not

(1.5 g/kg) determinable
Dietary Protein as a Source of Energy
Cal/g = ​4 cal ​of “metabolizable energy” 1-3 years 13 g/day 10-50 g/day
= ​3.2 cal ​of “net metabolizable (1.1 g/kg) (5-20% of
1,000 cal)
energy”
4-8 years 19 g/day 30-100 g/day
Proteins in the Human Body (0.95 g/kg) (10-30% of
● Growth and maintenance ​(ex. 1,300 cal)
Collagen, Keratin, Elastin, Fibrin)
9-13 years 34 g/day 40-130 g/day
● Transportation ​(ex. Hemoglobin,
(0.95 g/kg) (10-30% of
Myoglobin) 1,700 cal)
● Enzyme ​(ex. Salivary Amylase)
● Fluid and electrolyte balance ​(ex. Boys 52 g/day 55-175 g/day
During inflammatory process by 14-18 (0.8 g/kg) (10-30% of
releasing reactive proteins) years 2,200 cal)
● Hormones ​aka chemical Girls 46 g/day 43-135 g/day
messengers (ex. Insulin, oxytocin, 14-18 (0.8 g/kg) (10-30% of
thyroxine or thyroid hormones) years 1,800 cal)
● Immunity ​(ex. immunoglobulins)
Men 19-50 56 g/day 55-190 g/day
years (0.8 g/kg) (10-35% of
Minimum Required Amount of Protein
2,200 cal)
Adults - proteins ≥ 35g/day to get enough
essential amino acids and nitrogen for the Women 46 g/day 45-160 g/day
synthesis of the body proteins, DNA and 19-50 (0.8 g/kg) (10-35% of
RNA (parts of chromosomes) years 1,800 cal)

Pregnant 71 g/day 60-210 g/day

RDA (Recommended Dietary Allowance) and (1.1 g/kg) (10-35% of
and AMDR (Acceptable Macronutrient Breastfeed 2,400 cal)
Distribution Range) for Protein ing women

AGE RDA AMDR Foods high in protein

● Meat and fish
 ● Cheese beans, gazpacho, pumpkin seeds, spinach,
● Eggs tofu)
● Beans Incomplete Protein ​- low in certain
● Bread essential amino acids
● Hummus
● Nuts and Seeds Protein Quality​ - ability of a particular
(Note: plant proteins are found to be protein to provide a balanced pattern of
associated with less health risk than animal indispensable amino acids.
protein but a direct relationship has not High-quality protein​ - contains high
been proven) concentrations of the indispensable amino
acids.
Protein Content and Protein Density of Low-quality protein​ - deficient or lacking in
Various Foods one or more of these amino acids

Amino Acids
Food Protei Energy Protein
n Conten Density
Conte t (g/1000kJ
nt (kJ/100 energy)
(g/100 g food)
g
food)

Baked 27 761 36
Salmon

Skim 3.6 150 24

Milk

Hard-boi 13 680 19
led
Eggs
● Monomer unit of protein
Green 5.1 290 18
Peas Amino Acid Abbreviation

Cheddar 25 1670 15 Amino acid Abbreviatio Single

Cheese n letter

Whole 3.5 270 13 Alaine Ala A

Milk
Arginine Arg R
Peanuts 26 2380 11
Asparagine Asn N
Walnuts 14.8 2720 5.4
Aspartic Asp D
acid
Complete Protein ​- contain all ​9 essential
amino acids ​(ex. Avocado, garbanzo Cysteine Cys C
 Classified based on polarity, electric charge,
Glutamic Glu E
acid hydrophobicity.
Polar=water soluble
Glycine Gly G Non-polar=water insoluble

Histidine His H
a. Electrically charged side chains
Leucine Ile I Negative Positive
Lysine Lys K Aspartic acid Arginine

Glutamic acid Histidine

Methionine Met M
Lysine
Phenylalani Phe F
ne
b. Polar uncharged side chains
Proline Pro P Serine
Serine Ser S Threonine
Threonine Thr T Asparagine
Tryptophan Trp W Glutamine
Tyrosine Tyr Y
c. Special cases
Valine Val V
Cystine
Pyrrolysine Pyl O
Glycine
Selenocyste Sec U
ine Proline

Aspartic Asx B
d. Hydrophobic side chains
Acid or
Asparagine Alanine
Glutamic Glx Z Valine
acid or
Glutamine Isoleucine

Any amino Xaa X Leucine

acid
Methionine
Leucine or Xle J
Isoleucine Phenylalanine

Termination TERM Tyrosine

codon
Tryptophan
Classification based on R-group hydrophobic interactions.
Nonpolar, Aliphatic amino acids:​ The R
groups in this class of amino acids are
nonpolar and hydrophobic. Glycine, Alanine,
Valine, leucine, Isoleucine, Methionine,
Proline.

Polar, Uncharged amino acids​: The R

groups of these amino acids are more
soluble in water, or more hydrophilic, than
those of the nonpolar amino acids, because
they contain functional groups that form
hydrogen bonds with water. This class of
amino acids includes serine, threonine,
cysteine, asparagine, and glutamine.

Acidic amino acids​: Amino acids in which

R-group is acidic or negatively charged.
Glutamic acid and Aspartic acid

Aromatic amino acids:​ Phenylalanine, Basic amino acids:​ Amino acids in which
tyrosine, and tryptophan, with their aromatic R-group is basic or positively charged.
side chains, are relatively nonpolar Lysine, Arginine, Histidine
(hydrophobic). All can participate in
 Conditionally
● Glutamine
-​ essential under conditions of
infection, inflammation, and
improper nutrition or stress
-poorly soluble, unstable for storage

● Tyrosine
-​ lowered formation of tyrosine in
chronic renal failure due to partial
inhibition of phenylalanine
hydroxylase
Hydrophobic amino acids
-essential in premature infants
As their classification suggests, the side
chains tend to be repelled from water, so
Classification of proteins
this impacts the positioning of these amino
I. Gross structure
acids in the protein tertiary structure.
- fibrous protein
- Largely insoluble in ordinary
Polar Amino acids
aqueous media
Polar amino acid residues are typically
- High molecular protein
found on the outside of a protein following
- Structure and support
polymerization due to the hydrophilic
- Fibers made up of long linear
properties of the side chain.
molecules arranged parallel to the
fiber axis (globular protein)
Aromatic
- Soluble in aqueous media
Falling within other classifications, possess
- Crystallized and definite molecular
aromatic side chains. All absorb ultraviolet
weight
light, tyrosine absorbing the most and
- Can be denatured
phenylalanine the least
- Ex: enzymes and hormones
Classifications of proteins
II. Solubilities
Essential Included in Non-essential ● Albumins - Soluble in water
(cannot be protein (can be - Coagulation upon heating
synthesized) synthesized) - Ex. leucosin from wheat
Threonine, Valine, Alanine, ● Globulins- Insoluble in water
Histidine, Leucine, Aspartic acid, - Soluble in dilute solutions
Tryptophan, Isoleucine Glycine, - Precipitation occurs when
Methionine, Asparagine, salt concentration is increased
Phenylalanin Serine, Proline, - Ex. Legumin from peas
e, Lysine Glutamic acid, ● Glutelins - Insoluble in neutral
Arginine,
Glutamine, solvents
Cysteine, - Soluble in dilute acids and
Tyrosine alkalis
- Ex. gluten from wheat
● Alcohol soluble proteins
○ Fibrous proteins - See above
○ Histones- Soluble in water
- Insoluble in ammonia
- Precipitated by
solutions of other
proteins
○ Protamins
III. Non-protein constituents
Simple Proteins - ​All of the proteins in (II)
Conjugated Proteins​ - substances made
up of proteins combined with some other
compound or compounds. These are the:
Nucleoproteins​ - combinations of proteins
with nucleic acid
- Ex. products obtained from glandular
tissue and from the germ of grain
Glycoproteins​ - combinations of proteins
with carbohydrates (such as hexoses,
hexosamines, and hexuronic acids)
- Ex. mucin from saliva; osseomucoid
from bone; tendomucoid from
tendon
Phosphoproteins​ - combinations of protein
with phosphorus containing substances
other than nucleic acid or lecithin
- Ex. casein from milk; vitellin from
egg yolk
Chromoproteins​ - combinations of protein
with various pigments
- Ex. hemoglobin from blood pigment;
ferritin from liver and spleen;
catalase, peroxidase, cytochrome C
(iron-containing enzymes);
hemocyanin (copper-protein
complex)
Lipoproteins​ - combinations of proteins
with lipids
- Occurs in cell nuclei, blood, egg
yolk, milk, serum, etc.
IV. State of degradation
Native proteins​ - proteins in the state in
which they exist in the intact cell
Derived proteins​ - products of protein
degradation, the first stop of which is
denaturation. These are:
Primary Protein Derivatives​ - products of
comparatively slight hydrolytic change in the
protein molecule. These are:
Proteans​ - insoluble products resulting
probably from the action (for a
comparatively short time) of hot water, dilute
acids or enzymes. Ex. myosan from myosin;
odestan from edestin.
Metaproteins (infraproteins)​ - products of
further action of acids and alkalis and are
insoluble in solutions of neutral salts, but
soluble in dilute acids. Ex. acid metaprotein
or acid albuminate and alkali metaprotein or
alkali albuminate.
Coagulated proteins​ - insoluble products
resulting either from the action of heat or
alcohol
Secondary Protein Derivatives​ - products
of a more extensive hydrolysis of the
protein. These are:
Proteoses​ - soluble in water; cannot be
coagulated on heating; precipitated by
staurating their solutions with (NH​4​)​2​SO​4
Peptones​ - soluble in water; not coagulated
on heating; not precipitated by saturating
their solutions with (NH​4​)​2​SO​4​; not
precipitated by certain alkaloidal reagents
such as phosphotungstic acid.
*Peptides combinations of two or more
amino acids, the carboxyl group of one
amino acid being joined to the amino
group of another.
V. Function
Structural​ - myosin of muscle
Storage​ - ferritin (in the liver) stores iron
Enzymes​ - pepsin fo the stomach
Hormones​ - insulin, vasopressin
Antibodies
Toxins
Special Purpose​ - hemoglobin to carry
molecular oxygen; rhopsodin in the visual
process.
VI. Nutritional Completeness
Complete​ - maintaining life providing for
normal growth when used as a sole protein
food. Ex. casein, lactalbumin from milk;
ovalbumin and evovitellin from egg; glycinin
from soybean; excelsin from Brazilian nut;
edestin, glutenin and maize glutenin from
grains.
Partially Incomplete​ - maintaining life but
not supporting normal growth. Ex. gliadin
from wheat; herdedin from barley; prolamin
from rye.
Incomplete​ - incapable of maintaining life
or supporting growth when fed as the sole
protein. Ex. zein of corn; gelatin.
Chemical Properties of Proteins
A protein has a constant solubility
regardless of the amount of substance
present in the solid phase. This property is a
sensitive test for the presence of protein
impurity.
Proteins are hydrolyzed by:
Acids​ - 20% HCl; 25% H​2​SO​4​,
dodecysulfonic acid, picric acid. The organic
acids are more effective than the mineral
acids in liberating the NH​3 from
​ its amides.
Hydrolysis is proportional to the hydrogen
ion activity of the acid solutions.
Alkalis​ - NaOH, KOH and Ba(OH)​2​ cause
very rapid and complete hydrolysis but they
bring about decomposition, especially the
deamination of certain amino acids.
Unfortunately, alkaline hydrolysis results in
the racemization of the amino acids so that
they are isolated to a large extent in the
optically inactive form.
Enzymes​ - pepsin hydrolyzes protein to
proteoses, peptones, and polypeptides only.
Trypsin and ereptic enzymes hydrolyze
protein to amino acids but the process is
slow and incomplete.
Proteins are precipitated by:
Acids​ - because of free amino acids.
- “Alkaloidal reagents”
- Inorganic: HNO​3​ and HClO​4
- Organic: trichloroacetic, molybdic,
phosphotungstic, picric and tannic
- Picric ​- used in treatments of burns
because of astringent effect on
tissues, diminishes secretion of
mucous membranes, and prevents
toxin absorption
- Tannic​ - used to relieve diarrhea
- Commercial use: leather by
precipitating collagen in hides
- Also used in ointments for burns
producing protective crust of protein
tannate over the delicate area
- Sulfosalicylic acid - detect proteins
quantitatively, and determine them in
urine and body fluids
- Heller’s - Reagent: HNO​3
- Result: white precipitate turning
yellow
- Robert’s - Reagent: HNO​3​, MgSO​4
Result: white precipitate
Salts of Heavy Metals​ - precipitation
occurs on the alkaline side of the isoelectric
point; metals unite = proteinates (ex. Hg-,
Ag-, Pb-, Cuproteinates)
- AgNO​3​ - used in cauteries;
precipitates proteins of tissues as
silver salts
 - Antidotes for metallic poisoning: egg
white, milk, and other liquid protein;
metallic precipitate must be removed
from the stomach using emetic or by
a stomach tube to prevent digestion
of the protein and the liberation,
re-solution, and absorption of
poisonous metal.
Neutral Salts​ - (NH​4​)​2​SO​4​, Na​2​SO​4​, and
NaCl - precipitate or “salt out” proteins;
precipitation may be due to dehydration of
molecular aggregates in solutions.
Alcohol​ - 2 effects:
A. If solution is dilute (aqueous),
alcohol reduces solubility of proteins
due to increase in electrical forces
between charged particles in
solution.
B. At high alcohol conc., protein
molecules are dehydrated, thus
causing precipitation.
Proteins form complexes with:
A. Nucleic acids to form nucleoproteins
B. Carbohydrates to form glycoproteins
C. Phosphorus - containing substances
other than nucleic acid or lecithin to
form phosphoproteins
D. Pigments to form chromoproteins
E. Lipids to form lipoproteins
F. Enzymes and coenzymes
Proteins untie with certain dyestuffs. Among
them are picric acid and flavianic acid.
When burned, proteins decompose and
liberate a characteristic odor of burned hair
or feather. Blackens = the presence of
carbon.
Color Reactions of Proteins
Biuret Test​ - Reagents: NaOH, CuSO​4
- Result: violet color due to a complex
in which Cu is coordinated with four
H+ atoms, at least 2 peptide
linkages is required to produce a
positive result.
- Indication: presence of a peptide
linkage or other closely related
group such as the or the
- Free amino acids ≠ the Biuret test
- Ammonium salts = deep blue
compound
- Single peptide linkage ≠ Biuret
reaction
Fractionation of Proteins
Proteins may be fractionated by:
1. Sedimentation in the ultracentrifuge
2. “Salting Out” (increasing conc. Of
salt)
3. Addition of solvents like alcohol
4. Dialysis
Formation of Peptide Bonds
Peptide bond - a covalent bond formed
between two amino acids
- is formed through a
dehydration reaction
Structure of Proteins
 ● Primary​ - sequence of a chain of
amino acids
- Ex. a hormone that stimulates the
thyroid to release thyroxine consists
of a tripeptide: Glu-His-Pro
● Secondary​ - describes the way the
amino acids next to or near each
other along the polypeptide are
arranged in space
- Types:
- Alpha helix ​(Alanine, Glutamic
acid, Cysteine, Glutamine,
Leucine, Histidine, Methionine,
Lysine)
- Beta-pleated sheet ​(Valine, Proline,
Serine, Arginine, Aspartic acid,
Asparagine)
- Triple helix

Tertiary​ - a folding of a protein into a Quaternary​ - combination of two or more

compact 3D shape stabilized by interaction protein subunits to form a larger biologically
between side R groups of amino acids active protein.
- Cross links
Protein hydrolysis
Protein Denaturation
Denaturation​ - change in the chemical,
physical, and biological properties of a
protein from those of the native state,
characterized by an unfolding of the
molecule from its previous configuration.
- Occurs when there is a disruption of
any of the bonds that stabilize the
secondary, tertiary or quaternary
structure.
- Covalent amide bonds of the primary
structure are not affected
Kinds
● Unfolding of the peptide chains, ex.
Action of urea on albumin
● Dissociation of the protein into
smaller units, which may or may not
unfold, ex. Action of urea on the
tobacco mosaic virus molecule.
Denaturing Agents:
Physical Agents
A. Heat​ - by breaking apart hydrogen bonds
and the hydrophobic attractions between
nonpolar side groups
- Ex. cooking, disinfection
- water is necessary for denaturation
and coagulation by heat.
- The steps in heat coagulation are:
1. Denaturation
2. Flocculation
3. Coagulation
B. Light​ - clouding of the lens of the eye in
old-age cataract is probably due to
denaturing of the globulins present in the
lens. Glass workers are particularly subject
to cataract presumably as a result of the
infrared rays emanating from the molten
glass. Change of fibrogen to fibrin in blood
clotting may be partly due to light.
C. Surface action
D. High pressure
E. Mechanical agitation
Chemical Agents
Organic solvents ​ - by forming their own
hydrogen bonds with a protein and
disrupting the hydrophobic interactions
- Ex. Alcohol, acetone, ether
A. Acids and alkalies (bases) ​ - affect the
hydrogen bonding between R groups and
disrupts the ionic bonds (salt bridges)
- Ex. lactic acid in the preparation of
yogurt and cheese, tannic acid in
burnt ointment
B. Salts of heavy metals ​ - form ionic
bonds or react with the disulfide bonds
(-S-S-); the denatured protein solidifies
- Ex. Ag+, Pb​2+​, Hg​2+
C. Enzymes
D. Detergents
E. Urea and guanidine
F. Agitation​ - stretches the polypeptide
chains until the stabilizing interactions are
disrupted
- Ex. whipping of cream, beating of
egg whites
Alteration of properties due to
denaturation
1. Physical
a. Increase in the viscosity of the
solution
b. Increase in rate of diffusion
c. Cannot be crystallized
d. Decrease in solubility
1. Chemical​ - some groups in the
denatured protein molecules become
exposed and readily detectable. Ex.
sulhydryl (SH-), disulfide (​ —S—S—​), and
the phenolic group
2. Biological
a. Increased digestibility by proteolytic
enzyme has been found in certain
denatured proteins
b. Enzymatic or hormonal activity is
usually destroyed
c. Modification of the specific
immunological properties
Detection and determination of Proteins
1. Heat coagulation​ - albumin is often
detected in urine by the appearance of a
coagulum on heating. The addition of acetic
acid to the heated sample will intensify the
protein precipitate.
- Used sometimes for the gravimetric
determination of proteins
2. Precipitating Agents ​- In Heller’s Ring
Test, protein in urine is detected by layering
urine over conc. HNO​3​ and observing the
ring of acid-denatured protein which
appears at the interface of the two liquids.
3. Specific Gravity​ - The specific gravity of
plasma or serum is dependent on its protein
content. A method for the determination of
plasma proteins involves the timing of the
rate at which a drop of plasma falls through
a column of organic solvents of a density
slightly less than that of plasma.
4. Refractive Index​ - index of refraction of
protein solutions is greater than that of
water by an amount which is proportional to
the concentration of protein. Serum has
been analyzed in this method.
Biological significance of proteins
1. Providing the structural framework of
tissues, membranes, and cell walls
2. Maintaining osmotic integrity
3. Storage of some particular element
(ex. Iron in ferritin)
4. Enzymes, to catalyze biological
reactions
5. Hormones, to regulate metabolic
processes (ex. insulin)
6. Carriage of molecular oxygen (ex.
hemoglobin)
7. Transportation of lipids (ex.
lipoproteins)
8. Taking part in antibody formation
9. Acting to a certain extent as buffers
in biological processes
Factors which influence the biological
value of proteins
1. Amounts and relative proportions of
their constituent amino acids
2. Nutritional availability (due to
liberation and absorption) of their
constituent amino acids under
conditions of digestion in the
gastrointestinal tract
3. Methods of processing or
preparation of foodstuffs
Enzymes​ - are proteins that increase the
rate of reaction by lowering the energy of
activation.
- Catalyze nearly all the chemical
reactions taking place in the cells of
the body
- Mediators of metabolism
- Usually ends in ​-ase ​(i.e. sucrase,
lactase, maltase)
- Have unique 3D shapes that fit the
shapes of the reactants
(​substrates​)

Names and Classification
- Describes function in enzyme (i.e.,
oxidase - catalyzes oxidation,
hydrolase - catalyzes hydrolysis)
- Common names of digestion
enzymes still use ​-in​ (e.g. pepsin,
trypsin)
How do enzymes work
- Weakening of bonds lowers
activation energy
Enzyme Catalyzed Reaction
- The proper alignment of a substrate
within the active site forms an
enzyme-substrate (ES) complex.
- The combination of enzyme and
substrate provides an alternative
pathway for the reaction that has a
lower activation energy
- E + S ⇋ ES → E + P
- E + S ⇋ ES - Substrate Binding
- ES → E + P - Catalytic Step
Factors Affecting Enzyme Activity
● Environmental conditions
● Enzyme and Substrate
Concentration
- Increasing the enzyme concentration
when the substrate concentration
remains constant increases the rate
of the catalyzed reaction.
- Constant enzyme concentration: ↑
substrate concentration = the rate
the reaction, as long as enzyme
molecules > substrate molecules
 ● Cofactors - ​Inorganic substances
- Metal Ions - bonded to one or
more amino acid side chains

● Irreversible Inhibition - ​A molecule

● Coenzymes - ​Organic
- Ex: Presence of Iron in the
quaternary structure- hemoglobin to
pick up oxygen
causes an enzyme to lose all
enzymatic activity.
- Antibiotics produced by bacteria -
used to inhibit bacterial growth (ex.
Penicilin)

Enzyme Inhibitors
Reversible Competitive inhibition
- Resemble a normal substrate
- Competes with it for the active site
Types of Enzyme Specificity
Enzymes may recognize and catalyze:
- A single substrate
- A group of similar substrates
- A particular type of bond

Reversible Non-competitive inhibition​ -

Do not enter the activation site
- Bind to another part of the enzyme
- Changes the shape of the enzyme,
altering the activation site
Lock-And-Key Model​ - substrate and Insulin​ - synthesized as inactive proinsulin
enzyme active site have complementary - Proinsulin = 2 chains are connected
shapes by a polypeptide of 33 amino acids

Digestive Enzymes​ - produced as inactive

forms and stored at the pancreas
Allosteric Enzymes
- Positive Regulator​ - causes
change in shape of active site →
substrate bind = speeds up reaction
- Negative Regulator​ - prevent
proper binding of substrate = slows
down rate of reaction

Induced Fit Model​ - active site changes

shape to bind substrate(s) more effectively.

Factors Affecting Regulation of Enzyme

Activity

Zymogens​ - are inactive

precursors
- Are called
Proenzymes
- Activated by removal of
peptide sections from
proteins
Vitamins
• Organic molecules that are essential for
normal health and growth. They must be
obtained from diet because they are not
synthesized in the body.
• Vitamins can be classified into two groups:
Water-soluble and Fat-soluble.
WATER-SOLUBLE
• Vitamins that have polar groups which
make them soluble in aqueous
environments.
• ​Thiamin (Vitamin B1)​ was the first
B vitamin to be identified.
• The TPP (thiamine
pyrophosphate) coenzyme is
involved in the decarboxylation
reactions of α – keto carboxylic acids
and reactions that cleave bonds to
carbonyl carbons of α –
hydroxyketones.
• Dietary sources: liver, yeast, whole
grain bread, cereals, and milk
• A deficiency of thiamin may result
in beriberi, which is characterized by
poor appetite, fatigue, weight loss,
nerve degeneration, and heart
failure.
• ​Riboflavin (Vitamin B2)
• It is used to make the coenzymes flavin
adenine dinucleotide (FAD) and flavin
mononucleotide (FMN).
• Riboflavin is needed for good vision and
healthy skin and hair.
• Dietary sources: beef liver, chicken, eggs,
green leafy vegetables, dairy foods,
peanuts, and whole grains
• A deficiency of riboflavin includes
dermatitis, dry skin, tongue inflammation,
and cataracts.
• ​Niacin (Vitamin B3)
• It is a component of the enzymes
nicotinamide adenine dinucleotide and its
phosphate form.
• These coenzymes participate in
oxidation-reduction, energy-production
reactions in carbohydrates, fat, and protein
metabolism.
• Dietary sources: brewer’s yeast, chicken,
beef, fish, liver, brown rice, and whole
grains
• A deficiency of niacin can result in pellagra
characterized by dermatitis, muscle fatigue,
loss of appetite, diarrhea.
• ​Pantothenic Acid (Vitamin B5)
• It is a part of a complex coenzyme known
as Coenzyme A. Coenzyme A transfers a
two-carbon acetyl group from pyruvate to
the citric acid cycle for energy production.
• Dietary sources: beef, liver, salmon, eggs,
brewer’s yeast, whole grains, and
vegetables.
• A deficiency of pantothenic acid is
characterized by fatigue, retarded growth,
muscle cramps, and anemia.
• Pyridoxine (Vitamin B6)
• Pyridoxine and an aldehyde, Pyridoxal, are
forms of Vitamin B6 that are converted to
the coenzymes pyridoxal phosphate (PLP).
• These PLP coenzymes participate in
many enzyme catalyzed reactions such as
transaminations of amino acids and
decarboxylations.
• Dietary sources: meat, liver, fish, nuts,
whole grains, and spinach
• Deficiency of pyridoxine may lead to
dermatitis, fatigue, anemia, and retarded
growth.
Cobalamin (Vitamin B12)
• It is a coenzyme consisting of four pyrrole
rings with a cobalt ion in the center. In its
coenzyme form, it participates in the
transfer of methyl groups, molecular
rearrangements, the formation of red blood
cells, and synthesis of acetylcholine for
nerve cells.
• Dietary sources: liver, beef, kidney,
chicken, fish: salmon, halibut, and tuna,
yogurt, and milk
• Deficiency of Cobalamin is found in
pernicious anemia and results in malformed
RBCs, nerve damage, and some mental
disorders.
• Cobalamin is not present in plants, strict
vegetarians can experience symptoms of
pernicious anemia.
• ​Ascorbic Acid (Vitamin C)
• Its major function in the cells is its role in
the synthesis of hydroxyproline and
hydroxylysine, which are needed to form
collagen.
• Dietary sources: blueberries, oranges,
strawberries, cantaloupe, tomatoes, red and
green peppers, broccoli, and cabbage
• A deficiency can lead to scurvy
characterized by bleeding gums, weakened
connective tissue, slow-healing wounds,
and anemia.
that transfer single-carbon groups and
synthesize purines and pyrimidine to make
DNA and RNA.
• Dietary sources: green leafy vegetables,
beans, meat, seafood, yeast, asparagus,
and whole grain products.
• A deficiency of Folate can lead to
abnormal red blood cells ,anemia,
intestinal-tract disturbances, loss of hair,
growth impairment, depression, and spina
bifida when there is deficiency of folic acid

• Biotin
• It is a coenzyme for enzymes that transfer
a carboxyl group in the reaction of pyruvate
to oxaloacetate or acetyl-CoA to
malonyl-CoA, which occurs in the synthesis
of fatty acids.
• Dietary sources: liver, yeast, eggs, and
nuts
• Deficiency of biotin can lead to dermatitis,
loss of hair, fatigue, anemia, nausea, and
depression.
FAT-SOLUBLE
• Vitamins that are nonpolar compounds
soluble in lipid components of the body,
such as fat deposits and cell membranes.
• Vitamin A
• It consists of three different forms
depending on the oxidation of the functional
group: Retinol (alcohol), Retinal (aldehyde),
and Retinoic Acid (carboxylic acid). It is
•​ Folic Acid (Folate)
involved in the synthesis of RNA and
• It is composed of a pyrimidine ring,
glycoproteins.
p-aminobenzoic acid (PABA), and
• The retinol in the retinas of the eyes plays
glutamate.
a role in vision.
• In the cells, an enzyme called
• Dietary sources: yellow and green fruits
dihydrofolate reductase adds H atoms to the
and vegetables
atoms in the heterocyclic ring of folate to
• A deficiency of Vitamin A can cause night
yield the coenzyme tetrahydrofolate (THF).
blindness, depression of immune response
This THF coenzyme is used in reactions
and inhibition of growth.
• Vitamin D
• The most prevalent form is the Vitamin D3
or cholecalciferol. It is not a vitamin because
it is not required in the diet. Its function in
the body is to regulate the absorption of
phosphorus and calcium during bone
growth.
• Dietary sources: sunlight, cod liver oil, egg
yolk, and milk with Vitamin D.
• A deficiency in Vitamin D can result in
weak bone structure, rickets in children, and
osteomalacia in adults.
• Vitamin K
• Vitamin K, or Phylloquinone (in plants),
has a large saturated side chain. Vitamin
K2, or Menaquinone (in animals), has a very
long unsaturated side chain. Vitamin K2
takes part in synthesizing zymogens for
blood clotting.
• Dietary sources: liver, spinach, and
cauliflower
• Vitamin K deficiency can lead to bleeding
from minor cuts, delayed clotting times, and
bruising.

Vitamins and Function

• Vitamin E
• Vitamin E, or Tocopherol, has a major role
Water Coenzyme Function
in cells as an antioxidant but not much is soluble
known. It protects the cells in the body by vitamins
removing damaging chemicals and by
preventing the oxidation of unsaturated fatty Thiamine Thiamine Decarboxylation
acids. (B1) Pyrophoshate
• It has been used to reduce the damage to Riboflavin Flavin Adenine Electron transfer
the retinas that can be caused by high (B2) Dinucleotide
oxygen levels. • Dietary sources: meat, (FAD); Flavin
whole grains, vegetable oils, and vegetable Mononucleotide
• Vitamin E deficiency can cause hemolysis (FMN)
of RBCs and anemia.
Niacin Nicotinamide Oxidation-reduct
(B3) Adenine ion
 Dinucleotide prothrombin for
(NAD+); blood clotting
Nicotinamide
Adenine
Dinucleotide Digestion and Metabolism
Phosphate Gastrointestinal Tract
(NADP+) • Mouth
When you swallow, your tongue pushes the
Pantothe Coenzyme A Acetyl group food into your throat. A small flap of tissue,
nic Acid transfer called the epiglottis, folds over your
(B5)
windpipe to prevent choking and the food
Pyridoxin Pyridoxal Transamination passes into your esophagus.
e (B6) Phosphate
• Esophagus
Cobalami Methylcobalamin Methyl group Once you begin swallowing, the process
n (B12) transfer
becomes automatic. Your brain signals the
Ascorbic Vitamin C Collagen muscles of the esophagus and peristalsis
Acid synthesis, begins.
healing of
wounds • Lower Esophageal Sphincter
When food reaches the end of your
Biotin Biocytin Carboxylation
esophagus, a ringlike muscle—called the
Folic Acid Tetrhydrofolate Methyl Group lower esophageal sphincter —relaxes and
Transfer lets food pass into your stomach.

• Stomach
After food enters your stomach, the
Fat soluble vitamins Function
stomach muscles mix the food and liquid
A Formation of visual with digestive juices. The stomach slowly
pigments, empties its contents, called chyme, into your
development of small intestine.
epithelial cells
• Small Intestine
D Absorption of
calcium and The muscles of the small intestine mix food
phosphate, with digestive juices from the pancreas,
deposition of liver, and intestine, and push the mixture
calcium and forward for further digestion.
phosphate in bone
• Large Intestine
E Antioxidant,
Waste products from the digestive process
prevents oxidation
of Vitamin A and include undigested parts of food, fluid, and
unsaturated fatty older cells from the lining of your GI tract.
acids Peristalsis helps move the stool into your
rectum.
K Synthesis of • Rectum
The lower end of your large intestine, the
rectum, stores stool until it pushes stool out
of your anus during a bowel movement.
Metabolism - the sum total of all chemical
reactions involved in maintaining the living
state of an organism.
- divided into two categories:
- ANABOLISM or CATABOLISM
- METABOLIC PATHWAYS
Bioenergetics - describes the biochemical or
metabolic pathways by which the cell
ultimately obtains energy.
Carbohydrate Metabolism
Carbohydrate Digestion - complex sugars
are called polysaccharides, which serve as
energy storage and as structural
components.
- carbohydrates are broken down into
simple sugars that can be transported
throughout the body.
- digestion begins in the mouth and ends
with monosaccharides being absorbed
across the epithelium of the small intestine.
Then, cellular respiration begins.
- GLYCOLYSIS
- a process where the
monosaccharide glucose is oxidized,
releasing the energy stored in its
bonds to produce ATP.
- cells take up the circulating glucose
and, through glycolysis, transfer
some of the energy in glucose to
ADP to form ATP. - the last step in
glycolysis produces the product
pyruvate.
- the two phosphate groups are then
transferred to two ADPs to form two
ATPs. Thus, glycolysis uses two
ATPs but generates four ATPs,
yielding a net gain of two ATPs and
two molecules of pyruvate. - in the
presence of oxygen, pyruvate
continues on to the Krebs cycle.
Energy Requiring Phase
Step 1. A phosphate group is transferred
from ATP to glucose, making glucose-6-
phosphate.
Step 2. Glucose-6-phosphate is converted
into its isomer, fructose-6-phosphate
Step 3. A phosphate group is transferred
from ATP to fructose-6- phosphate,
producing fructose-1,6- bisphosphate.
Step 4. Fructose-1,6-bisphosphate splits to
form two three-carbon sugars:
dihydroxyacetone phosphate (DHAP) and
glyceraldehyde-3- phosphate.
Step 5. DHAP is converted into
glyceraldehyde-3-phosphate.
Energy-Releasing Phase
Step 6. Two half reactions occur
simultaneously:
1) Glyceraldehyde-3-phosphate (one of the
three-carbon sugars formed in the initial
phase) is oxidized,
2) NAD+ is reduced to NADH + H+. The
overall reaction is exergonic, releasing
energy that is then used to phosphorylate
the molecule, forming
1,3-bisphosphoglycerate.
Step 7. 1,3-bisphosphoglycerate donates
one of its phosphate groups to ADP making
a molecule of ATP and turning into
3-phosphoglycerate in the process.
Step 8. 3-phosphoglycerate is converted
into its isomer, 2- phosphoglycerate.
Step 9. 2-phosphoglycerate loses a
molecule of water, becoming
phosphoenolpyruvate (PEP)
Step 10. PEP readily donates its phosphate
group to ADP making a second molecule of
ATP. As it loses its phosphate, PEP is
converted to pyruvate, the end product of
glycolysis.
 - KREBS CYCLE
- the pyruvate generated during
glycolysis are transported across the
mitochondrial membrane into the
inner mitochondrial matrix, where
they are metabolized by enzymes in
the Krebs Cycle.
- during the Krebs Cycle,
high-energy molecules, including
ATP, NADH, and FADH2, are
created. NADH and FADH2 then
pass electrons through the electron
transport chain in the mitochondria
to generate more ATP molecules.
PART 1: Decarboxylation Removes Two
Carbon Atoms
Reaction 1: Formation of Citrate
• To start the Krebs cycle, citrate synthase
combines acetyl CoA and oxaloacetate to
form a six-carbon citrate molecule; CoA is
subsequently released and can combine
with another pyruvate molecule to begin the
cycle again.
Reaction 2: Isomerization to isocitrate
• The aconitase enzyme converts citrate into
isocitrate.
Reaction 3: First Oxidative Decarboxylation
Isocitrate dehydrogenase converts isocitrate
into the five-carbon α-ketoglutarate,
Reaction 4 : Second Oxidative
ANAEROBIC RESPIRATION
Decarboxylation • A second CO2 is
- when oxygen is limited or absent, pyruvate
removed as α-ketoglutarate undergoes
enters an anaerobic pathway. In these
oxidative decarboxylation. The resulting 4-C
reactions, pyruvate can be converted into
group combines with coenzyme A to form
lactic acid.
succinyl CoA.
• PART 2:
AEROBIC RESPIRATION
Reaction 5: Hydrolysis of Succinyl CoA
- in the presence of oxygen, pyruvate can
• The enzyme succinyl CoA dehydrogenase
enter the Krebs cycle where additional
then converts succinyl CoA into succinate
energy is extracted as electrons are
and forms the high-energy molecule GTP,
transferred from the pyruvate to the
which transfers its energy to ADP to
receptors NAD+, GDP, and FAD, with
produce ATP.
carbon dioxide being a “waste product”
Reaction 6: Dehydration of Succinate
• Succinate dehydrogenase then converts
succinate to fumarate, forming a molecule
of FADH2.
Reaction 7: Hydration
• Fumarase then converts fumarate into
malate. Water adds to the double bond of
fumarate to yield malate.
Reaction 8: Dehydration forms oxaloacetate
• Malate in the presence of malate
dehydrogenase is converted back into
oxaloacetate while reducing NAD+ to
NADH.
• Oxaloacetate is then ready to combine
with the next acetyl CoA to start the Krebs
cycle again.
SUMMARY OF PRODUCTS :
• For each turn of the cycle, three NADH,
one ATP (through GTP), and one FADH2
are created. Each carbon of pyruvate is
converted into CO2, which is released as a
byproduct of oxidative (aerobic) respiration.
Electron Transport Chain
- uses the NADH and FADH2 produced by
the Krebs cycle to generate ATP.
- consists of a series of four enzyme
complexes (Complex I – Complex IV) and
two coenzymes (ubiquinone and
Cytochrome c), which act as electron
carriers and proton pumps.
- The electrons released from NADH and
FADH2 are passed along the chain by each
of the carriers, which are reduced when
they receive the electron and oxidized when
passing it onto the next carrier. Each of
these reactions releases a small amount of
energy, which is used to pump H+ ions
across the inner membrane.
- The accumulation of these protons in the
space between the membranes creates a
proton gradient with respect to the
mitochondrial matrix. Also embedded in the
inner mitochondrial membrane is an
amazing protein pore complex called ATP
synthase.
- Effectively, it is a turbine that is powered
by the flow of H+ ions across the inner
membrane down a gradient and into the
mitochondrial matrix. As the H+ ions
traverse the complex, the shaft of the
complex rotates. This rotation enables other
portions of ATP synthase to encourage ADP
and P​i to
​ create ATP.
In accounting for the total number of ATP
produced per glucose molecule through
aerobic respiration, it is important to
remember the following points: A net of two
ATP are produced through glycolysis (four
produced and two consumed during the
energy-consuming stage).
However, these two ATP are used for
transporting the NADH produced during
glycolysis from the cytoplasm into the
mitochondria. Therefore, the net production
of ATP during glycolysis is zero.
Oxidative Phosphorylation
- with the presence of oxygen, energy is
passed through the electron carriers to
collect gradually the energy needed to
attach a phosphate to ADP and produce
ATP. - without oxygen, electron flow through
the ETC ceases.

NOTE: In all phases after glycolysis, the

number of ATP, NADH, and FADH2
produced must be multiplied by two to
reflect how each glucose molecule
produces two pyruvate molecules.

Electron Transport Chain

In the ETC, about three ATP are produced
for every oxidized NADH. However, only
about two ATP are produced for every
oxidized FADH2 . The electrons from
FADH2 produce less ATP, because they
start at a lower point in the ETC (Complex
II) compared to the electrons from NADH
(Complex I)
Therefore, for every glucose molecule that
enters aerobic respiration, a net total of 36
ATPs are produced
 4. INTRAMOLECULAR
Amino acid and Protein Metabolism

Proteins - contain a long chain of amino 2. Transamination - amino groups are

acids. removed from amino acids and transferred
- important tissue builders in the body which to acceptor keto-acids.
help in the cell structure, functions,
hemoglobin formation to carry oxygen,
enzyme for metabolic reaction and other
functions in the body. Also in supply the
nitrogen for the DNA and RNA genetic
materials and the energy production.

Protein Metabolism - the process to

breakdown food used by the body to gain
energy. - some of the protein will be
converted into glucose through
gluconeogenesis
1. Deamination - elimination of amino group
from amino acid with ammonia formation.
1. OXIDATIVE

3. Decarboxylation - reduction of carbon.

2. REDUCTIVE
3. HYDROLYTIC
Lipid Metabolism

Lipids - are broken down and utilized

through β-oxidation
- represent a potent energy and carbon
source Lipid Metabolism - involves
degradation of fatty acids.
- Organic Acid Metabolism introduces the β-oxidation Pathway: Fatty Acids
concept of lipid metabolism by describing
the process of fatty acid metabolism through
β-oxidation.

β-oxidation - metabolic process by which

fatty acids and their lipidic derivatives are
broken down.
1. Activation
2. Oxidation
3. Hydration
4. Oxidation
5. Cleavage
- this cycle repeats until the fatty acid has
been completely reduced to acetyl-CoA,
which is fed through the Krebs Cycle to
yield cellular energy in the form of ATP.
 SAMPLE PROBLEM
Using the 7.3 kcal/mole for ATP , how many
Metabolic Substrate(s) Products ATP
Pathway Oxidized kcal are conserved as ATP from one mole
of glucose in each of the following?
Glycolysis 1 Glucose 2 Pyruvate, 6 a. Glycolysis
2ATP, 2 ATP 6 x 7.3
NADH

Oxidation 2 Pyruvate 2 Acteyl 6 b. Oxidation of pyruvate to acetyl CoA

CoA, ATP 6 x 7.3
2NADH,
2CO​2 c. Citric Acid cycle
24 x 7.3
Citric Acid 2 Acetyl 6NADH, 2 24
Cycle CoA FADH2 , 2 ATP
ATP, 4CO​2 d. Complete oxidation of glucose to CO​2
and H​2​O
Complete Glucose + 6 CO​2​ + 36 36 x 7.3
Oxidation 6O​2 6H​2​O + 36 ATP
ATP ATP AND FATTY ACID OXIDATION

HEALTH NOTE: EFFICIENCY OF

FATTY NUMBER OF Beta-Oxi
ENERGY PRODUCTION ACID ACETYL COA dation
• Energy of the hydrolysis of ATP: Cycles
• 7.3 kcal/ mole for 1 ATP = 687 kcal for 36
moles ATP Myristic 7 acetyl CoA 6
• Cells – about 38% efficient in converting Acid (C14)
the total available chemical energy in Palmitic 8 acetyl CoA 7
glucose to ATP Acid (C16)
• 38% of 687kcal = 263 kcal –stored as ATP
in cells Stearic Acid 9 acetyl CoA 8
• 687 kcal -263 kcal = 424 kcal – lost as (C18)
heat
ATP Production for Myristic ATP
ENERGY YIELD FROM GLUCOSE Acid
GLUCOSE(C​6​H​12​O​6​)
36 moles ATP Activation - 2ATP
1 mole glucose
7 Acetyl CoA 7acetyl CoA x 84 ATP
12ATP/acetyl CoA
Molar Mass = 180g/mole
1 mole glucose 6 Beta-oxidation cycles 12 ATP
180 g glucose 6 FADH​2​ x 2ATP/FADH​2

36 moles ATP ÷ 180 g glucose 6 NADH x 3ATP/NADH 18

= 0.20 mole ATP per g of glucose TOTAL 112 ATP
ENERGY YIELD FROM FATS
MYRISTIC ACID (C​14​H​28​O​2​ )
112 moles ATP
1 mole myristic acid

Molar Mass = 228g/mole

1 mole myristic acid
228 g/mole

112 moles ATP ÷ 228 g/mole

= 0.49 mole ATP per g of myristic acid

SAMPLE PROBLEM
How much ATP will be produced from the
Beta Oxidation of palmitic acid, a C 16
saturated fatty acid (C​16​H​32​O​2​ )?

ATP Production for Palmitic Acid(C​16​H​32​O​2​ )

ATP Activation - 2 ATP
8 Acetyl CoA
8 acetyl CoA x 12 ATP/acetyl CoA = 96 ATP
7 Beta-oxidation cycles
7 FADH2 x 2 ATP/FADH2 = 14 ATP
7 NADH x 3 ATP/NADH = 21 ATP
TOTAL = 129 ATP