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P HI NMA- CAGAYAN DE ORO COLLEGE
COLLEGE OF ALLIED HEALTH AND S CI ENCES

AH-MEAN-OH-
ACID
PRESENTED BY GROUP 1
 AT THE END OF THE
LEARNING LESSON, WE WILL BE
ABLE
• Define TO:
amino acid and understand the
TARGETS: structure of amino acids (building
blocks of proteins)
• Give 20 common, naturally occuring
Amino Acids.
• Understand how amino acids are linked
together.
• Know the Roles and Fuctions as well as
the sources of amino acids
BACKGROUND

AMINO ACID
AMINO ACIDS
• They are molecules containing an amine
group, a carboxylic acid group, and a side-
chain that is specific to each amino acid.

• The key element of amino acid are carbon,

hydrogen, oxygen, and nitrogen.

• Amino acids are the basic structural building

units of protein and other biomolecules; they
are also utilized as an energy source.
 • Amino acids are concentrated
in protein-rich foods such as
SOURCE meat, fish, and soybeans.
OF
• Some people also take certain
AMINO amino acids in supplement form
ACID as a natural way to boost
athletic performance or improve
mood.
Roles and Functions
• Amino acids build muscles, cause
chemical reactions in the body, transport
nutrients, prevent illness, and carry out
other functions.

• Amino acid deficiency can result in

decreased immunity, digestive problems,
depression, fertility issues, lower mental
alertness, slowed growth in children, and
many other health issues.
20 AMINO ACIDS

9 ESSE NT IAL 11 NON-ESSENTIAL 8 CONDITIONAL

AMINO AC IDS AMINO ACIDS AMINO ACIDS
• They’re involved in many • Are those that can be • Are nonessential amino
processes, including synthesized by the body acids that become
tissue growth, energy and are different from essential in certain
production, immune essential amino acids that circumstances, such as
function, and nutrient are obtained from food. illness or pregnancy.
absorption.
9 ESSENTIAL AMINO ACIDS

PHENYLALANINE THREONINE
•It plays an integral role in the structure and •It also plays a role in fat metabolism and
function of proteins and enzymes and the immune function
production of other amino acids

VALINE METHIONINE
•It helps stimulate muscle growth and •This amino acid plays an important role in
regeneration and is involved in energy metabolism and detoxification.
production

TRYPTOPHAN LEUCINE
•Often associated with drowsiness, tryptophan •It also helps regulate blood sugar levels,
is a precursor to serotonin, a neurotransmitter stimulates wound healing, and produces
that regulates your appetite, sleep, and mood growth hormones.
9 ESSENTIAL AMINO ACIDS

ISOLEUCINE
•It’s also important for immune function,
hemoglobin production, and energy regulation.
HISTIDINE
•It’s critical for maintaining the myelin sheath,
a protective barrier that surrounds your nerve
LYSINE cells
•It’s also important for energy production,
immune function, and the production of
collagen and elastin
11 NON-ESSENTIAL AMINO
ACIDS
ALANINE ASPAR AGINE
•It works to remove these toxins so the liver is •It also acts as a detoxifier in the system and
able to metabolize them and eliminate them from regulates metabolism.
the body.

ASPARTIC AC ID CYSTEINE
•It also acts as a synthesizer for other amino acids. •It also strengthens stomach lining and is essential
to healthy hair, skin and nails.
ADDICTION C ONTROL
Presentations are communication tools that can be
GLUTAM INE GLYCINE
used as demonstrations.

•Proper brain function and digestion require •It is essential for proper cell growth and function,
glutamine as does the immune system. and is also crucial to digestive health.
11 NON-ESSENTIAL AMINO
ACIDS SER INE
•It is found in all cell membranes, also aids in
muscle formation and immune health.

TYROSINE TAURINE
•It also acts as a stress reducer and skin rebuilder. •It has also been shown to improve brain function
and athletic performance

PROLINE CYSTINE
•This amino acid helps in the regeneration of skin •It is one of the amino acids responsible for the
and helps to reduce sagging and wrinkles. creation of glutathione.
AMINO ACID METABOLISM

PROTEINS ARE
DIGESTED
by proteolytic enzymes such as pepsin and
AMINO ACIDS
trypsin, completely turning dietary protiens
into their constituent amino acids. Then amino undergo common reactions, such as
acids are therapidly absorbed from the intestine Transmination, then followed by deamination.
into the blood and subsequently become part of Where transmination is the process by which
the body’s pool of amino acids. amino groups are removed from amino acids
and transferred to acceptor keto-acids, while
Deamination is the process where amino
groups are removed from amino acids,
MAJOR SITE resulting in the formation ammonia.
of amino acid metabolism is in the liver, and
provides protein up to 12% to 20% of the total
body daily energy requirement.
 1. ALIPHATIC SIDE CHAINS
CLASSIFICATI It implies that the protein side chain contains only carbon
and hydrogen atoms. Although its side-chain contains a
ONS OF sulphur atom, it is largely non-reactive, meaning that
AMINO ACIDS Methionine effectively substitutes well with the true
aliphatic amino acids.

EXAMPLES
 2. POLAR SIDE CHAINS
Polar side chains contain groups that are either charged at
physiological pH or groups that are able to participate in
hydrogen bonding.

E
X
A
M
P
CLASSIFICATI L
ONS OF E
AMINO ACIDS S
 3. ACIDIC - HYDROPHILIC
CLASSIFICATI Have carboxyl group in their side chain (COOH) and a
negative charge.
ONS OF
EXAMPLE
AMINO ACIDS
 4. BASIC - HYDROPHILIC
Contain amino group in their side chain (NH2) and a
positive charge.

E
X
A
M
CLASSIFICATI P
ONS OF L
E
AMINO ACIDS
 5. HETEROCYCLIC/AROMATIC
CLASSIFICATI •It is an amino acid that includes an aromatic ring. Among
the 20 standard amino acids, the following are classify
ONS OF considered aromatic: phenylalanine, tryptophan and
AMINO ACIDS tyrosine.

EXAMPLES
A. NEUTRAL – MONOAMINE-
MONOCARBOXYLIC
1. 2.
BRANCHED CHAIN
STRAIGHT CHAIN
AMINO ACIDS
(BCAA)
a.Glycine It supress protein breakdown and are
b.Alanine used as an efficient energy source
c.Serine during exercise.
d.Threonine a.Valine
b.Leucine
c.Isoleucine
B. AROMATIC AMINO ACIDS –
AMINO ACIDS WITH PHENYL
HYDROXYPHENYL, OR INDOLE
RINGS.
1.Phenylalanine – phenyl ring
2.Tyrosine – hydroxyphenyl-ring
3.Trptophan – indole ring

C. IMINO ACIDS – IMINO –

MOLECULE THAT CONTAINS
BOTH IMINE (>C=NH) AND
CARBOXYL
1.Pyroline FUNCTIONAL
GROUP
2.Hydroxyproline
NON-POLAR, • Glycine (Gly)
ALIPHATIC R • Alanine (Ala)
• Proline (Pro)
GROUPS
AMINO ACID
• Is an amino acid containing an aliphatic side • Valine (Val)
chain functional group.
• Aliphatic R groups are nonpolar and
• Leucine (Leu)
hydrophobic. • Methionine (Met)
• Most aliphatic amino acids are found within
protein molecules. However, alanine and • Isoleucine (Ile)
glycine may be found either inside or outside
a protein molecule.
1. GLYCINE (GLY)
• Glycine is a nonpolar amino acid because there is a second
hydrogen atom at the ± carbon, glycine is not optically active.
• Glycine is the simplest amino acid and most commonly found in
animal proteins.
• It is a glucogenic and non-essential amino acid that is produced
naturally by living bodies and plays a key role in the creation of
several other important bio-compounds and proteins.

2. ALANINE (ALA)
• is an aliphatic amino acid, because the side-chain connected to the
α-carbon atom is a methyl group (-CH3).
• alanine is the simplest α-amino acid after glycine.
• The methyl side-chain of alanine is non-reactive and is therefore
hardly ever directly involved in protein function.
3. PROLINE (PRO)
•Proline is unique among the standard amino
acids in that it does not have both free α-amino
and free α-carboxyl groups. Instead, its side
chain forms a cyclic structure as the nitrogen
atom of proline is linked to two carbon atoms.

4 VALINE (VAL)
• is an aliphatic amino acid that is closely
related to leucine and isoleucine both in
structure and function.
• These amino acids are extremely
hydrophobic and are almost always found
in the interior of proteins.
• is often referred to as one of the amino
acids with hydrocarbon side chains, or as a
branched chain amino acid.
5. LEUCINE (LEU)
• is one of the three amino acid with a
branched hydrocarbon side chain.
• it has one additional methylene group in its
side chain compared with valine.
• Like valine, leucine is hydrophobic and
generally buried in folded proteins.
 6. METHIONINE 7. ISOLEUCINE
•(MET)
Nonpolar side chains are mostly •(ILE)
It is classified as a non-polar,
composed of nonpolar uncharged (at physiological pH),
hydrocarbons. The side chain of branched-chain, aliphatic amino
Methionine includes a sulfur atom as acid.
well. There is nothing in the side • Like Valine, and Threonine,
chain to cause a dipole. Isoleucine is C-beta branched.
• Therefore, methionine is nonpolar
because it's side chain has no dipole.
AROMATIC R GROUPS

Aromatic amino acids are relatively

nonpolar. To different degrees, all
aromatic amino acids absorb ultraviolet
light
 PHENYLALANINE

• Hydrophobic because of the benzyl Unique Features

side chain.
• Promotes alertness and vitality. Alanine plus a phenyl
• Elevates mood.
• Converted to tyrosine, which
• Decreases pain.
is, in turn, converted to L-
• Aids in memory and learning.
dopa
• Part of aspartame, a common
• Interferes with the
sweetener used in prepared foods as
sugar replacement. production of serotonin
 TYROSIN UNIQUE TRYPTOPHAN UNIQUE
FEATURES FEATURES
• Metabolically synthesized Similar to phenylalanine but • Precursor of serotonin and Bulky, aromatic side chains
from Phenylalanine. with polar hydroxyl group on melatonin, a neurohormone • Indole group
• Precursor of a number of phenyl ring and powerful antioxidant.
• Precursor for serotonin
hormones, particularly • Important metabolically • Natural Relaxant; alleviates
thyroid hormones. because ionization altered by insomnia by inducing sleep, and niacin
• Mood elevator. micro pH changes soothes anxiety, and reduces
• Reduces body fat depression.
• Used in the treatment of
migraine headaches and
ADHD

TYROSIN AND
 POLAR,
UNCHARGE • R groups are more soluble in
D GROUPS water
• Contain functional groups that can
form hydrogen bonds
• Serine , threonine, cysteine,
asparagine and glutamine
POLAR, UNCHARGED
GROUPS
1. Serine (Ser) 2. Threonine (Thr)
• Also an alcohol because of its side chain
• Contain aliphatic hydroxyl groups
• Highly concentrated in cell membranes
• Component of myelin sheaths - serine
palymitoyltransferase
• Also an alcohol because of its side chain
• It also contain aliphatic hydroxyl group.
• Important component of tooth enamel and
residue of proteins such as collagen and
elastin.
POLAR, UNCHARGED
GROUPS
3. Cysteine (Cys) 4. Asparagine (Asn)
• Important for protein synthesis, • First to be isolated in 1806 in a crystalline
detoxification and diverse metabolic form by French chemist Louis Nicolas
functions. Vauquelin and Pierre Jean Robiquet from
• Collagen production and skin elasticity and asparagus juice
texture. • Is required for development and function of
• Found in beta-keratin, the main protein in brain
nails, skin and hair.
POLAR, UNCHARGED
GROUPS
5. Glutamine (Gln)
• Most abundant amino acid in the body
• Plays an important role in maintaining the
balancing of acid-base ratio.
• Used to transport or remove excess ammonia
• Also is marked as a supplement for muscle
growth in weightlifting and body building.
POSITIVELY CHARGED
(BASIC) R GROUPS
POSITIVELY CHARGED (BASIC) R
GROUPS ARGININE
• Classified as a semi-essential or conditionally
essential amino acid.
LYSINE • Plays an important role in cell division, healing of
• Has a net positive charge, one of the three wounds, stimulation of protein synthesis, immune
basic amino acids. function, and the release of hormones.
• An essential amino acid necessary for human
health.
• Needed for proper growth and development. HISTIDINE
• Production of antibodies and lowers • A dietary essential amino acid
triglyceride levels. • Considered as a precursor of histamine
• Helps in absorption and conservation of • Involved in inflammatory response
calcium. • Stimulates the secretion of the digestive enzyme
gastrin.
• Serving as a neurotransmitter in the brain and
CNS.
 NEGATIVELY CHARGED
(ACIDIC) GROUP

• At neutral pH, two amino acids,

aspartic acid or aspartate (Asp) and
glutamic acid or glutamate, contain
acidic side chains (Glu). Their side
chains include carboxylic acid groups
with low pKas, allowing them to lose
protons and become negatively
charged.
 A SPA RTAT E
(A SPA RT I C A C I D )
• Aspartic acid (also known as aspartate) is a
non-essential amino acid that mammals can
easily and spontaneously produce.
• It is one among the 20 amino acids that make
up proteins.
• its three-letter code is ASP
• its one-letter code is D.
• GAC and GAU are the DNA codons that
code for aspartic acid.
• 2-aminobuanedioic acid is the IUPAC name..
NEGATIVELY CHARGED (ACIDIC)
GROUP)
GL UTAMINE
(GL UTAMIC
ACID)
• Glutamine is a glutamic acid derivative that
is created in the body through an energy-
intensive reaction mediated by glutamine
synthase.
• It has anti-cancer properties as well.
• Glutamine is an amino acid that the body
uses to make proteins.
• Other amino acids and glucose require it as
well.
• Supplementing with glutamine may benefit
gut health, immunological function, and
other bodily functions, particularly during
stressful times when the body utilizes more
glutamine.
• The carboxylate anions and salts of glutamic
acid are referred to as glutamates.
 • A short chain of amino acids, primarily
consist of two or more amino acids that are
formed by a peptide bond or a covalent
bond(in a case of two amino acids bonding).
⚬ Dipeptide (2 amino acids)
⚬ Tripeptide (3 amino acids)
• Polypeptide (50 or more amino acids)
PEPTIDES • Is usually smaller and shorter than proteins
• Helps in the formation of proteins through
peptide bonding of amino acids, or by the
formations of polypeptides.
• Peptide bonds held the proteins together from
the presence of polypeptides in its chain.
AMIDE BOND
FORMATION • heating a carboxylic
(RCOOH) with ammonia (NH3)
acid

or an amine ( R’NH2 or R’2NH)

• carbonyl compound that contains a
forms an amide.
nitrogen atom bonded to a
carbonyl atom

3rd Degree Amide

CLASSIFICATION OF AMIDE
DIPEPTIDE
FORMATION

• A dipeptide has two amino acids joined together by

one amide bond.
• Amide bond is called as a peptide bond
• To form a dipeptide, the –NH3 group of one amino
acid forms an amide bond with the carboxylate (-
COO) of another amino acid, and the elements H2O
are removed.
CONSTITUSTIO
NAL ISOMERS
Dipeptides (A and B)
N & C TERMINAL
AMINO ACIDS
N-terminal amino acid - The amino acid
with the free –NH3+ group and is written
on the left.

C-terminal amino acid - The amino acid

with the free –COO− group and is written
on the right.
NEUROPEPTI ENKEPHALINS
DES Pentapeptides synthesized in the brain act as pain killers
and sedatives by binding to pain receptors.
• Met-enkephalin
• Leu-enkephalin

ENDORPHINS
Contains amino acid that blocks pain and are thought to
produce the feeling of well being experienced by an
athlete after excessive or strenuous exercise.
PEPTIDE
HORMONE
OXYTOCIN AND
VASOPRESSIN
OXYTOCIN
A peptide hormone and neuropeptide
normally produced in the hypothalamus and
released by the posterior pituitary.

VASOPRESSIN
A hormone synthesized from the AVP gene
as a peptide prohormone in neurons in the
hypothalamus, and is converted to AVP.
 L I P P O N C O T T I L L U S T R AT E D R E V I E W S B I O CH E MI S T RY 7 TH E D I T I O N

REFERENCE By Denise R. Ferrier

THE BIOLOGY PROJECT

By University of Arizona

S S T U D Y. C O M

By Brekke Peterson Munks

PUBCHEM

By National Center for Biotechnology Information

S T RU C T U RE A N D F U N C T I O N - A MI N O A CI D

By Oregon State University

B I O C H E MI S T RY D E MY S T I F I E D

By McGraw-Hill
MEET THE TEAM

A C A O , A D R I A N J AY Y U , B EA LY K A H D EB A RO SA N ,
• Classification of Amino Acids. • NON-POLAR, Aliphatic R H EN D R EY
• Peptides
• A. Neutral Groups • Amide Bond Formation
• B. Aromatic Amino Acids
• Imino Acids-Imino
MEET THE TEAM

RICAFR E NT E, DIANGO, NOLI CABIGQUEZ,

• KENNE
NON-POLAR, TH R Groups
Aliphatic • JANEN
Negatively Charged (Acidic) • KIMBERLY
Polar Uncharged Groups
Group
MEET THE TEAM

EBUÑA, M ANNY JC . GALUA, MA. CAINOY, JEMIMAH

• Amino Acid Introduction • THERESA
Positively Charged (Basic) R • Source of Amino Acid
• Neuropeptides Groups • Roles and Function
• Peptide Hormone • Essential vs. Non Essential
Amino Acid
MEET THE TEAM

MUGOT, KR IST EN CABAC TULAN, ARA RESULGA,

• Amino Acid Metabolism • N & C Terminal • ANABELLE
Aromatic R Groups
END OF PRESENTATION

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