I.

Amino Acids
Amino acids are organic nutrients that appear in foods and in the human body either as building blocks of proteins or as free
amino acids.
Amino acids are made of the amino group (NH2), carboxyl group (COOH) and a side chain containing carbon, hydrogen or
oxygen; two amino acids (cysteine and methionine) also contain sulfur and one (selenocysteine) contains selenium.

Functions of Amino Acids

Amino acids are a source of energy; like proteins, they can provide about 4 Calories per gram.
In the human body, certain amino acids can be converted to other amino acids, proteins, glucose, fatty acids or ketones.
Other functions of amino acids:
Chemical messengers (neurotransmitters) in the nervous system: aspartate, GABA, glutamate, glycine, serine
Precursors of other neurotransmitters or amino acid-based hormones:
Tyrosine is a precursor of dopamine, epinephrine, norepinephrine and thyroxine.
Tryptophan is a precursor of melatonin and serotonin and nicotinic acid (vitamin B3)
Histidine is a precursor of histamine.
Glycine is a precursor of heme, a part of hemoglobin.
Aspartate, glutamate and glycine are precursors of nucleic acids, which are parts of DNA.

Names Symbol Abbreviation Structural Formula Notes

1. Glycine, C2H5NO2
Aminomethanoic acid
Aminoacetic acid
Glycollol
2. Alanine, C3H7NO2
2-Aminopropionic acid
Aliphatic R Groups
G Gly Least complex structure. Not
(GGU chiral. Side chain small enough
GGC to fit into niches too small for
GGA other amino acids.
GGG)
A Ala
(GCU
GCC Alanine (Ala, A), Valine (Val,
GCA V), Leucine (Leu,
GCG) L), Isoleucine (Ile, I)

3. Isoleucine, I Ile
C6H13NO2 (AUU no reactive functional
AUC groups
2-Amino-3- AUA) highly hydrophobic:
methylpentanoic acid
play important role in
maintaining 3-D
4. Leucine, L Leu structures of proteins
C6H13NO2 (UUA because of their
2-Amino-4- UUG tendency to cluster away
methylpenthanoic acid CUU from water.
CUC
CUA
CUG)

5. Valine, C5H11NO2 V Val

(GUU
2-Amino-3- GUC
methylbutanoic acid GUA
GUG)

6. Proline, C5H7NO2 P Pro Has cyclic side chain called a

Pyrrolidine-2- (CCU pyrolidine ring. Restricts
carboxylic acid CCC geometry of polypeptides,
CCA sometimes introducing abrupt
changes in direction of
CCG)
polypeptide chain.

Aromatic R Groups
7. Phenylalanine, F Phe Phenylalanine has benzene
C9H11NO2 (UUU ring therefore hydrophobic.
UUC)
(S)-2-Amino-3-
phenylpropanoic acid

8. Tyrosine, Y Tyr
C9H11NO3 (UAU
L-2-Amino-3- UAC)
(4-hydroxyphenyl)
propanoic acid Tyrosine and Tryptophan
have side chains with polar
groups, therefore less
hydrophobic than Phe.
9. Tryptophan, W Trp
C11H12N2O2 (UGG)
2-Amino-3-(1H-indol-3-
yl) propanoic acid

Sulfur-containing R Groups
10. Methionine, M Met Methionine is hydrophobic.
C5H11NO2S (AUG) Sulfur atom is nucleophilic.

2-Amino-4-
(methylthio)butanoic
acid

11. Cysteine, C Cys Cysteine is somewhat

C3H7NO2S (UGU hydrophobic. Highly reactive.
Form disulfide bridges and may
UGC)
2-Amino-3- stabilize 3-D structure of proteins
by cross-linking Cys residues in
sulfhydrylpropanoic
peptide chains.
acid

Side Chains with Polar Alcohol Groups

12. Serine, S Ser Serine and Threonine have
C3H7NO2 (UCU uncharged polar side chains.
UCC Alcohol groups give
2-Amino-3- UCA hydrophilic character.
hydroxypropanoic acid UCG
AGU
AGC) Weakly ionizable.

13. Theronine, T Thr

C4H9NO3 (ACU
ACC
2-Amino-3- ACA
hydroxybutanoic acid ACG)

Basic R Groups
14. Arginine, R Arg
C6H14N4O2 (CGU
CGC Histidine, Lysine,
2-Amino-5- CGA and Arginine have
guanidinopentanoic acid CGG hydrophilic side chains that
AGA
are nitrogenous bases and
AGG)
positively charged at
physiological pH.
15. Histidine, H His
C6H9N3O2 (CAU
CAC) Arg is most basic amino
2-Amino-3-(1H-imidazol-
4 yl)propanoic acid
acid, and contribute
positive charges to
proteins.
16. Lysine, K Lys
C6H14N2O2 (AAA
AAG)
2,6-Diaminohexanoic
acid
Diammoniohexanoic
acid
 Acidic R Groups and their Amide derivatives
17. Aspartate, D Asp
C4H7NO4 (GAU
GAC)
2-aminobutanedioic Aspartate and Glutamate a
acid
re dicarboxylic acids,
ionizable at physiological
18. Glutamate, E Glu pH. Confer a negative
C5H9NO4 (GAA charge on proteins.
GAG)
2-Aminopentanedioic
acid

19. Asparagine, N Asn

C4H8N2O3 (AAU Asparagine and Glutamine
AAC) are amides of Asp and Glu,
2-Amino-3- respectively.
carbamoylpropanoic
acid
highly polar and often
found on surface of
proteins
20. Glutamine, Q Gln
polar amide groups can
C5H10N2O3 (CAA form H-bonds with
CAG)
L-Glutamine atoms in other amino
(levo)glutamide acids with polar side
2-Amino-4- chains.
carbamoylbutanoic acid

II. ESSENTIAL Amino Acids

Plants are able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis
of all of the amino acids. The human body can synthesize all of the amino acids necessary to build proteins except for the ten called the
"essential amino acids" An adequate diet must contain these essential amino acids. Typically, they are supplied by meat and dairy
products, but if those are not consumed, some care must be applied to ensuring an adequate supply. They can be supplied by a
combination of cereal grains (wheat, corn, rice, etc.) and legumes (beans,peanuts, etc.). Plants able to make all the amino acids. Humans,
on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids."
1. Histidine (His)
In foods, histidine is incorporated into proteins.
2. Isoleucine (Ile)
Synthesize from pyruvate from employing leucine biosynthesis enzymes in other organisms such as bacteria.
Inability to breakdown along with other amino acids is associated with the disease called maple syrup urine
disease, resulting in discoloration and sweet smell in the patients urine.

3. Leucine (Leu)
It is used in the liver, adipose tissue, and the muscle tissue. Adipose and Muscle tissue use leucine for the
formation of sterols.
4. Lysine (Lys)
 Synthesis of protein. Production of animal feed it serves as the limiting amino acid when optimizing the growth of
certain animals such as pigs and chickens for the production of meat.
5. Methionine (Met)
Methionine is important in the growth of new blood vessels, and supplementation may benefit those suffering
from Parkinsons, drug withdrawal, schizophrenia, radiation, copper poisoning, asthma, allergies, alcoholism, or
depression
6. Phenylalanine (Phe)
Found naturally on breast milk of mammals. It is used in the manufacture of food and drink products and sold as a
nutritional supplement for its reputed analgesic and antidepressant effects.

7. Threonine (Thr)
Essential to humans. Pre-cursor for glycine, and can be used as a prod rug to reliably elevate brain glycine levels.
8. Tryptophan (Trp)
Is needed to prevent illness or death, but cannot be synthesized and must be ingested short.
9. Valine (Val)
Synthesized in plants from pyruvic acid.
10. Arginine (Arg)
Are required for the young, but not for adults.

Why amino acids are important and what role do they play in the body?
Amino acids are central to virtually every function of the human body. They are used in structures and in metabolic
reactions for the bodys optimal functioning. Protein and amino acids are used by the body for growth and development, making
tissues such as muscle, skin, nails, and hair. They are also used in making hormones and antibodies. We use amino acids for
chromosomes, which contain our genetic code. We also use them for neurotransmitter production, cell growth, reproduction and repair.
Proteins are essential for glandular function and for detoxification. Amino acids can also be used for the manufacture of energy and
enzymes (molecules involved in speeding up reactions). Any amino acid excess is stored by the body, as glycogen, for future use. Amino
acids also help to regulate water balance and the bodys pH (acid/base balance).