Erbil polytechnic university

Institute of medicine
Department of pharmacy
First stage
Group: C

Report about:
Amino acids

prepared by: supervised by:

kamal Seamand Dr. Cheman
Ismail Bilal
Sardar Salem
Esra Talhat
Shewaz Momen
Contents
INTRODUCTION.....................................................................................................................................................3
PHENYLALANINE..................................................................................................................................................3
HISTIDINE...............................................................................................................................................................5
TRYPTOPHAN.........................................................................................................................................................7
TYROSINE................................................................................................................................................................9
GLUTAMINE..........................................................................................................................................................10
SOURCES...............................................................................................................................................................12

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INTRODUCTION

Amino acids serve as the fundamental building blocks of life, playing pivotal roles in the
structure, function, and regulation of virtually all biological processes. Comprising a
diverse family of organic compounds, each amino acid contributes distinct characteristics
to the intricate tapestry of life. From their indispensable role in protein synthesis to their
involvement in neurotransmission and metabolic pathways, amino acids stand as the
molecular architects of cellular life. Understanding their properties, functions, and
significance offers profound insights into the complexities of biological systems and has
far-reaching implications in fields ranging from medicine to nutrition and beyond. This
introduction sets the stage for a deep dive into the captivating world of amino acids,
unraveling their pivotal contributions to the marvel of life itself.

We are talking about 5 amino acids including.

(Phenylalanine, Histidine, Tryptophan, Tyrosine, Glutamine)

PHENYLALANINE

Phenylalanine is an essential aromatic amino acid with a crucial role in protein synthesis
and various physiological functions within the human body.

STRUCTURE
Phenylalanine (symbol Phe or F) is an essential α-amino acid with the formula C9 H11
NO2.
It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl
group in place of a terminal hydrogen of alanine.
This essential amino acid is classified as neutral, and nonpolar because of the inert and
hydrophobic nature of the benzyl side chain.

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FUNCTTIONS

1. Protein Synthesis:
Phenylalanine is an essential amino acid, meaning it cannot be synthesized in the body
and must be obtained through the diet.
It is a vital building block for the synthesis of proteins, which are crucial for the growth,
repair, and maintenance of tissues, as well as the production of enzymes and various
structural components within the body.

2. Precursor for Neurotransmitters:

Phenylalanine is a precursor for several important neurotransmitters, including dopamine,
norepinephrine, and epinephrine.
These neurotransmitters play essential roles in mood regulation, stress response, and
cognitive function.

3. Tyrosine Synthesis:
Within the body, phenylalanine can be converted into another amino acid called tyrosine
through a process known as hydroxylation. Tyrosine, in turn, acts as a precursor for the
synthesis of important molecules such as thyroid hormones and melanin, the pigment
responsible for skin, hair, and eye color.

4. Phenylketonuria (PKU) Treatment:

In the context of phenylketonuria (PKU), a genetic disorder in which the body cannot
metabolize phenylalanine properly, individuals with PKU must closely monitor their
phenylalanine intake. Additionally, they may take a special formula that contains limited
phenylalanine but includes other necessary nutrients and amino acids. This specialized
diet helps prevent the accumulation of phenylalanine and the associated neurological
issues.

5. Pharmaceutical and Industrial Applications:

Phenylalanine also has applications in the pharmaceutical and food industries. Its
derivatives are used as sweeteners, flavor enhancers, and in the production of certain
drugs and pharmaceutical compounds.

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HISTIDINE

Histidine is an essential aromatic amino acid that plays a crucial role in various biological
processes.

Contains an -amino group, a carboxylic acid group, and an imidazole side chain.
Histidine has unique roles in proton buffering, metal ion chelation, scavenging of reactive
oxygen and nitrogen species, erythropoiesis, and the histaminergic system.
HIS-rich proteins, HIS-containing dipeptides, and methyl- and sulphur-containing
derivatives of HIS have specific functions.
Initially, HIS was shown to treat rheumatoid arthritis and anemia in patients with chronic
renal failure.
Currently, HIS and/or HIS-containing dipeptides (HIS-CD) are investigated to prevent
fatigue during strenuous exercise and for therapy in ageing-related disorders, metabolic
syndrome, atopic dermatitis, ulcers, inflammatory bowel diseases, ocular diseases, and
neurological disorders.
People use histidine for diarrhea due to cholera infection, eczema, kidney failure,
metabolic syndrome,

STRUCTURE

The chemical structure of histidine includes a hexagonal ring with two nitrogen atoms,
one of which is part of an imidazole ring.
It has a side chain with a carboxyl group and an amino group.
The chemical formula for histidine is
C₆H₉N₃O₂.

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FUNCTTIONS

1. Protein Building: Histidine is one of the essential amino acids, meaning the body
cannot produce it and must obtain it from the diet.
It is a building block for proteins, contributing to the structure of various proteins in the
body.
2. Enzyme Catalysis: Histidine plays a crucial role in enzyme catalysis.
It can act as a proton donor or acceptor in enzymatic reactions, influencing the activity of
various enzymes.
3. Buffering Agent: The imidazole side chain of histidine has a pka value near
physiological PH, allowing it to act as a buffer in biological systems. This helps regulate
the PH of cellular environments.
4. Metal Binding: Histidine residues can bind to metal ions, particularly in
metalloproteins and metalloenzymes.
This metal binding is essential for the structure and function of these proteins.
5. Neurotransmitter Precursor: Histidine is a precursor to histamine, a neurotransmitter
involved in various physiological processes, including immune responses, gastric acid
secretion, and neurotransmission in the central nervous system.
6. DNA Stabilization: Histidine is involved in the stabilization of DNA structures.
It can interact with DNA molecules, contributing to the overall stability of the double
helix.
7. Proton Shuttle: Histidine can act as a proton shuttle, aiding in the transfer of protons
during enzymatic reactions and other cellular processes.
8. Signal Transduction: It plays a role in signal transduction pathways, influencing
cellular responses to external stimuli.
9. Metalloprotein Activation: Histidine residues can activate metalloproteins by
coordinating with metal ions, influencing their activity and function.
10. DNA Binding: Histidine has been implicated in DNA-binding proteins, participating
in processes such as gene regulation.
11. Antioxidant Properties: It may exhibit antioxidant properties, helping to counteract
oxidative stress in cells.

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TRYPTOPHAN

Tryptophan, an amino acid that is nutritionally important and occurs in small amounts in
proteins.
It is an essential amino acid, meaning that humans and certain other animals cannot
synthesize it and must obtain it from their diets.
Infants require greater amounts of tryptophan than adults to ensure normal growth and
development.
Tryptophan is used by the body to manufacture several important substances, including
the neurotransmitter serotonin and the vitamin niacin.
Diets poor in tryptophan can lead to pellagra, a disease resulting from niacin deficiency;
however, this disease is now rare in developed countries.
In 1901 the English biochemist Frederick G. Hopkins isolated tryptophan from casein, the
major protein found in milk.

The chemical structure of tryptophan is

C₁₁H₁₂N₂O₂

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FUNCTTIONS

The body uses tryptophan to produce:

1. Serotonin: A neurotransmitter involved in regulating mood, appetite, sleep, pain, sex
drive, and digestion.
2. Melatonin: A hormone that helps regulate the circadian rhythm (sleep-wake cycle).
3. Vitamin B-3: Niacin is needed for energy metabolism and DNA production.
The body needs enough iron, riboflavin, and vitamin B-6 to change dietary tryptophan
into niacin.
Tryptophan is also necessary for the production of the body's:
 Proteins
 Enzymes
 Muscle tis

Sources of Tryptophan
 Tryptophan can be found in foods such as;
 Chicken
 Turkey
 Fish
 Egg whites
 Milk
 Peanuts
 Soybeans
 Sunflower seeds
 Sesame seeds
 Pumpkin seeds
 Other high-protein foods

Getting tryptophan into the brain can be tricky as it competes for entry with other
tryptophan in the bloodstream with less competition for entry to the brain.

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TYROSINE

L-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20

standard amino acids that are used by cells to synthesize proteins.
It is a non-essential amino acid with a polar side group.
The word "tyrosine" is from the Greektyrós, meaning cheese, as it was first discovered in
1846 by German chemist Justus von Liebig in the protein casein from cheese.
It is called tyrosylwhen referred to as a functional group or side chain.
While tyrosine is generally classified as a hydrophobicamino acid, it is more hydrophilic
than phenylalanine.
It is encoded by the codons UAC and UAU in messenger RNA.
The structural formula for tyrosine is:
C₉H₁₁NO₃

Functions
Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of
the phenol functionality.
It occurs in proteins that are part of signal transduction processes and functions as a
receiver of phosphate groups that are transferred by way of protein kinases.
Phosphorylation of the hydroxyl group can change the activity of the target protein, or
may form part of a signaling cascade via SH2 domainbinding.
A tyrosine residue also plays an important role in photosynthesis.

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In chloroplasts (photosystem II), it acts as an electron donor in the reduction of
oxidized chlorophyll. In this process, it loses the hydrogen atom of its phenolic OH-group.
This radical is subsequently reduced in the photosystem II by the four core manganese
clusters. citation needed

Top Foods High in Tyrosine

Tyrosine is one of the 20 amino acids that people need to make proteins. It is a
non-essential amino acid — which means your body can make it, so it doesn't have to be
included in the diet. In fact, tyrosine is a building block that appears in almost every
protein in the human body.
Sleep deprivation
One study suggests that taking tyrosine may help you be more alert after sleep
deprivation. More research is needed.

GLUTAMINE

Glutamine is the most abundant amino acid in the body and is a building block for
making proteins.
It is also needed to make other amino acids and glucose.
Glutamine supplements might help gut function, immune function, and other processes,
especially in times of stress when the body uses more glutamine.
Glutamine is important for removing excess ammonia from the body and supports the
immune and digestive systems.
What is the glutamine?
Glutamine is the most abundant naturally occurring.
Nonessential amino acid in the human body, and one of the few amino acids that can
directly cross the blood-brain barrier.
It is a building block for making proteins and is involved in more metabolic processes
than any other amino acid.
Glutamine is important for removing excess ammonia, supporting the immune and
digestive systems, and may be needed for normal brain function and digestion.

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The body can usually synthesize sufficient amounts of glutamine, but in some instances of
stress, the body’s demand for glutamine increases, and it may need to be obtained from
the diet or supplements.
It Is Found in Many Foods:
Glutamine is naturally found in a variety of foods.
It has been estimated that a typical diet contains 3 to 6 grams per day, but this can vary
based on your specific diet.
The largest amounts are found in animal products due to their high protein contents.
However, some plant-based foods have a greater percentage of it in their protein.
One study used advanced lab techniques to determine how much L-glutamine is found in
various foods.

The following are the percentages of protein made up of L-glutamine in each food:
Eggs: 4.4% (0.6 g per 100 g of eggs)
Beef: 4.8% (1.2 g per 100 g of beef)
Skim milk: 8.1% (0.3 g per 100 g of milk)
Tofu: 9.1% (0.6 g per 100 g of tofu)
White rice: 11.1% (0.3 g per 100 g of rice)
Corn: 16.2% (0.4 g per 100 g of corn)

Although some plant sources, such as white rice and corn, have a large percent of protein
made up of glutamine, they have fairly low protein contents overall.
Thus, meat and other animal products are the simplest ways to get high amounts of it.
Unfortunately, the exact glutamine content of many specific foods has not been studied.
However, because glutamine is a necessary part of proteins, virtually any food containing
protein will contain some glutamine.
Focusing on getting enough protein in your overall diet is an easy way to potentially
increase the amount of glutamine you are consuming.

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SOURCES

 https://www.webmd.com/vitamins/ai/ingredientmono-878/glutamine

 https://www.healthline.com/nutrition/glutamine

 https://www.webmd.com/diet/health-benefits-glutamine

 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6266414/

 https://www.mountsinai.org/health-library/supplement/glutamine

 https://pubchem.ncbi.nlm.nih.gov/compound/Phenylalanine

 https://www.healthline.com/

 https://www.webmd.com/vitamins/ai/ingredientmono-653/phenylalanine

 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7146355/

 https://www.webmd.com/vitamins/ai/ingredientmono-467/histidine

 https://www.webmd.com/diet/foods-high-in-tryptophan

 https://www.healthline.com/health/tryptophan

 https://www.webmd.com/vitamins/ai/ingredientmono-1037/tyrosine

 https://www.webmd.com/diet/foods-high-in-tyrosine

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