Introduction:

Amino acids are a class of important Q biomolecules that contain both amino groups and carboxylate
groups. In most contexts, the term ‘amino acids’ refers to the a-amino acids, so-called because both the
amino and carboxyl groups are attached to the a-carbon of the structure. However, other types of amino
acids are encountered in nature, such as the B-amino acids, in which the amino and carboxyl groups are
attached to different carbons in the backbone. The key elements of an amino acid are carbon ©,
hydrogen (H), oxygen (0),

And nitrogen (N), although other elements are found in the side chains of certain amino acids. About
500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be
classified in many ways. They can be classified according to the core structural functional groups’
locations as alpha- (a-), beta- (B-), gamma- (y-) or delta- (8-) amino acids; other categories relate to
polarity, pH level, and side-chain group type (aliphatic, acyclic, aron xic, containing hydroxyl or sulfur,
etc.). In thecontaining nyaroxyi or suitur, etc.). In the form of proteins, amino acid residues form the
second-largest component (water is the largest) of human muscles and other tissues. Beyond their role
as residues in proteins, amino acids participate in a Q number of processes such as neurotransmitter
transport and biosynthesis.

CONTENT:

1) History:

The first few amino acids were discovered in the early 19th century. In 1806, French chemists Louis-
Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound in asparagus that was subsequently
named asparagine, the first amino acid to be discovered. Cystine was discovered in 1810, although its
monomer, cysteine, remained undiscovered until 1884. Glycine and leucine were discovered in 1820. The
last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose,
who also determined the essential amino acids and established the minim daily requirements of all
amino acids for optimal growth. of all amino acids for optimal growth.

The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to
it. The first use of th term "amino acid" in the English langua dates from 1898, while the German term,
Aminosäure, was used earlier. Proteins were found to yield amino acids after enzymatic digestion or acid
hydrolysis. In 1902, Emil Fischer and Franz Hofmeister independently proposed that proteins are formed
from many amino acids, whereby bonds are formed between the amino group of one amino acid with
the carboxyl group of another, resulting in a linear structure that Fischer termed "peptide".

2) Structure:

The term amino acid usually refers to an a- amino carboxylic acid in which the a carbon atom adjacent to
a carboxylic acid moiety (- COOH) carries three other substituents: an amino group (-NH2), a hydrogen
atom (-H), and a variable side chain conventionally symbolized as "-R". These four substituents are
arranged around the a carbon in a tetrahedral fashion. Twonoverlapping arrangements are possible By
conventionarrangements are possible. By convention, these optically active, mirror-image stereoisomers
are designated the I and d forms. Except in the case of glycine, in which R is a second hydro atom, the
four substituents are differen making the a carbon atom a center of chirality. Only the l-isomers of amino
acids are commonly found in proteins. The biosynthetic pathways that produce amino acids are
stereospecific, and most generate only l-isomers. Therefore, l-isomers are present at much higher
concentrations in human tissues and bodily fluids. d-Amino acids, although less common than l-amino
acids, do have some important roles in nature. For example, they have long been known to be
components of the cell walls of certain bacteria. Recently, d-aspartate and d- serine have been found to
exist in significant concentrations in mammalian brains. In fact, evidence suggests that d-serine acts as a
genuine neurotransmitter.

When dissolved in aqueous solutions at neutral pH, the carboxylic acid groups of amino acids are
deprotonated, while their amino groups are protonated. This makes each amino acid molecule a dipolar
ion or zwitterion (from the GeX an zwitter, meaning mongrel).

3) Zwitterions:

In aqueous solution, amino acids exist two forms (as illustrated at the right), th molecular form and the
zwitterion form in equilibrium with each other. The two forms co-exist over the pH range pK1 - 2 to pK2 +
2, which for glycine is pH 0-12. The ratio of the concentrations of the two isomers is independent of pH.
The value of this ratio cannot be determined experimentally.

Because all amino acids contain amine and carboxylic acid functional groups, they are amphiprotic.At pH
= pK1 (ca. 2.2) there will be equal concentration of the species NH3+CH(R)CO₂H and NH3+CH(R)CO2 and
at pH = pK2 (ca. 10) there will be equal concentration of the species NH3*CH(R) CO2 and NH2CH(R)CO2.
It follows that the neutral molecule and the zwitterion are effectively the only species present at
biological pH.
It is generally assumed that the concentration of the zwitterion is much greater than the concentration
of the neutral molecule on the basis comparisons with the known pK values

4) Isoelectric point:

The variation in titration curves when the amino acids can be grouped by category. With
the exception of tyrosine, using titration to distinguish among hydrophobic amino acids is
problematic.

At pH values between the two pKa values, the zwitterion predominates but coexists in
dynamic equilibrium with small amounts of net negative and net positive ions. At the exact
midpoint between the two pKa values, the trace amount of net negative and trace of net
positive ions exactly balance, so that average net charge of all forms present is zero. This
pH is known as the isoelectric point pl, so pl = ½(pKa1 + pKa2). The individual amino acids
all have slightly different pKa values and therefore have different isoelectric points. For
amino acids with charged side chains, the pKa of the side chain is involved. Thus for Asp
or Glu with negative side chains, pl = 2(pKa₁ + pKaR), where pKap is the side chain pKa.
Cysteine also has a potentially negative side chain with pKa = 8.14, so plxould be
calculated as for Asp and Glu, even though the side

5) Essential amino acids :

The body needs 20 different amino acids to maintain good health and normal functioning.
People must obtain nine of these amino acids, called the essential amino acids, through
food. Good dietary sources include meat, eggs, tofu, soy, buckwheat, quinoa, and dairy

Amino acids are compounds that combine to make proteins. When a person eats a food that contains
protein, their digestive system breaks the protein down into amino acids. The body then combines the
amino acids in various ways to carry out bodily functions.
A healthy body can manufacture the other 11 amino acids, so these do not usually need to enter the
body through the diet.

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.

Lysine

Lysine plays a vital role in building muscle, maintaining bone strength, aiding recovery from injury or
surgery, and regulating hormones, antibodies, and enzymes. It also have antiviral effects. There is not a
lot of research available on lysine deficiency, but a study on rats indicates that lysine deficiency can lead
to stress- induced anxiety.

Histidine

Histidine facilitates growth, the creation of blood cells, and tissue repair. It also helps maintain the
special protective covering over nerve cells, which is called the myelin sheath. The body metabolizes
histidine into histamine, which is crucial for immunity, reproductive health, and digestion. The results of
a study that recruited women with obesity and metabolic syndrome suggest that histidine supplements
may lower BMI and insulin resistance.

Deficiency can cause anemia, and low blood levels appear to be more common among people with
arthritis ar idney disease.

Threonine

Threonine is necessary for healthy skin and teeth, as it is a component in tooth enamel, collagen, and
elastin. It helps a metabolism and may be beneficial for people with indigestion, anxiety, and mild
depression.A 2018 study found that threonine deficiency in fish led to these animals having a lowered
resistance to disease.

Methionine
Methionine and the nonessential amino acid cysteine play a role in the health and flexibility of skin and
hair. Methionine also helps keep nails strong. It aids the proper absorption of selenium and zinc and the
removal of heavy metals, such as lead and mercury.

Valine

Valine is essential for mental focus, mu coordination, and emotional calm. Peo may use valine
supplements for muscle growth, tissue repair, and energy. Deficiency may cause insomnia and reduced
mental function.

Isoleucine

Isoleucine helps with wound healing, immunity, blood sugar regulation, and hormone production. It is
primarily present in muscle tissue and regulates energy levels. Older adults may be more prone to
isoleucine deficiency than younger people. This deficiency may cause muscle wasting and shaking.

Phenylalanine

Phenylalanine helps the body use other amino acids as well as proteins and enzymes. The body converts
phenylala to tyrosine, which is necessary for specific brain functions. Phenylalanine deficiency, though
rare, can lead to poor weight gain in infants. It may also cause eczema, fatigue, and memory problems in
adults.

Phenylalanine is often in the artificial sweetener aspartame, which manufacturers use to make diet
sodas. Large doses of aspartame can increase the levels of phenylalanine in the brain and may cause
anxiety and jitteriness and affect sleep. People with a rare genetic disorder called phenylketonuria (PKU)
are unable to metabolize phenylalanine. As a result, they should avoid consuming foods that contain
high levels of this amino a in acid.

6) Synthesis:
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual
amino acids usi glucose as a carbon source. Some ami acids are produced by enzymatic conversions of
synthetic intermediates. 2- Aminothiazoline-4-carboxylic acid is an intermediate in one industrial
synthesis of L- cysteine for example. Aspartic acid is produced by the addition of ammonia to fumarate
using a lyase.

In plants, nitrogen is first assimilated into organic compounds in the form of glutamate, formed from
alpha- ketoglutarate and ammonia in the mitochondrion. For other amino acids, plants use
transaminases to move the amino group from glutamate to another alpha-keto acid. For example,
aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate.
Other organisms use transaminases for amino acid synthesis, too.

Nonstandard amino acids are usually formed through modifications to standard amino acids. For exam
homocysteine is formed through the transsulfuration Microorganisms and plants synthesize many

Uncommon amino acids. For example, some

Microbes make 2-aminoisobutyric

Acid and lanthionine, which is a sulfide-

Bridged derivative of alanine. Both of the

Amino acids are found in

Peptidic lantibiotics such as alamethicin.

However, in plants, 1-aminocyclopropane-1-

Carboxylic acid is a small disubstituted

Cyclic amino acid that is a key intermediate

Hormone ethylene.

7) Amino Acid Dating:

Amino acid dating is a dating technique used to estimate the age of a specimen in paleobiology,
molecular paleontology, archaeology, forensic science, taphonomy, sedimentary geology, and other
fields. This technique relates changes in amino acid molecules to the time elapsed since they were
formed.

All biological tissues contain amino acids. All amino acids except glycine (the simplest one) are optically
active, having a stereocenter at their a-C atom. This means that the amino acid can have two different
configurations, “D” or “which are mirror images of each other. With a few important exceptions, living
organisms keep all their amino acids in the “L” configuration. When an organism dies, control over the
configuration of the amino acids ceases, and the ratio of D to L moves from a value near O towards an
equilibrium value near 1, a process called racemization. Thus, measuring the ratio of D to L in a sample
enables one to estimate how long ago the specimen died.

8) Unusual Amino Acids:

Several L-amino acids have physiologic functions as free amino acids rather th constituents of proteins.
Examples are as follows:

1.ẞ-Alanine is part of the vitamin pantothenic acid.

2. Homocysteine, homoserine, ornithine, and citrulline are intermediates in the biosynthesis of certain
other amino acids.

3. Taurine, which has an amino group in the B-carbon and a sulfonic acid group instead of COOH, is
present in the CNS and as a component of certain bile acids participate in digestion and absorption of
lipids in the gastrointestinal tract.
9) Conditional amino acids:

Although 11 of the amino acids are nonessential, humans may require some of them if they are under
stress or have an illness. During these times, the body m be able to make enough of these amino acids to
keep up with the increased demand. These amino acids are “conditional,” which means that a person
may require them in certain situations. People may sometimes wish to take essential amino acid
supplements. It is best to seek advice from a doctor first regarding safety and dosage.

10) Incorporating essential amino acids into the diet:

Although it is possible to be deficient in essential amino acids, most people can obtain enough of them
by eating a diet that includes protein.

The foods in the following list are the most common sources of essential amino acids:

Lysine is in meat, eggs, soy, black beans, quinoa, and pumpkin seeds.

• Meat, fish, poultry, n, seeds, and whole grains contain large amounts of histidine.

High quantities of threonine.

• Methionine is in eggs, grains, nuts, and seeds.

• Valine is in soy, cheese, peanuts, mushrooms, whole grains, and vegetables.

⚫ Isoleucine is plentiful in meat, fish, poultry, eggs, cheese, lentils, nuts, and seeds.

Dairy, soy, beans, and legumes are sources of leucine.

Phenylalanine is in dairy, meat, poultry, soy, fish, beans, and nuts.

These are just a few examples of foods that are rich in essential amino acids. All foods that contain
protein, whether plant-based or animal-based, will contain at least some of the essential amino acids.

Bibliography:

1. https://en.wikipedia.org/wiki/Amino_acid

2. https://www.sciencedirect.com/topics/medi and-dentistry/amino-acid

3. https://www.sigmaaldrich.com/life- science/metabolomics/learning- center/amino-acid-

4. https://www.medicalnewstoday.com/articles amino-acids

5. https://www.healthkart.com/connect/the- all-essential-amino-acids-foods-list-you- must-know-

6. https://www.google.co.in/search? Q=amino+acids&tbm=isch&chips=q:amino+a Z3LMW

7. https://acknowledgementsample.com/2013/ sample-for-school-pect/