ASSIGNMENT # 5: AMINO ACIDS

 Name: Mariano, Mariella Jasmine                                Rating:

Course/Section: BS Psychology – 2C                           Date of Submission: March 29, 2023
 
I.AMINO ACIDS

I. ESSENTIAL AMINO ACIDS: They are called essential because they are required for growth and
development but they cannot be synthesized by the body and hence must be taken as a part of diet.
· Adequate amount of essential amino acids are required to maintain the proper nitrogen balance in the body

STRUCTURE EXAMPLES FUNCTIONS RESULT IF DEFICIENT

- Histidine is an amino acid - Histidinemia results from

1. most people get from food. deficiency ofl-histidase (l-
It's used in growth, repair of histidine ammonia lyase),
damaged tissues, and making resulting in accumulation of
- Histidine blood cells. histidine and its metabolites
- It helps protect nerve cells. in blood, urine, and CSF
It's used by the body to make and in a deficiency of
histamine. urocanic acid.

- Isoleucine, as one of the

branched chain amino acids,
is also critical in
2. physiological functions of the
- Isoleucine deficiency is
whole body, such as growth,
most common in older
immunity, protein
- Isoleucine people and can lead to the
metabolism, fatty acid
weakening and wasting of
metabolism and glucose
muscle, and tremors.
transportation. Isoleucine can
improve the immune system,
including immune organs,
cells and reactive substances.

- Leucine is an essential
amino acid for protein
synthesis. Additionally,
3. similarly to other amino
- Leucine deficiency is
acids, the carbon skeleton of
much less common but can
leucine can be used to
- Leucine lead to similar symptoms,
generate ATP. However,
such as muscle weakness
leucine can also regulate
and blood sugar fluctuations
several cellular processes
such as protein synthesis,
tissue regeneration, and
metabolism.

4. - Lysine - It is involved in the - A deficiency of lysine can

synthesis of proteins, lead to impaired growth,
collagen, and enzymes, which anemia, and compromised
are essential for tissue repair
 immune function.
and growth. Lysine also helps - Lysine deficiency can also
in the absorption of calcium cause slow growth in
and the formation of children and may affect
carnitine, which aids in fat their cognitive
metabolism. Additionally, development. Additionally,
lysine has antiviral properties lysine deficiency has been
that can help prevent cold linked to the development
sores and herpes outbreaks. of cold sores and herpes
outbreaks.

- Methionine is an essential
amino acid that plays a vital
role in various physiological
functions. It is required for
the synthesis of proteins,
5. DNA, and other important
- Methionine deficiency can
molecules in the body.
lead to a range of health
Methionine also helps to
- Methionine problems such as liver
maintain healthy liver
damage, depression, and
function by aiding in the
impaired growth.
detoxification process.
Additionally, it acts as a
precursor for the production
of SAMe, a compound that
regulates mood and supports
joint health.

- One of the most severe

consequences of
phenylalanine deficiency is
- One of the primary a genetic disorder called
functions of phenylalanine is phenylketonuria (PKU). In
to promote the production of PKU patients, the body
dopamine, a neurotransmitter cannot break down
6. that regulates mood, phenylalanine properly due
motivation, and pleasure. to the absence or
Low levels of dopamine have malfunctioning of an
- Phenylalanine
been linked to depression and enzyme called
other mood disorders. phenylalanine hydroxylase.
Phenylalanine also helps in As a result, excess
the synthesis of adrenaline phenylalanine accumulates
and noradrenaline, hormones in the blood and brain
that regulate blood pressure leading to mental
and heart rate. retardation, seizures,
behavioral problems, and
other neurological
disorders.

7. - Threonine - Threonine mainly serves as - One of the most

a substrate for protein significant consequences of
synthesis, particularly mucin. threonine deficiency is
In addition, Thr can enter the impaired growth and
catabolic pathway, where it development.
can be metabolized to a
variety of important products - Threonine deficiency can
(glycine, acetyl CoA, also affect the immune
pyruvate) that play a crucial system's function by
reducing the production of
 antibodies that fight off
infections.

role in host metabolism. - Threonine deficiency can

cause neurological
problems such as confusion,
irritability, and seizures

- The body uses tryptophan to - Acute tryptophan

help make melatonin and depletion is associated with
serotonin. Melatonin helps increased pain sensitivity,
8. regulate the sleep-wake cycle, acoustic startle, motor
and serotonin is thought to activity, and aggression in
help regulate appetite, sleep, humans. Tryptophan
- Trytophan
mood, and pain. The liver can deficiency increases anxiety
also use tryptophan to and irritability in humans
produce niacin (vitamin B3), and may modulate
which is needed for energy aggressiveness and the
metabolism and DNA response to stress in
production. animals.

- Valine deficiency can

- It promotes muscle growth cause many physical and
and tissue repair. It is a mental side effects such as
9. precursor in the penicillin low muscle tone
biosynthetic pathway. Valine (hypotonia), hyperkinesia,
is one of three branched-chain hyperactivity, excessive
- Valine
amino acids (the others are drowsiness and delayed
leucine and isoleucine) that mental and physical
enhance energy, increase development. Low levels of
endurance, and aid in muscle valine may also cause a
tissue recovery and repair. deterioration in one's mental
health, and insomnia.

II. SEMI- ESSENTIAL: They are synthesized partially by the body but not at  the rate to meet   the
requirement in growing children, pregnant and lactating women

- Arginase deficiency
1. - Arginine is a conditionally (argininemia) is an
essential amino acid, autosomal recessive
especially in such conditions metabolic disorder
as trauma, burn injury, small- characterized by
bowel resection, and renal hyperammonemia
failure. L-arginine secondary to arginine
- Arginine
administration improves accumulation. Ammonia
cardiovascular, pulmonary, levels can vary according to
immune, and digestive the patient's current age and
functions and protect against status, presenting initially
the early stages of with slow growth, followed
cancerogenesis. by developmental delay and
cognitive problems.

2. - Cysteine - Cysteine is a non-essential - Cysteine deficiencies

amino acid important for identified by inherited
making protein, and for other metabolic disorders or
metabolic functions. It's reduced levels in body fluid
found in beta-keratin. This is have been associated with:
the main protein in nails, 1) impaired antioxidant
 defenses; 2) decreased
ability to metabolize drugs
skin, and hair. Cysteine is or toxic compounds; 3)
important for making depressed immune
collagen. functions; 4) some
psycoses; and 5)
homocystinemia.

- It is an essential component
- Tyrosine hydroxylase
for the production of several
(TH) deficiency is a
important brain chemicals
disorder that primarily
3. called neurotransmitters,
affects movement, with
including epinephrine,
symptoms that may range
norepinephrine, and
- Tyrosine from mild to severe. The
dopamine. Neurotransmitters
mild form of this disorder is
help nerve cells communicate
called TH-deficient dopa-
and influence mood. Tyrosine
responsive dystonia (DRD).
also helps produce melanin,
Symptoms usually appear
the pigment responsible for
during childhood
hair and skin color.

III. NON-ESSENTIAL AMINO ACIDS:

 These can be synthesized by the body and may not be required in the diet
 These amino acids are derived from the carbon skeletons of lipids and carbohydrates during their
metabolism or from the Transamination of essential amino acids

-  Alanine is an amino acid

1. that is used to make proteins.
 - Fatigue. Poor endurance
It is used to break down
and strength. Weakness and
tryptophan and vitamin B-6.
muscle atrophy (shrinkage)
 - Alanine It is a source of energy for
Dizziness and faintness due
muscles and the central
to fluctuating blood sugar
nervous system. It strengthens
levels.Jun
the immune system and helps
the body use sugars.

 - Asparagine synthetase
 - Asparagine is needed to deficiency is a condition
produce many proteins but that causes neurological
2. also plays other roles. problems in affected
Asparagine helps to break individuals starting soon
down toxic ammonia within after birth. Most people
 - Asparagine Acid
cells, is important for protein with this condition have an
modification, and is needed unusually small head size
for making a certain molecule (microcephaly ) that
that transmits signals in the worsens over time due to
brain (a neurotransmitter). loss (atrophy) of brain
tissue.

3.  - Glutamic Acid  - Glutamic acid is an amino  - One of the most common

acid used to form proteins. In consequences of glutamic
the body it turns into acid deficiency is impaired
glutamate. This is a chemical brain function, low levels of
that helps nerve cells in the this amino acid can lead to
brain send and receive cognitive impairment,
information from other cells. memory loss, and other
 neurological disorders.
Moreover, glutamic acid
It may be involved in learning deficiency can also affect
and memory. the immune system's ability
to fight off infections and
diseases.

 - The functions of glutamine

are many and include:
substrate for protein
synthesis, anabolic precursor  - Glutamine deficiency, a
for muscle growth, acid-base common finding in severe
balance in the kidney, illness, has a negative
4. substrate for ureogenesis in influence on immune status,
the liver, substrate for hepatic protein metabolism, and
and renal gluconeogenesis, an disease outcome. In several
 - Glutamine
oxidative fuel for intestine studies, a close relationship
and cells of the immune between glutamine,
system, inter-organ nitrogen branched-chain amino acid
transport, precursor for (BCAA), and protein
neurotransmitter synthesis, metabolism was
precursor for nucleotide and demonstrated.
nucleic acid synthesis and
precursor for glutathione
production.

 - Glycine is precursor for a

 - glycine
variety of important
amidinotransferase
metabolites such as
deficiency is an inherited
glutathione, porphyrins,
5. disorder that primarily
purines, haem, and creatine.
affects the brain. People
Glycine acts as
with this disorder have mild
neurotransmitter in central
 - Glycine to moderate intellectual
nervous system and it has
disability and delayed
many roles such as
speech development. Some
antioxidant, anti-
affected individuals develop
inflammatory, cryoprotective,
autistic behaviors that affect
and immunomodulatory in
communication and social
peripheral and nervous
interaction.
tissues.

- One of the significant

consequences of proline
deficiency is impaired
collagen synthesis. Without
 - Proline plays important enough proline, the body
6. roles in protein synthesis and cannot produce enough
structure, metabolism collagen, leading to
(particularly the synthesis of weakened connective
arginine, polyamines, and tissues and increased risk of
 - Proline
glutamate via pyrroline-5- injury.
carboxylate), and nutrition, as
well as wound healing, Another consequence of
antioxidative reactions, and pro- line deficiency is
immune responses. impaired immune function.
A lack of proline can
weaken the immune
system's ability to defend
against harmful pathogens. 
7.  - serine plays an essential  - Congenital microcephaly,
role in a broad range of seizures and severe
cellular functions including psychomotor retardation are
protein synthesis, symptoms of serine
 - Serine neurotransmission, and folate deficiency and can be
and methionine cycles and treated with
synthesis of sphingolipids, supplementation of L-
phospholipids, and sulphur serine, sometimes combined
containing amino acids. with glycine.

 - It is involved in the
synthesis of proteins,
enzymes, and  - If deficient, it can lead to
neurotransmitters. Aspartic various health problems
8. acid also helps to regulate the such as fatigue, depression,
pH balance in the body by and impaired cognitive
acting as a buffer. function. Aspartic acid
- Aspartic Acid
Additionally, it aids in the deficiency can also affect
production of energy by the body's ability to
participating in the Krebs detoxify harmful substances
cycle. Aspartic acid has been and regulate blood sugar
linked to improved cognitive levels.
function and memory
retention

II. ENZYME CLASSIFICATION

 To systematize the nomenclature for enzymes the International Union of Biochemical has
grouped enzyme into six major classes:

SELECTED TYPE OF REACTION EXAMPLES

MAIN CLASSES
SUBCLASSES CATALYZED (EQUATION)

1.Oxidoreductases- catalyzed  a synthetically useful

Oxidases class of reactions where
Oxidation-reduction involving two hydrogen atoms are
substrate molecules    
removed from a substrate

Catalyze reduction
2CH2CH2 (g) + H2
reactions. A reduction
Reductases (g) → CH3CH3 (g)
reaction involves the gain
2FeCl3 (aq) + H2 (g)
  of electrons; it is usually
→ 2FeCl2 (aq) +
coupled to oxidation and
2HCl (aq)
termed a redox reaction

Dehydrogenase Dehydrogenases catalyze CH3CH2OH + NAD+

oxidation-reduction -> CH3COH
reactions involving (acetaldehyde) +
hydrogen and reductases NADH + H+
catalyze reactions in
which a substrate is
reduced. Transaminases
catalyze the transfer of
 amino group, and kinases
catalyze the transfer of a
phosphate group.

 transfer of phosphate
Kinases groups from high-energy,  
phosphate-donating
  molecules to specific
substrates.

Transaminases are the

enzymes which catalyze
2.Transferases the transfer of amino
group from α-amino acid
 catalyze transfer of functional
to α-keto acid. ALT
groups between two substrates 
enzyme catalyzes the
reaction between l-alanine
Transaminase and α-ketoglutarate to
form pyruvate and l-
glutamate. The pyruvate
reacts with 2,4-
dinitrophenylhydrazine in
the alkaline condition to
form a red-brown
complex.

 Dehydratase catalyses
dehydration and
isomerisation reactions by
 Dehydratases a mechanism that does
not involve metals or
  other cofactors, unlike the
majority of the enzymes  
3.Lyases that catalyse similar
reactions.
catalyze the addition of a group to
a double bond or the removal of a
group to create a double bond in a Decarboxylases it catalyzes both a
manner that does not involve decarboxylation and a
hydrolysis   transamination during its
normal catalytic cycle.

Adenine deaminase
(ADE) catalyzes the
 Deaminases conversion of adenine to
hypoxanthine and
ammonia.

4.Isomerases Racemaces
   
catalyze the conversion of a  
substrate into another compound
that is isomeric with it
  Mutases catalyze
reactions in which a
Mutases functional group is
transferred from one atom
 in a substrate to another.
Synthetases catalyze
reactions in which two
 
smaller molecules are
linked to form a larger
one.

Epimerases

 Synthetases catalyze
reactions in which two
smaller molecules are
Synthetases linked to form a larger
one. The first enzymes to  
5.Ligases   be discovered were
named according to their
They catalyze linking /bonding source or method of
together of two compounds. The discovery.
linking is coupled to the breaking
of phosphate from ATP.
Carboxylases (sensu
stricto) are enzymes that
Carboxylases catalyze the incorporation
of a CO2 molecule into an
organic substrate.

Proteases catalyze the

6.Hydrolases Proteases hydrolysis of proteins to
 catalyze the addition of a water polypeptides,  
  oligopeptides, and amino
molecule to a  bond to break
acids.

Carbohydrases the breakdown of

carbohydrates into simple
  sugars.

Lipases are versatile

enzymes that catalyze not
only hydrolysis but also
synthesis of
acylglycerides [1]. They
Lipases are active at the oil–water
  interface of emulsified
substrates [2], where the
interfacial composition
has been found to change
continuously during the
biocatalysis [3].
catalyze cleavage of the
Nucleases phosphodiester bonds in
nucleic acids for various
  genetic and biological
processes.
Phosphatases catalyze the
Phosphatases hydrolysis of a
  phosphomonoester,
removing a phosphate
moiety from the substrate.
Water is split in the
 reaction, with the -OH
group attaching to the
phosphate ion, and the H+
protonating the hydroxyl
group of the other product