JUST A SIMPLE PRESENTATION ON AMINO ACIDS.

1. BISMILLAHIR RAHMANIR RAHIM
WELCOME
To our
PRESENtaTIOn

2. A Presentation on
AMINOACID
to
netishkumarkundu
Lecturer,Dept. of pharmacy,
MBSTU
By
Rasna Sharmin Keya
Jarin Tasnim Itu Group: Api
Mehedi Hasan
Salman Istiak Sabbir
Saiful islam

3. AMINO ACID
• Amino acids are building blocks of proteins. Proteins are
composed of 20 different amino acid.
• Amino acids are organic compounds having an amino
group attached to a chain containing an acid group.
Amino acid derived from proteins have the amino group
on a-carbon that is the carbon atom next to the carboxyl
group.

4. • All 20 amino acids have common
structural features
• All amino acids have an amino group (-
NH3
+), a carboxylate (-COO-) group
and a hydrogen bonded to the same
carbon atom (the -carbon)
• They differ from each other in their side
chain called R group.
• R groups vary in structure, size and
electric charges and influence the
solubility of amino acids in water.
STRUCTURAL FEATURES OF AMINO ACIDS

5. CLASSIFICATION OF AMINO ACIDS
ACCORDING TO PARTS OF OUR BODY REQUIREMENTS,
AMINO ACIDS ARE TWO TYPES:-
1)ESSENTIAL AMINO ACID
2)NON-ESSENTIAL AMINO ACID

6. ESSENTIAL AMINO ACIDS
 Essential amino acids – cannot be synthesized by the body.
Therefore they must be present in our diet.
THERE ARE 8 TYPES OF ESSENTIAL AMINO ACID.
THEY NEED TO SUPPLIED IN DAILY DIET
1. LYSINE
2. LEUCINE
3. ISOLEUCINE
4. METIONINE
5. TRYPTOPHAN
6. PHENYLALANINE
7. THREONINE
8. VALINE

7. NON ESSENTIAL AMINO ACIDS
They are synthesized in our body. Hence they need not to
be consumed in the diet.
Alanine
Asparagine
Aspartate
Glutamate
Glutamine
Glycine
Proline
Serine
Cysteine
tyrosine

8. On the basis of nature of reaction in solution ,amino acids
are three types.
they are :-
1)ACIDIC AMINO ACID
2)BASIC AMINO ACID
3) NEUTRAL AMINO ACID

9. ACIDIC AMINO ACID
Acidic amino acid contain one amino group and two carboxyl groups. Two
amino acids have acidic these are aspartic acid or aspartate (asp) and
glutamic acid or glutamate (glu).

10. BASIC AMINO ACID
Basic amino acid contain two amino groups and one carboxyl group. Here
are three amino acids that have basic. These are arginine (arg), lysine
(lys), and histidine (his).

11. NEUTRAL AMINO ACID
Neutral amino acid:-it contain one amino group and one
carboxyl group.
For example: alanine, glycine

12. METHODOFPREPARATIONOFAMINOACID
1.By strecker method:
The strecker amino acid synthesis is an organic reaction used to
convert an aldehyde or ketone and a pri-mary amine or
ammonia to an α-amino acid using a metal cyanide, acid
catalyst, and water.

13. 2.By koop synthesis:-
Α- keto acids are treated with ammonia to form the
corresponding amine which on catalytic reduction yields an
amino acid.

14. PROPERTIES OF AMINO ACID
 Solubility: most of the amino acids are soluble in water and insoluble in
organic solvents.
 Melting point: melt at higher temperature
(above 200 c)
 Taste: sweet - glycine, alanine, valine
Tasteless – leucine
Bitter – arginine, isoleucine
 Optical activity: all the amino acids except glycine possess optical
isomers due to presence of asymmetric carbon atom.
Glycine

15.  Alanine and all other amino acids have an asymmetric carbon
at position 2 (the a-carbon atom). For this reason they all are
optically active and exist in D and L forms. Which are non
super-imposable mirror images.

16. CHEMICAL PROPERTIES
 A) reactions due to carboxylic group
1)amino acids form salts (-coona) with bases and estres (-COOR) with
alcohols.
2) deacarboxylation : amino acids undergo decarboxylation to
produce amines.
H2n-ch2-cooh + ba(oh)2 ch3-nh2 + baco3 + h2o
Glycine methylamine
3) reaction with ammonia : form amides
Aspartic acid + NH3 aspargamine
Glutamic acid + nh3 glutamine

17. REACTIONS DUE TO NH2 GROUP
1 ) Amino groups behave as bases and combine with acids
(eg.Hcl) to form salts.
2) reaction with ninhydrin
The a-amino acid react
With ninhydrin to form a
Purple, blue or pink colour
Complex.
Ninhydrin reaction is used
For the quantitative
Determination of amino
Acids and proteins.

18.  Oxidative demination :the amino acids undergo oxidative
deamination to liberate free ammonia.
 Transmethylation: Transfer of amino group from an amino acid
to a methyal group is called transmethylation

19.  Amino acids as ampholytes : amino acids contain both acidic (-COOH) and basic (-
NH2) groups. They can donate a proton and accept a proton. Hence they are also
called as ampholytes.
 Zwitter ions : amino acids also exist in zwitter ion form. Zwitter ion is a hybrid
molecule that contain both positive as well as negative ionic groups. Eg. Leucine
- AT ISOELECTRIC PH - CARRIES NO NET CHARGE

20. ISOELECTRIC POINT
Isoelectric point:-in acidic solution, an amino acid exist as a
positive ion and migrates toward the cathode.In basic solution
the amino acid exist as a negative ion and migrates toward the
anode. At a certain ph that is hydrogen ion concentration the
amino acid molecule would not migrate to either electrode and
exist as a a neutral dipolar ion. This ph is called the isoelectric
point of amino acid.

21. ISOELECTRIC POINT OF SOME AMINO ACID
ALANIN 6.1
VALINE 6.0
SERINE 5.7
THREONINE 5.6
ASPARTIC ACID 2.8
GLUTAMIC ACID 3.2
LYSINE 9.7
ARGININE 10.8

22. TRANSAMINATION
Definition:-Transamination as the name implies, refers to
the transfer of an amine group from one molecule to
another. This reaction is catalyzed by a family of enzymes
called transaminases. Actually, the transamination reaction
results in the exchange of an amine group on one acid with
a keto . New group on another acid.

23. BIOLOGICAL SIGNIFICANCE OF
TRANSAMINATION
• Transamination is used both for the catabolic as well as
anabolic processes.
• The resultant α-keto acid can be completely oxidized to
provide energy, glucose, fats or ketone bodies depending
upon the cellular requirement.
• Since it is a reversible process, it is also used for the
synthesis of non essential amino acids.

24. IMPORTANCE OF AMINO ACIDS
• Amino Acids are the building blocks of proteins
• They are important in many biological molecules,
such as forming parts of coenzymes
• Or as precursors for the biosynthesis of molecules
such as heme
• They are critical to life, and have many functions
in metabolism

25. THANKS
TO
ALL