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AMINO ACIDS

Abhishek Sharma
B.Pharmacy 5th sem
Shoolini university
Amino acids

• 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.

• R group may be hydrogen, aliphatic group, or aromatic ring.
CLASSIFICATION (ON THE BASIS OF
STRUCTURE)


Amino acids are classified as neutral, acidic, or basic according
to no of amino acids and carboxyl group in the molecule.



1) Neutral amino acids - contain one amino acid and one
carboxyl group
R
C
COOH



NH2
2) Acidic amino acids - contain one amino group and two
carboxyl group
HOOC

CH
NH2

COOH
3) Basic amino acids – contain two amino groups and one
carboxyl group.
H2N

CH
NH2

COOH
CLASSIFICATION – ON THE BASIS OF POLARITY
1) Non polar amino acids – the are also referred to as hydrophobic
(water hating) They have no charge on R group.
Glycine (Gly)

Methionine (Met)

Alanine (Ala)
Phenylalanine (Phe)
Valine (Val)

Tryptophan (Trp)
Leucine (leu)

Isoleucine
(Ile)
2) POLAR AMINO ACIDS WITH NO CHARGE ON R GROUP
They carry no charge on R group. They possess groups such
as hydroxyl, sulfhydril and amide.
Serine (Ser)

Threonine (Thr)

Tyrosine (Tyr)

Cysteine (cys)

Asparagine (Asn)

Glutamine (Gln)
3) POLAR AMINO ACID WITH POSITIVE R GROUP


Lysine (Lys)

Arginine (Arg)

Histidine (His)

4) Polar amino acid with negative R group
Aspartic acid (Asp)

Glutamic acid (Glu)
CLASSIFICATION ON THE BASIS OF NUTRTION


Eesential amino acids – cannot be synthesized by
the body. Therefore they must be present in our
diet.
Arginine*
Histidine*
Isoleucine
Leucine
Valine

Lysine
Methionine
Threonine
Phenylalanine
Tryptophan

* Can be synthesized by adults but not by growing
children. They are also called as semi essential
amino acids.


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
CLASSIFICATION ON THE BASIS OF METABOLIC
FATE


1) Glycogenic amino acid – these amino acids
serve as a precursor for the formation of glucose or
glycogen.
eg. alanine, aspartate, glycine, methionine etc.

2) Ketogenic amino acid – fat can be synthesized
from these amino acids.
eg. Lucine and lysine
PROPERTIES OF AMINO ACIDS


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



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.
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

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

glycine

CH3-NH2 + BaCO3 + H2O

methylamine

3) Reaction with ammonia : form amides
aspartic acid + NH3
glutamic acid + NH3

aspargamine
glutamine
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.


Oxidative deamination :The amino acids undergo
oxidative deamination to liberate free ammonia.



Transmethylation: transfer of amino group from an
amino acid to a keto group is called
transmethylation
REFERENCE:
Biochemistry – u. satyanarayana
 Advanced organic chemistry – bahl n bahl


Thank you

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Amino acids abhishek sharma

  • 1. AMINO ACIDS Abhishek Sharma B.Pharmacy 5th sem Shoolini university
  • 2. Amino acids • 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. • R group may be hydrogen, aliphatic group, or aromatic ring.
  • 3. CLASSIFICATION (ON THE BASIS OF STRUCTURE)  Amino acids are classified as neutral, acidic, or basic according to no of amino acids and carboxyl group in the molecule.  1) Neutral amino acids - contain one amino acid and one carboxyl group R C COOH  NH2 2) Acidic amino acids - contain one amino group and two carboxyl group HOOC CH NH2 COOH
  • 4. 3) Basic amino acids – contain two amino groups and one carboxyl group. H2N CH NH2 COOH
  • 5. CLASSIFICATION – ON THE BASIS OF POLARITY 1) Non polar amino acids – the are also referred to as hydrophobic (water hating) They have no charge on R group. Glycine (Gly) Methionine (Met) Alanine (Ala) Phenylalanine (Phe) Valine (Val) Tryptophan (Trp) Leucine (leu) Isoleucine (Ile)
  • 6. 2) POLAR AMINO ACIDS WITH NO CHARGE ON R GROUP They carry no charge on R group. They possess groups such as hydroxyl, sulfhydril and amide. Serine (Ser) Threonine (Thr) Tyrosine (Tyr) Cysteine (cys) Asparagine (Asn) Glutamine (Gln)
  • 7. 3) POLAR AMINO ACID WITH POSITIVE R GROUP  Lysine (Lys) Arginine (Arg) Histidine (His) 4) Polar amino acid with negative R group Aspartic acid (Asp) Glutamic acid (Glu)
  • 8. CLASSIFICATION ON THE BASIS OF NUTRTION  Eesential amino acids – cannot be synthesized by the body. Therefore they must be present in our diet. Arginine* Histidine* Isoleucine Leucine Valine Lysine Methionine Threonine Phenylalanine Tryptophan * Can be synthesized by adults but not by growing children. They are also called as semi essential amino acids.
  • 9.  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
  • 10. CLASSIFICATION ON THE BASIS OF METABOLIC FATE  1) Glycogenic amino acid – these amino acids serve as a precursor for the formation of glucose or glycogen. eg. alanine, aspartate, glycine, methionine etc. 2) Ketogenic amino acid – fat can be synthesized from these amino acids. eg. Lucine and lysine
  • 11. PROPERTIES OF AMINO ACIDS  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 
  • 12.  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.
  • 13. 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 
  • 14. 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 glycine CH3-NH2 + BaCO3 + H2O methylamine 3) Reaction with ammonia : form amides aspartic acid + NH3 glutamic acid + NH3 aspargamine glutamine
  • 15. 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.
  • 16.  Oxidative deamination :The amino acids undergo oxidative deamination to liberate free ammonia.  Transmethylation: transfer of amino group from an amino acid to a keto group is called transmethylation
  • 17. REFERENCE: Biochemistry – u. satyanarayana  Advanced organic chemistry – bahl n bahl  Thank you