AMINO ACIDS:

Structure and Properties

 All proteins are polymers of amino acids
 Proteins are composed of a number of
amino acids linked by peptide bonds.
 Although about 300 amino acids occur in
nature, only 20 of them are seen in human
body
 Most of the amino acids are alpha amino
acids ( except proline)
The general structural formula for an α amino acid
Classification of Amino Acids
I. Based on Structure:
A. Aliphatic amino acids
1. Monoamino monocarboxylic acid
 simple amino acids ( Glycine and Alanine)
 branched chain amino acids ( Valine, Leucine ,
Isoleucine)
 hydroxyamino acids ( Serine , Threonine )
 sulphur containing amino acids ( Cysteine, Methionine)
 amino acids with amide group ( Asparagine,
Glutamine)
 2. Monoamino dicarboxylic acid . Aspartic acid , Glutamic
acid
3. Dibasic monocarboxylic acid . Lysine, Arginine
B. Aromatic amino acids :
Phenylalanine , Tyrosine
C. Heterocyclic amino acids :
Tryptophan
D. Imino acid: Proline
E. Derived amino acids
1. Derived amino acids found in proteins:
 hydroxyl proline and hydroxyl lysine
 Gamma carboxylation of glutamic acids residues
of protein
2. Derived amino acids not seen in proteins ( non
protein amino acids)
 Ornithine, Citrulline , Homocysteine
3. Non alpha amino acids
 Gamma amino butyric acid ( GABA) is derived from
glutamic acid
 Beta alanine is a component of pantothenic acid
and co enzyme A.
Simple Amino Acids
Branched Chain Amino Acids
Hydroxyamino Acids
Sulfur Containing Amino Acids
Amino Acids with amide group
Dicarboxylic Acid
Dibasic monocarboxylic acid
Aromatic Amino Acids
Heterocyclic amino acid: Tryptophan
Histidine and Proline
Some derived amino acids
Based on Side Chain

A. Amino acids having non-polar side chains:

 include Alanine, Valine, Leucine,
Isoleucine,Methionine, Proline,
Phenylalanine and Tryptophan.
 are hydrophobic (water repellant) and
lipophilic.
 the parts of proteins made up of these
amino acids will be hydrophobic in nature.
B. Amino acids having uncharged or non-
ionic polar side chains:
 Glycine, Serine, Threonine,
Cysteine,Tyrosine, Glutamine and
Asparagine belong to this group.
 These amino acids are hydrophilic
in nature.
C. Amino acids having charged or ionic polar side chains (hydrophilic):

a. Acidic amino acids

 They have a negative charge on the R
group
 Aspartic acid and Glutamic acid.
 (Tyrosine is mildly acidic).
b. Basic amino acids
 They have a positive
charge on the R group
 Includes Lysine,
Arginine and Histidine.
Based on Metabolism
A. Purely ketogenic
 Leucine is purely ketogenic because it is converted to ketone bodies
B. Ketogenic and glucogenic:
 Lysine, Isoleucine,Phenylalanine, Tyrosine and Tryptophan are
partially ketogenic and partially glucogenic.
 During metabolism, part of the carbon skeleton of these
amino acids will enter the ketogenic pathway and the other part to glucogenic pathway
C. Purely glucogenic:
 All the remaining 14 amino acids are purely glucogenic as they enter only into the glucogenic
pathway.
Metabolic Fates of Amino acids
Based on Nutritional Requirements

A. Essential or indispensable
 The amino acids may further be classified according to their
essential nature for growth.
 Isoleucine, Leucine, Threonine, Lysine, Methionine,
Phenylalanine, Tryptophan, and Valine are essential amino
acids.
 Their carbon skeleton cannot be synthesized by human
beings and so preformed amino acids are to be taken in food
for normal growth. Normal growth and optimal health will
not occur, if one such amino acid is deficient in the diet.
B. Partially essential or
Semiessential
 Histidine and Arginine are semi-
indispensable amino acids.
 Growing children require them in
food. But they are not essential
for the adult individual.
C. Non-essential or Dispensable:
 non-essential, because their carbon skeleton can be synthesized by the
body.
 So we need not have to ingest these amino acids as such.
 However, they are also required for normal protein synthesis.
 The non-essential amino acids are Alanine,Asparagine, Aspartic acid,
Cysteine, Glutamine, Glutamic Acid, Glycine, Proline, Serine and Tyrosine.
 All body proteins do contain all the non-essential amino acids.
D. Conditionally essential amino acids:
 When a person is suffering from a moderate to severe chronic illness, person may lose the ability to
manufacture enough non-essential amino acids and thus require supplementation.
 Problems with digestion will also necessitate supplementation of “non-essential” amino acids.
 These amino acids are normally non-essential, but become essential during times of physiological
stress.
 Then these amino acids have to be taken in food or through supplements.
 These conditionally essential amino acids are Arginine, Glycine, Cysteine,Tyrosine, Proline, Glutamine
and Taurine.
"Any Help In Learning These Little Molecules Proves Truely
Valuable"
This stands for
Arginine, Histidine, Isoleucine, Leucine, Threonine, Lysine,
Methionine, Phenylalanine, Tryptophan and Valine in that order.
Arginine and Histidine are semi-essential amino acids; while
others are essential
Properties of Amino Acids

 Glycine, alanine, valine, serine, tryptophan, histidine and proline are sweet
in taste, leucine is tasteless , isoleucine and arginine are bitter
 Sodium glutamate is a flavoring agent.
 Aspartame, an artificial sweetener contains aspartic acid and
phenylalanine.
 All amino acids have high melting points (more than 200°C).
 All amino acids are soluble in water and alcohol (polar solvents); but
insoluble in non-polar solvents (benzene)
Ampholyte and Isoelectric Points

 Amino acids can exist as ampholytes or zwitterions (German word “zwitter” =

hybrid) in solution, depending on the pH of the medium.
 The pH at which the molecule carries no net charge is known as isoelectric
point or isoelectric pH (pI).
 In acidic solution, they are cationic in form and in alkaline solution they
behave as anions .
 At isoelectric point, the amino acid will carry no net charge; all the groups
are ionized but the charges will cancel each other.
 Therefore, at isoelectric point, there is no mobility in an electrical field.
 Solubility and buffering capacity will be minimum at isoelectric pH.
Optical Activity

 Amino acids having an asymmetric carbon atom exhibit optical activity.

 Asymmetry arises when 4 different groups are attached to the same carbon
atom
 Glycine is the simplest amino acid and has no asymmetric carbon atom .
 All others are optically active.
 The mirror image forms produced with reference to the alpha carbon atom,
are called D and L isomers.
 The L-amino acids occur in nature and are therefore called natural amino
acids.
 D-amino acids are seen in small amounts in micro-organisms
and as constituents of certain antibiotics such as Gramicidin-S,
Polymyxin, Actinomycin-D and Valinomycin, as well as bacterial cell
wall peptidoglycans.
 D-amino acids have multiple functions in bacteria, like synthesis of
cross-links in cell wall.
 Isoleucine and Threonine have 2 optically active centers and therefore
each has 4 diastereoisomers.
GENERAL REACTIONS OF AMINO GROUPS

I. Due to Carboxyl Group

A. Decarboxylation
 The amino acids will undergo alpha decarboxylation to form the corresponding
amine.
 some important amines are produced from amino acids.
 For example:
Histidine → Histamine + CO2
Tyrosine → Tyramine + CO2
Tryptophan → Tryptamine + CO2
Lysine → Cadaverine + CO2
Glutamic acid → Gamma amino butyric acid (GABA) + CO2
B. Amide Formation

 The-COOH group of dicarboxylic amino acids (other than alpha

carboxyl) can combine with ammonia to form the corresponding
amide.
 For example:
Aspartic acid + NH3 → Asparagine
Glutamic acid + NH3 → Glutamine
 These amides are also components of
protein structure.
 The amide group of glutamine serves as
the source of nitrogen
for nucleic acid synthesis.
II Due to Amino Group
A. Transamination
 The alpha amino group of amino acid can be
transferred to alpha keto acid to form the
corresponding new amino acid and alpha
keto acid .
 This is an important reaction in the body for
the interconversion of amino acids and for
synthesis of non-essential amino acids.
Transamination reaction
 B. Oxidative Deamination
 The alpha amino group is removed from the
amino acid to form the corresponding keto
acid and ammonia.
 In the body, Glutamic acid is the most
common amino acid to undergo oxidative
deamination.
C.Formation of Carbamino Compound

 Carbon dioxide adds to the alpha amino group of

aminoacids to form carbamino compounds.
 The reaction occurs at alkaline pH and serves as
a mechanism for the transport of carbon dioxide
from tissues to the lungs by hemoglobin

Hb—NH2 + CO2 → Hb—NH—COOH (Carbamino-Hb)

III. Due to Side Chains

A. Transmethylation
 The methyl group of Methionine,
after activation, may be transferred
to an acceptor, which becomes
methylated (see.
 Methionine + Acceptor → Methylated
Acceptor +Homocysteine
B. Ester Formation by the OH Group

 The hydroxy amino acids can form

esters with phosphoricacid. In this
manner, the Serine and Threonine
residues of proteins are involved in
the formation of phosphoproteins.
 Similarly, these hydroxyl groups can
form O-glycosidic bonds with
carbohydrate residues to form
glycoproteins.
C.Reaction of the Amide Group

 Theamide groups of Glutamine

and Asparagine can form N-
glycosidic bonds with
carbohydrate residues to form
glycoproteins
D. Reactions of SH Group

 Cysteine has a sulfhydryl (SH) group and it can form

adisulfide (S-S) bond with another cysteine residue.
 Thetwo cysteine residues can connect two polypeptide
chainsby the formation of interchain disulfide bonds or
links
 The dimer formed by two cysteine residues is sometimes
called Cystine or Dicysteine.
Amino acid Derivatives of Importance

 Gamma amino butyric acid (GABA, a derivative of glutamic acid) and

dopamine (derived from tyrosine) are neurotransmitters. GABA pentin can pass
blood brain barrier and can form GABA in brain.
 Histamine (synthesized from histidine) is the mediator of allergic reactions.
 Thyroxine (from tyrosine) is an important thyroid hormone.
 Cycloserine, a derivative of serine is an antituberculous drug.
 Azaserine inhibits reactions where amide groups are added, and so acts as an
anticancer drug.
 Histidine residues are important in the buffering activity of proteins.
 Ornithine and citrulline are derivatives of arginine and are essential for urea
synthesis.
End of Lecture!