Amino Acids

AMINO ACIDS
Introduction
Living cells produce an impresivve variety of
macromolecules
Macromolecules are biopolymers constructed of
monomer units or building blocks
Eg. Nucleic acids : the monomer units are nucleotides
Polysaccharides : the monomer units are sugar
derivatives
protein : the monomer units are amino acids
(May substances other than amino acids attached to
them)

Macromolecules serve as :
- structural components
- Biocatalyst
- Hormones
- Receptors
- Repositories of genetic information

B. Biomedical importance
Glycine & glutamic acid : involved in the transmission of
impulses in the nervous system
Essential amino acids : must be supplied in the diet, since our
bodies cannot synthesize them in amount adequate to
support growth (infants) or to maintain health (adults)
Decarboxylation of certain amino acids produces
the corresponding amine
histamin
gamma amino butyrate (GABA) -- have important
biologic function

A number of deseases are due to abnormalities of the

transport of amino acids into cells --
are characterized by the presence of greatly increased
amounts of one or more amino acids in the urine :
as the aminoacidurias
FUNCTIONAL GROUPS IN AMINO ACIDS
- Amino groups (NH2) : proton aceptors
- Carboxylic acid groups (COOH) : proton donors

- Alfa amino acid : both are attached to the same carbon

atom
- R- CH- COOH
!
- NH2
- About 300

amino acids occur in the nature only 20 of

these occur in the proteins
- Complete hydrolysis of proteins produces 20-L-alfaamino acids
- All 4 groups linked to the alfa carbon atom of amino
acids are different groups about the alfa-carbon atom
confer optical activity on amino acids exception of
glycine (R= a hydrogen atom)

Optical activity : the ability to rotate the plane of plane

polarized light
Although some amino acids found in protein sare
dextrorotatory and some levorotatory at pH 7.0
-- all have the absolute configurations of L-gliseraldehyde
and hence are L-alfa-amino acids

Protonic equilibria of amino acid

R-COOH === R-COO- + H+
R-NH3+ <=====R-NH2 + H +
R-COOH & R-NH3+ : proton donors /acidic
R-COO- & R-NH2

: proton acceptors

At pH of blood plasma : 7.4

the intracellular space 7.1
Carboxyl groups exist as carboxylate ions, R-COO-

Amino groups are exist as protonated form, R-NH3+

pKa = - log Ka
Ka : relative acid strengths of weak acid/acid diss. Constant
pKa values for alfa- carboxyl : 2
alfa-amino group : 10
The net charge of amino acid depends upon
The pH/proton concentration, of the surrounding sol.
Isoelectric pH (pI) : is the pH midway between pK values on
either side of the isoelectric

Ex. Alanine : pK1 (R-COOH) : 2.35

pK2 (R-NH3-)

: 9.69

pI alanine is : 0.5 (2.35 + 9.69) = 6.02

the basic of the relative polarities of their R groups

1. Non polar :
alanine isoleusine
Leucine methionine
Phenylalanine proline
Tryptophan
valine

2. Polar
Arginine
Cysteine
Glycine
Serine

asparagine aspartic acid

glutamic acid
glutamine
histidine
lysine
threonine tyrosine

with aliphatic side chains Classification

-glycine (Gly) aminoacetic acid
- Alanine (Ala) 2-aminopropanoic acid
- Valine (Val) 2-amino-3-methylbutanoic acid
- Leucine (Leu) 2-amino-4-methylpentanoic acid
- Isoleucine (Ile) 2-amino-3-methyl

with side chains containing hydroxylic groups

- serine (Ser) 2-amino-3-hydroxypropanoic acid
- Threonine (Thr) 2-amino-3-hydroxybutanoic acid

- with side chains containing sulfur atoms

- Cysteine (Cys) 2-amino-3-mercaptopropanoic acid
- Methionine (Met) 2-amino-4-(methylthio)butanoic acid

- with side chains containing acidic groups or

their amides
-

Aspartic acid (Asp) Aminosuccinic acid

Asparagine (Asn) 2-aminosuccinamic acid
Glutamic acid (Glu) 2-aminoglutaric acid
Glutamine (Gln) 2-aminoglutaramic acid

with side chains containing basic groups

-

Arginine(Arg) 2-amino-5-guanidovaleric acid

Lysine (Lys) 2,6-diaminohexanoic acid
Hydroxylysine 2,6-diamino-5-hydroxyhexanoic acid
Histidine (His) 2-amino-1H-imidazole-4-propanoic acid

- containing aromatic rings

- Phenylalanine (Phe) 2-amino-3-phenylpropanoic acid
- Tyrosine (Tyr) 2-amino-3-(4-hydroxyphenyl)propanoic
acid
- Tryptophan (Trp) 2-amino-3-(3-indolyl)propanoic acid

- containing amino acids

- Proline (Pro) 2-pyrrolidinecarboxylic acid
- 4-hydroxyproline (Hyp) 4-hydroxy-2-pyrrolidine
carboxylic acid

 alfa amino acids not present in protein but

essential in mammalian metabolism
1. Homocysteine (2-amino-4-mercaptobutanoic acid)
An intermediate in methionine biosynthesis

2. Cysteinesulfinic acid (1-amino-2-sulfinopropanoic acid)

an intermediate in cysteine catabolism
3. Homoserine (2-amino-3-hydroxybutanoic acid)
an intermediate in threonine,aspartate and methionine
metabolism
4. Ornithine (2,5-bisaminopentanoic acid)
intermediate in threonine,aspartate and methionine
metabolism

 5. Citrulline(2-amino-5-ureidopentanoic acid)
Intermediate in the biosynthesis of urea
6. Argininosuccinic acid :

Intermediate in the biosynthesis of urea

7. DOPA (3,4-dihydroxyphenylalanine)
Precursor of melanin
8. 3-monoiodotyrosine :precursor of thyroid hormones
9. 3,5-diiodotyrosine : precursor of thyroid hormones
10.3,5,3-triiodothyrosine (T3) :precursor of thyroid hormones

11. Thyroxine (3,5,35 tetraiodothyronine =T4) ; precursor of

thyroid hormones

 alfa-amino acids not occur in proteins but perform

essential function in non mammalian metabolism
1. Alfa-gama-diaminobutyric acid
In polymyxin antibiotics
2. 2,3-diaminosuccinic acid :
excreted by Streptomyces rimosus which produces oxytetracycline
3. Alfa-amino adipic acid (2,aminoadipic acid )
intermediate of lysine biosynthesis by yeast
4. 2,6-diaminopimelic acid :
bacterial cell walls; intermediate of lysine biosynthesis by bacteria
5. 2,3-diaminopropanoic acid
in the antibiotic viomycin
6. Saccharopine : intermediate of lysine biosynthesis by yeast and
Neurospora

 Amino acids with non alfa-amino groups

important functions in mammalian
metabolism
1. Beta-alanine (2-aminopropanoic acid) :
Part of coenzyme A and of the vitamin pantetheine
2. Taurine (2-aminoethylsulfonic acid) :
Occurs in bile combined with bile acids
3. Gama-aminobutiric acid(3-aminobutanoic acid)
Formed from glutamate in brain tissue
4. Beta-aminoisobutyric acid (2-methyl-3-aminopropanoic
acid) :
End product of pyrimidine catabolism

 A variety of separatory techinques

- Chromatography
- paper chromatography
- thin layer chromatography
- ion exchange chromatography
- High-voltage electrophoresis

PROTEIN
-protein are high-molecular weight polypeptides
MW 8.000-10.000
Play a central role in cel function and cell structure
Analyces of certain proteins and enzyme of the
blood are used for diagnostic purposes

 Classification
- by solubility
albumins, globulins, protemine,
histone
- by overall shape
1. globular proteins : axial ratios less
than 10 not over 3-4
albumins, globulins, insulin

2. Fibrous proteins : axial ratios greater than 10

keratin, myosin, collagen, fibrin

- by function
-

Catalytic role : enzymes

Contraction : actin, myosin
Gene regulation : histones
Hormonal role : insulin
Protection : fibrin, Ig, interferon
Regulatory role : calmodulin
Structural role : collagen, elastin, keratins
Transport : albumin, Hb, lipoproteins, transferrin

 The bonds that stabilisize proteins

Disulfide bonds
Peptide bonds
Hydrogen bonds : formed between the hydrogen and
oxygen atoms of the peptide bonds themselves
Hydrophobic interactions
Electrostatic bonds ; formed between N-terminal and Cterminal residues

 Protein structure
1. Primary structure
: sequences amino acids
2. Secondary structure : alfa helix
3. Tertiary structure : consist of disulfides bonds
4. Quarternary structure : consist of 2 or more
polypeptide chains united by forces other than covalent
bonds