AMINO ACIDS

Structural Properties, Classification, Acid

Base Buffer Properties
 Learning Objectives

• Count all amino acids

• Define amino acid structure
• Explain characteristics of amino acids
• Explain structure of glutathione
• Explain uncommon and nonstandard amino acids
• Define functional groups of amino acids
• Define glucogenic, ketogenic, essential, conditionally essential amino
acids
• Define isomerism concept
• Explain importance of isomers
• Books suggestion; Harper’s Illustrated Biochemistry and Lippincott Illustrated
Rewiews Biochemistry
• More than 300 amino acids occur in nature
• Only 20 of them are coded for by DNA in the cell
• All of them except Proline are Alpha Amino acids
• Proline is an imino acid
• Amino group is attached to the same carbon atom to which
Carboxyl group is attached
 The 21 st Amino acid
‘’Selenocysteine’’

• Synthesized from Serine and Selenium while Serine is

attached to transfer RNA
• Found in several proteins such as Glutathione peroxidase
• Glutathione peroxidase is one of the most important
Antioxidant enzymes
 The 22 nd Amino acid
‘’Pyrrolysine’’

• Found in a few proteins in several methanogenic (Methane

producing) archaea and in one known bacterium
• Plays a role in methane biosynthesis
 Lehninger
Principles of Biochemistry
• At physiologic pH (Approximately 7.4);
• Carboxyl group is dissociated forming Negatively
charged Carboxylate group and Positively charged
Amino group
• In proteins; Carboxyl group of one amino acid is linked to
Amino group of the next amino acid
• Forms an amide (PEPTIDE) bond
• Water is eliminated during this reaction ( Dehydration
reaction)
 Amino acid units in a peptide chain are
Known as Amino acid residues

• Proteins contain between 50 and 2000 amino acid residues

Purslane
 Glutathione
One of The Most Important Antioxidant

• Consists of 3 amino acid residues

• Tripeptide
• Glutamate + Cysteine + Glycine
• Side chains ;
• Dictates the role an amino acid plays in a protein
 Simple Amino Acids

• Glycine ; The simplest amino acid

• Collagen ; The most abundant protein in our body
• In Collagen protein ; Every 3 rd of amino acid is Glycine
 Simple Amino Acids

• Alanine;
• Alanine - Glucose Cycle between Muscle and Liver
• Primarily oxidized in Skeletal muscle, whereas the other
amino acids catabolized in Liver
 Hydroxyl Containing Amino Acids

• Hydroxyl group of Serine, Threonine and rarely, Tyrosine

can serve as an attachment site for Phosphate group
• Phosphorylation/ Dephosphorylation reactions are very
important in the regulation of enzyme activities in
Metabolism
• Hydroxyl group of Serine or Threonine, can serve as an
attachment site for oligosaccharide chains in Glycoproteins
Sulfur Containing Amino Acids
• The side chain of Cysteine contains Thiol= (-SH) group
• Thiol group is important component of the active site
of many enzymes
Sulfhydryl (= SH =Thiol) groups of 2 Cysteine
Produce Disulfide bond (-S-S-)

• 2 Cysteine amino acids form Cystine

 Amino Acids With Amide Group

• Amide group of Asparagine can serve as an attachment

site for oligosaccharide chains in Glycoproteins
 Amino Acids With Amide Group

• Glutamine is an energy source for intestinal cells

Acidic Amino Acids
 MSG= Mono Sodium Glutamate
Food Additive ‘’Chinese Salt’’
• Flavoring agent
 www.pubmed.com
J Biomed Sci 2015.Monosodium glutamate-induced
oxidative kidney damage and possible mechanisms:
a mini-review
• Animal studies suggest that chronic Mono
Sodium Glutamate (MSG) intake induces
Kidney damage by oxidative stress
Basic Amino Acids
Aromatic Amino Acids
 Proline

• An imino acid not Amino acid

• Because its side chain loops back to form a five-membered
ring with its amino group,
• Which causes proline to produce kinks in the polypeptide
backbone
• Collagen is rich in Proline
 Amino acid side chains contribute
Both Charge and Hydrophobicity to Proteins
• Amino acid composition of a peptide chain has a profound
effect on its physical and chemical properties
• Proteins rich in Aliphatic or Aromatic amino groups are
relatively insoluble in water and are likely to be found in
cell membranes
• Proteins rich in polar amino acids are more water soluble
Amino Acids Can Act as Acids and Bases
• Amino and carboxyl groups of amino acids, along with the
ionizable R groups of some amino acids, function as Weak
acids and bases
• Amino acids with side chain;
• Acidic (Glu, Asp) or Basic (Lys, His, Arg) groups will confer
charge and buffering capacity to a protein
• Charge on the protein is dependent primarily on the side
chain functional groups of amino acids
• Proteins are an important part of the buffering capacity of
cells and biological fluids, including blood
 Isoelectric Point (= pI)
‘’pH at which an amino acid is electrically NEUTRAL’’

• Charge on an amino acid depends on pH

• Isoelectric point (pI) is the pH at which an amino
acid is electrically neutral
• In which the sum of the positive charges equals
the sum of the negative charges
 Principle of Isoelectric Focusing Technique

• Proteins with varying isoelectric points will migrate in the

presence of a pH gradient and electric field until the net
charge of a protein is zero, in which migration will cease
• The balance between acidic and basic side chains in a protein
determines its isoelectric point (pI) and net charge in solution
• Proteins rich in Lysine and Arginine are basic in solution and
have a positive charge at neutral pH
• Acidic proteins, rich in Aspartate and Glutamate have a
negative charge
• Because of their side chain functional groups;
• All proteins become more positively charged at acidic pH and
more negatively charged at basic pH
 Uncommon Amino Acids
• 4-Hydroxyproline, a derivative of Proline, and 5-Hydroxylysine,
derived from Lysine; Found in Collagen, a fibrous protein of
connective tissues
• 6-N-Methyllysine; a constituent of Myosin, a contractile
protein of muscle
• Gamma carboxyglutamate; Found in Blood-clotting protein
Prothrombin and in Certain other proteins that bind Ca2+ as
part of their biological function
• Desmosine; a derivative of 4 Lysine residues, which is found in
the fibrous protein Elastin
 Uncommon Amino Acids
• Some amino acid residues in a protein may be modified
transiently to alter the protein’s function
• Addition of Phosphoryl, Methyl, Acetyl, Adenylyl or ADP-
ribosyl to particular amino acid residues can increase or
decrease a protein’s activity
• Phosphorylation is a particularly common regulatory
modification
 Non- standard Amino acids

• Produced from Glutamate

• Acts as Neurotransmitter
 Non-standard Amino acids

• Ornithine and Citrulline ; Arginine derivatives, essential for

UREA synthesis
 Non- standard Amino acids

• Thyroxine = Thyroide hormone = T4

 Non- standard Amino acids

• SAM = S- Adenosyl Methionine ; Methyl Donor

 Non- standard Amino acids

• Homocysteine
• Homocysteinemia increases Atherosclerosis risk
Non Alpha Amino Acids
 Non- standard Amino acids

• Beta Alanine; In Coenzyme A structure

• Acetyl Coenzyme A; Common product of
metabolism of proteins, carbohydrates and lipids
 Non- standard Amino acids

• Taurine; In structure of Bile acids

Special Groups in Amino Acids

• Arginine has Guanidino group

 Special Groups in Amino Acids
• Phenyl alanine has Benzene group

• Tyrosine has Phenol group

 Special Groups in Amino Acids
• Trytophan has Indole group
 Special Groups in Amino Acids
• Histidine has Imidazole group
 Classification of Amino Acids
Based on Metabolism
• 1. Glucogenic ; Convertible to Glucose
• 2. Ketogenic; Convertible to Ketone bodies such
as Acetone
• 3. Both Glucogenic and Ketogenic
 Purely Ketogenic Amino Acids
• Leucine
• Lysine
• Essential amino acids cannot be produced by the body and
must be present in the diet and necessary for normal body
functions
• Non-essential amino acids can be produced by the body and
are therefore not required as part of the diet
 Conditionally Essential amino acids

• Can be produced by the body, but at rates lower than

certain conditional requirements (e.g. During Pregnancy
or Infancy)– they are essential at certain times only
• Pregnants and Growing children need them in food
• Not essential for Adults
• Moderate or Severe illness and Digestion disorders
necessiate Supplementation of them
 Isomer

• Each of 2 or more compounds with the same formula but

• A different arrangement of atoms in the molecule and
• Different properties
Chiral Carbon (= Optically Active Carbon) Atom

• Attached to 4 Different chemical groups

• Amino acids have Chiral carbon atoms EXCEPT
Glycine
• Nonsuperposable mirror
images of each other
(= Enantiomers)
 Stereoisomerism in α-amino acids

• Nearly all biological compounds with a chiral center occur

naturally in only one stereoisomeric form, either D or L
• 2 Stereoisomers of Alanine; L- Alanine and D- Alanine
• Cells are able to specifically synthesize L isomers of amino
acids because;
• Active sites of enzymes are asymmetric, causing the
reactions they catalyze to be stereospecific
• Amino acid residues in protein molecules are exclusively
L- stereoisomers
• D- Amino acids are found in some antibiotics and
in bacterial cell wall
 Importance of Isomers
‘’Thalidomide Tragedy’’
Aminoacidemia = Blood Amino Acid
Aminoaciduria = Urine Amino Acid
Lippincotttt’s Illustrated Reviews Biochemistry