Introduction to Amino Acids

Introduction to Amino Acids

a. Definition
Amino acids are the building blocks of proteins
As the name implies, they contain an amino group and a carboxylic acid groups
Only 20 amino acids are found in the body, most of which are L-isomers
Amino acids are zwitterions, meaning, they contain a positive and a negative charge. Unionized amino acids do not actually
exist in any form
Amino acids are amphoteric; they may act as a base or as an acid
b.

Structure
All amino acids have five basic subparts: alpha carbon, an amino group, carboxyl group, Hydrogen group, and a variable
group (aka side chain/prosthetic group)
The side chain of an amino acid determines the property of that amino acid

AMINO ACID UTILIZATION

Build new tissue protein
Replace old tissue protein
Synthesize peptide hormones
Donate amino group for synthesis of other amino acids
Catabolize C skeleton for energy (~ 10% energy from amino acids)
Synthesize nucleotides
Synthesize neurotransmitters, amino acid derived hormones
Replace hemoglobin, synthesize heme (lifetime ~ 4 months)
Synthesize enzymes (lifetime ~ hours to day)
A. Classification of Amino Acids
a. Building Stones vs. Non-building stone Amino Acids
Building Stones
Glycine
Alanine
Valine
Leucine
Isoleucine
Hydroxylysine

Serine
Threonine
Phenylalanine
Tyrosine
Iodogorgic Acid*
Arginine

Thyroxine*
Tryptophan
Proline
Hydroxyproline
Cystine*
Histidine

Methionine
Aspartic Acid
Glutamic Acid
Hydroxyglutamic acid*
Lysine

H
H2N C COOH
R
Non-building stones
Amino butyric acid
Canavanine
Citrulline

Homocystine
Dkenkolic acid
Lanthionine

Biochemistry Lecture Notes

Prepared by: Jonathan M. Barcelo, BS Bio, BSN, RN

Dibromotyrosine
Dihydroxyphenylalanine
Hydroxyvaline

Norvaline
Norleucine
Ornithine

b.

According to Molecular Structure

1. Monoamino-monocarboxylic
2. Monoamino-dicarboxylic
3. Diamino-monocarboxylic
4. Diamino-dicarboxylic
5. Heterocyclic

c.

According to Polarity
Non-polar
Leucine (Leu, L)
Alanine (Ala, A)
Proline (Pro, P)
Valine (Val, V)

Polar, Uncharged
Glycine (Gly, G)
Serine (Ser, S)
Asparagine (Asn, N)
Glutamine (Gln, Q)

Polar, Acidic
Aspartic Acid (Asp, D)
Glutamic Acid (Glu, E)
Methionine (Met, M)
Tryptophan (Trp, W)
Phenylalanine (Phe, F)
Isoleucine (Ile, I)
Threonine (Thr, T)
Cysteine (Cys, C)
Tyrosine (Tyr, Y)
Histidine (His, H)

Polar, Basic
Lysine (Lys, K)
Arginine (Arg, R)

Ketogenic vs. Glucogenic

e.

Essential vs. Non-essential

Essential amino acids, also called limiting amino acids, are those that cannot be produced in our body and therefore have to
be obtained from food sources. There are 8 (or 9) essential amino acids.

d.

Functions of essential amino acids

1.

Tryptophan: Necessary for the synthesis of neurotransmitter serotonin. It helps relieve migraine and depression.

2.

Tyrosine: Is precursor of dopamine, norepinephrine and adrenaline. It enhances positive mood. It is also antioxidant.

3.

Valine: Essential for muscle development. Side effects of high levels of valine in the body include hallucinations.

4.

Isoleucine: Necessary for the synthesis of hemoglobin, major constituent of red blood cells.

5.

Leucine: Beneficial for skin, bone and tissue wound healing. It promotes growth hormone synthesis.

6.

Lysine: Component of muscle protein, and is needed in the synthesis of enzymes and hormones. It is also a precursor for L-carathine which is
essential for healthy nervous system function.

7.

Methionine: Is antioxidant. It helps in breakdown of fats and aids in reducing muscle degeneration. It is also good for healthy skin and nail.

8.

Phenylalanine: Beneficial for healthy nervous system. It boosts memory and learning. It may be useful against depression and suppressing
appetite.

9.

Threonine augments collagen and tooth enamel

Properties of Amino Acids

1. Crystalline Structures
Most amino acids assume cystlline shapes
Biochemistry Lecture Notes
Prepared by: Jonathan M. Barcelo, BS Bio, BSN, RN

2.

3.

4.

5.

Stereochemistry
- With the exception of Glycine, all amino acids obtained from hydrolysis of proteins under sufficiently mild conditions show
optical activity they can rotate the plane of polarization of plane-polarized light light in a polarimeter
- Factors affecting optical activity of proteins:
a. Concentration of the amino acid itself
b. pH of its solution
c. nature of the solvent
d. presenceof other electrolytes
e. temperature

6.

Solubility
- Most amino acids are soluble in polar solvents such as water and ethanol but insoluble in non-polar solvents such as
hexane, benzene or ether
Ultraviolet Absorption Spectrum
- aromatic amino acids tryptophan, tyrosine, histidine and phenylalanine absorb UV light
- Above 240 nm, most of the ultraviolet absorption of proteins is due to their tryptophan content
High Melting points
- Implication: presence of charged group, high energy needed to disrupt the ionic forces maintaining the crystal lattice.
Usually, the melting points are above 200oC
Acid-base properties
- dipolar ions = zwitterions
- When a crystalline amino acid is dissolved in water, it can either act as an acid or base
- According to Bronsted-Lowry theory, an acid is a proton donor and a base is a proton acceptor
- Substances having this property is called AMPHOTERIC and are called AMPHOLYTES (amphoteric electrolytes)

Note: D- and L- refers to the configuration, (+) means dextrorotation, (-) means levorotation
Note: Such compounds which can exist in right-handed or left-handed forms are called Chiral compounds.This phenomenon of stereoisomerism is also
called CHIRALITY (handedness). Optical activity is expressed quantitatively expressed as SPECIFIC ROTATION.

Other Properties
1. Amphoteric Zwitterions/ Amphions
- it acts either as an acid or as a base
- amino acids are amphiprotic;
sources of H+
a. COOH group
b. Protonated amine group of NH3 +
c. SH group
d. Guanidium moiety of Arginine
e. Protonated Nitrogen of the
heterocyclic ring of Arginine
f. Phenolic OH of Tyrosine
2. Isoelectric Point
- At a certain pH, amino acids behave as both
acids or bases; the net electric charge is
neutral, because the negative charges are
equal to the positive charges
3. Salt Formation amino acids react with HCl and NaOH to
form salts
Equation:
4.

5.

Esterification alcohol reacts with the carboxyl group to

form esters
Equation:
Liberation of Nitrogen the nitrous acid reaction causes
the amino group to liberate Nitrogen; not given by proline,

Biochemistry Lecture Notes

Prepared by: Jonathan M. Barcelo, BS Bio, BSN, RN

hydroxyproline, and imino group; measures free amino

groups in proteins
Equation:
6.

Formaldehyde reacts to mask the amino group to lose

the basic/ alkaline property of amino acids
Equation:

7.

Methylation amino groups can be methylated

Equation:

8.

Amino group can be acetyated.

Equation:

9.

Acyl halide formation

Equation:

10. Formation of Primary amines

Equation:
11. Dehydration causes amino acids to react with each other
in a ring formation, known as diketopiperazine ring
Equation:

12. Ionization of R groups

Equation:

16. Schiff Base Formation

Equation:

13. Oxidation of thiol groups

Equation:

References:

Understanding Pathophysiology by Huether and Mc Cance,

Biochemistry by Lehninger, Principles of Anatomy and Physiology by Tortora
and Grabowski, Introduction to Organic and Biochemistry by Bettleheim,
Harpers Biochemistry

14. Mercaptan formation

Equation:
15. Carbamoylation
Equation:

NOTE: UNDERSTAND WHAT YOU ARE REVIEWING!!!

Biochemistry Lecture Notes

Prepared by: Jonathan M. Barcelo, BS Bio, BSN, RN