Amino Acids

S Maloy, San Diego State University, San Diego, CA, USA

© 2013 Elsevier Inc. All rights reserved.

This article is a revision of the previous edition article by B Willis, P A Lessard, A J Sinskey, volume 1, pp 54–56, © 2001, Elsevier Inc.

Glossary supplied in the diet. There are nine essential amino acids
Chiral An asymmetric molecule that cannot be for humans: histidine, isoleucine, leucine, lysine,
superimposed on its mirror image. methionine, phenylalanine, threonine, tryptophan, and
Essential amino acids Amino acids that cannot be valine.
synthesized by an organism and therefore must be

Introduction maintaining cell shape to elegant and delicate enzymatic

machines that carry out highly regulated chemical reactions.
Amino acids are a class of important biomolecules that con­
tain both amino groups ð−NH3 þ Þ and carboxylate groups
(–COO−). In most contexts, the term ‘amino acids’ refers
to the α-amino acids, so-called because both the amino
Sources and Uses of Amino Acids
and carboxyl groups are attached to the α-carbon of the
Plants and many bacteria synthesize all 20 of the amino acids
structure depicted in Figure 1(a). However, other types of
listed in Figure 2. Amino acids are synthesized from a variety of
amino acids are encountered in nature, such as the
primary metabolites in living cells. However, vertebrates,
β-amino acids, in which the amino and carboxyl groups
including humans, are only able to manufacture a subset of
are attached to different carbons in the backbone
(Figure 1(b)). these amino acids. Hence, they must obtain the remainder of
All α-amino acids (with the exception of glycine) have four their amino acids from their diet. Amino acids that must be
different substituents attached to the α-carbon and are there­ obtained in this manner are known as essential amino acids
fore chiral molecules. Chirality, also called handedness, is a (Figure 2). Since proteins are composed of amino acids, diets
special subset of asymmetry describing objects that have no that are rich in protein are more likely to contain sufficient
internal plane of symmetry and are not superimposable upon amounts of each of the essential amino acids to preclude any
their own mirror image. Almost all of the amino acids found deficiencies.
in nature have the same chirality with respect to the α-carbon In animal feeds, however, where the bulk of the protein
and are referred to as L-amino acids based on chemical present may come from a single source such as grain, imbal­
nomenclature guidelines. Their rare, stereoisomer, ances in the individual essential amino acids can occur. For
mirror-image counterparts are called D-amino acids. Just as example, corn (maize) provides the bulk of protein in feed for
your right hand will not fit properly into a left-hand glove, a livestock. Yet the protein found in normal field corn is dis­
D-amino acid will not fit properly in a space that fits an proportionately low in lysine. To compensate, farmers
L-amino acid. routinely add lysine to animal feed to improve its nutritional
Although hundreds of amino acids have been identified value.
or synthesized, 20 of these are often designated the common Amino acids are produced commercially from a variety
amino acids. These are shown in Figure 2. In biological sys­ of sources and for a variety of uses. For example, lysine,
tems, these amino acids are the building blocks of proteins. tryptophan, and threonine to be used as feed supplements
Under the direction of messenger RNA during protein synth­ are produced by fermentation. In these processes, geneti­
esis, the amino and carboxyl side chains of two amino acids are cally altered bacteria that produce more of an amino acid
condensed chemically on the ribosome, which acts as an amino than they need for their own growth excrete the excess
acid polymerase. This reaction releases water and is called amino acid into their growth medium. Once the desired
peptide bond formation (Figure 1(c)). Chains of amino acids amino acid accumulates to a sufficient level, the bacteria
linked in this manner are thus called polypeptides or, more can be removed and the amino acid purified for use directly
simply, proteins. or as an ingredient in feed formulations. Glutamic acid,
Proteins are polymers with a constant backbone region which is often used as the flavor-enhancer monosodium
(the peptide bonds) and variable side chains (the ‘R’ side glutamate (MSG), is similarly produced by microbial fer­
chains of amino acids). The chemical properties of the side mentation. Other amino acids are produced commercially
chain of each amino acid (e.g., its size, charge, or hydrophobi­ by chemically hydrolyzing proteins. Thus, cysteine, which is
city) and the order in which the amino acids are polymerized particularly abundant in the protein keratin, is produced
contribute to the overall shape and chemical properties and from hair.
therefore the function of each protein. These functions can vary In addition, amino acids have many other functions as well,
widely, from proteins that form physical structures for including osmoregulation (proline), neurotransmitters

108 Brenner’s Encyclopedia of Genetics, 2nd edition, Volume 1 doi:10.1016/B978-0-12-374984-0.00051-6

 Amino Acids 109

(a)
α-Carbon atom
O
H
H2N C C OH

(b)
O O O
H H
H2N C C OH H2N CH2 CH2 C OH H2N C C OH

CH3 CH2

CH2

O P OH

CH3

(c)
O O O O
H H
H2N C C OH + H2N C C OH H2N CH C NH CH C OH + H2O

R1 R2 R1 R2

Figure 1 Structural features of amino acids. (a) Common structure of α-amino acids, position of the α-carbon is labeled; ‘R’ represents any number of
possible chemical structures, which may be as simple as a single hydrogen atom (–H, as in the amino acid glycine) or more complex chemical groups, as
in (b); (b) Examples of naturally occurring amino acids, with different ‘R’ groups. From left to right: alanine, β-alanine, and phosphinothricine. Note that in
β-alanine the amino group is attached to the β-carbon. Phosphinothricin, a herbicide, is an unusual amino acid in that it contains phosphorus; (c)
Representation of peptide bond formation.

Alanine Ala A CH3 *Leucine Leu L CH2 CH CH3

CH3
Arginine Arg R CH2 CH2 CH2 NH C NH2 *Lysine Lys K CH2 CH2 CH2 CH2 NH2

NH
Asparagine Asn N CH2 C NH2 *Methionine Met M CH2 CH2 S CH3
O
Asparate Asp D CH2 C OH *Phenylalanine Phe F CH2
O HN CH COOH
Cysteine Cys C CH2 SH P
Proline Pro H2C CH2
C
H2
Glutamate Glu E CH2 CH2 C OH
Serine Ser S CH2 OH
O
Glutamine Gln Q CH2 CH2 C NH2 *Threonine Thr T CH CH3
O OH
Glycine Gly G H
*Tryptophan Trp W H2C
H NH
N
*Histidine His H CH2
N *Tyrosine Tyr Y CH2 OH
H
*Isoleucine Ile I C CH2 CH3
*Valine Val V CH CH3
CH3
CH3

Figure 2 The 20 common amino acids. Three- and one-letter abbreviations and the composition of the ‘R’ side chain group are shown. Asterisks indicate
which amino acids are essential for humans. Proline is an imino acid; not just the side group but the entire structure is shown. Tyrosine can be synthesized
from phenylalanine and therefore is not essential if phenylalanine is provided.
110 Amino Acids

(gamma-aminobutyric acid), metabolic intermediates See also: Biotechnology; Genetic Code; Translation.
(ornithine and citrulline), and inhibitors (dehydroproline).
Amino acids are also important components of cos­
metics and medications. Amino acids or their chemical
analogs can be used as precursors for synthesis of pharma­ Further Reading
ceutical agents. Synthetic polymers of amino acids are
used to encapsulate drugs so as to aid in their absorption Berg JM, Tymoczko JL, and Stryer L (2002) Biochemistry, 5th edn. New York: WH
Freeman. http://www.ncbi.nlm.nih.gov/books/NBK21154/
or to control their release into the bloodstream. Current
research into amino acids promises to yield new polymers Relevant Websites
that can be used as textile fibers, novel antibiotics to
combat infectious diseases, and nutritionally enhanced http://biomodel.uah.es – A primer on the three-dimensional structure.
plants to feed a hungry world. http://prowl.rockefeller.edu – Properties of amino acids.