Arginine is a complex amino acid that is often found at the active (or catalytic) site in proteins and enzymes

due to its amine-containing side chain. Although arginine is considered an essential amino acid (it must be obtained through the diet), this is true only during the juvenile period in humans. Arginine is incorporated in proteins at about a 4.7 percent on a per-mole basis when compared to the other amino acids. Natural sources of arginine are brown rice, nuts, popcorn, raisins, and whole-wheat products.

Alanine is a non-essential amino acid that is involved in the metabolism of tryptophan and the vitamin pyridoxine. The alpha-carbon in alanine is substituted with a levorotatory (l)-methyl group, making it one of the simplest amino acids with respect to molecular structure. This amino acid is one of the most widely used in protein construction, averaging about 9 percent of average protein composition on a per-mole basis when compared with the other amino acids. Alanine has little therapeutic role in humans, although it has been demonstrated to display a cholesterol-reducing effect in rats. This is the only naturally occurring beta amino acid, however this biochemical is not used in the biosynthesis of any major proteins or enzymes. Structurally, the IUPAC name for beta-alanine would be 3- (or beta- ) aminopropionic acid. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (vitamin B-5) which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid. Asparagine, the beta-amido derivative of aspartic acid, is considered a non-essential amino acid. This amino acid plays an important role in the biosynthesis of glycoproteins and is also essential to the synthesis of a large number of other proteins. On a per-mole basis, asparagine is incorporated into proteins and enzymes at a rate of 4.4 percent with respect to the other amino acids. Aspartic acid is one of two amino acids (the other is glutamic acid) that has a negatively charged carboxylate group on the side chain. This gives aspartic acid an overall negative charge at physiological hydrogen ion concentrations (approximately pH 7.3). Although aspartic acid is considered a non-essential amino acid, it plays a paramount role in metabolism during construction of other amino acids and biochemicals in the citric acid cycle. Among the biochemicals that are synthesized from aspartic acid are asparagine, arginine, lysine, methionine, threonine, isoleucine, and several nucleotides The major biochemical function of carnitine is to act as a trans-membrane carrier of fatty acids to the interior of mitochondria. Carnitine is not used in the biosynthesis of proteins or enzymes and has an unusual structure compared to the classical amino acids. It is synthesized naturally from the amino acids methionine and lysine, but good external sources of carnitine are milk products and meats.

Citrulline exists primarily in the liver, where it is heavily involved in the urea cycle to detoxify and excrete ammonia. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. Next, it is combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine. Citrulline is not a component of any major proteins or enzymes

Cysteine is only incorporated into proteins at the rate of 2.8 percent relative to the other amino acids, but the unique thiol side chain of this amino acid is often heavily involved in the threedimensional stability of proteins and enzymes. The side chain is also often involved in the chemistry occurring at the active sites of many enzymes. Cysteine is also critical to the metabolism of a number of essential biochemicals including coenzyme A, heparin, biotin, lipoic acid, and glutathione. Cystine is the product of an oxidation between the thiol side chains of two cysteine amino acids. As such, cystine is not considered one of the 20 amino acids. This oxidation product is found in abundance in a variety of proteins such as hair keratin, insulin, the digestive enzymes chromotrypsinogen A, papain, and trypsinogen where it is heavily involved in stabilizing the tertiary structure of these macromolecules. gamma-Aminobutyric acid (GABA) is the product of a biochemical decarboxylation reaction of glutamic acid by the vitamin pyridoxal. GABA serves as a inhibitory neurotransmitter to block the transmission of an impulse from one cell to another in the central nervous system. Medically, GABA has been used to treat both epilepsy and hypertension where it is thought to induce tranquility in individuals who have a high activity of manic behavior and acute agitation.

Glutamic acid is biosynthesized from a number of amino acids including ornithine and arginine. When aminated, glutamic acid forms the important amino acid glutamine. Because it has a carboxylic acid moiety on the side chain, glutamic acid is one of only two amino acids (the other being aspartic acid) that has a net negative charge at physiological pH. This negative charge makes glutamic acid a very polar molecule and it is usually found on the outside of proteins and enzymes where it is free to interact with the aqueous intracellular surroundings. On a molar basis, glutamic acid is incorporated into proteins at a rate of 6.2 percent compared to the other amino acids. Glutamine is one of the twenty amino acids generally present in animal proteins. A monoamide of glutamic acid, the biochemical is also a component of many plants and was first isolated from beet juice in 1883. Glutamine was not isolated as a component from a protein, however, until 1932 and was first chemically produced the following year. The substance plays an important role in the cellular metabolism of animals and is the only amino acid with the ability to easily cross the barrier between blood and brain tissue. Combined, glutamine and glutamic acid are responsible for the vast majority of the amino nitrogen located in the brain, and are of central importance in the regulation of bodily ammonia levels. Though it is readily synthesized naturally within the body, glutamine is popularly sold as a nutritional supplement for athletes.

Glutathione is actually a tripeptide made up the amino acids gamma-glutamic acid, cysteine, and glycine. The primary biological function of glutathione is to act as a non-enzymatic reducing agent to help keep cysteine thiol side chains in a reduced state on the surface of proteins. Glutathione is also used to prevent oxidative stress in most cells and helps to trap free radicals that can damage DNA and RNA. There is a direct correlation with the speed of aging and the reduction of glutathione concentrations in intracellular fluids. As individuals grow older, glutathione levels drop, and the ability to detoxify free radicals decreases.

Glycine is the simplest amino acid and is the only amino acid that is not optically active (it has no stereoisomers). This amino acid is essential for the biosynthesis of nucleic acids as well as of bile acids, porphyrins, creatine phosphate, and other amino acids. On a molar basis, glycine is the second most common amino acid found in proteins and enzymes being incorporated at the rate of 7.5 percent compared to the other amino acids. Glycine is also similar to gamma-aminobutyric acid and glutamic acid in the ability to inhibit neurotransmitter signals in the central nervous system.

Histidine is one of the basic (with reference to pH) amino acids due to its aromatic nitrogenheterocyclic imidazole side chain. This amino acid is biochemically metabolized into the neurotransmitter histamine and the set of genes that produce the enzymes responsible for histidine biosynthesis are controlled by the well-studied histidine operon. The disruption of histidine biosynthesis in bacteria is the basis for the famous Ames test, used to determine the mutagenability of various chemicals. Histidine is incorporated into proteins and enzymes at a molar percentage of 2.1 compared to the other amino acids.

Hydroxyproline is derived from the amino acid proline and is used almost exclusively in structural proteins including collagen, connective tissue in mammals, and in plant cell walls. An unusual feature of this amino acid is that it is not incorporated into collagen during biosynthesis at the ribosome, but is formed from proline by a posttranslational modification by an enzymatic hydroxylation reaction. Non-hydroxylated collagen is commonly termed pro-collagen

Isoleucine is a member of the aliphatic side-chain amino acid family that is composed of extremely hydrophobic biochemicals that are found principally in the interior of proteins and enzymes. Like several other members of this family (valine and leucine), isoleucine is an essential amino acid that is not synthesized by mammalian tissues. Another feature of this class of amino acids is that they appear to have no other significant biological role than incorporation into proteins and enzymes, where their main purpose is to help dictate the tertiary structure of the macromolecules. Isoleucine is incorporated into proteins at a molar rate of 4.6 percent when compared to the other amino acids.

Leucine, like its cousins isoleucine and valine, is a hydrophobic amino acid that is found as a structural element on the interior of proteins and enzymes. There appears to be no other significant metabolic role for these amino acids, but they are essential and because they are not synthesized by mammalian tissues, must be taken in the diet. Leucine ties glycine for the position of second most common amino acid found in proteins with a concentration of 7.5 percent on a molar basis compared to the other amino acids. Lysine is an essential amino acid that has a net positive charge at physiological pH values making it one of the three basic (with respect to charge) amino acids. This polar amino acid is commonly found on the surfaces of proteins and enzymes, and sometimes appears in the active site. Sources of lysine include meats, fish, poultry, and dairy products. Lysine is incorporated into proteins at the rate of 7 percent on a molar basis compared to the other amino acids.

Methionine is an important amino acid that helps to initiate translation of messenger RNA by being the first amino acid incorporated into the N-terminal position of all proteins. This sulfurcontaining amino acid is also the source of sulfur for cysteine in animals and man. In that regard, methionine is considered an essential amino acid whereas cysteine is not, so cysteine is nonessential only as long as the diet contains adaquate amounts of methionine. The terminal methyl group of the methionine side chain often participates in biochemical methyl transfer reactions making methionine a member of the "methyl donor" class of biochemicals. On a molar basis, methionine is incorporated into proteins and enzymes at the rate of 1.7 percent, but this is partially due to posttranslational protein-modifying events that often occur where methionine and several other N-terminal amino acids are removed from the protein.

Ornithine plays an important role in the urea cycle and is the precursor of the amino acids citrulline, glutamic acid, and proline. Another primary role of ornithine is being an intermediate in arginine biosynthesis, although this is due to its participation in the urea cycle (responsible for the production of urea). Ornithine is not directly incorporated into proteins and enzymes and does not have a codon in the genetic code.

Phenylalanine is an essential amino acid that is also one of the aromatic amino acids that exhibit ultraviolet radiation absorption properties with a large extinction coefficient. This characteristic is often used as an analytical tool to quantify the amount of protein in a sample. Phenylalanine plays a key role in the biosynthesis of other amino acids and some neurotransmitters. It is the most commonly found aromatic amino acid in proteins and enzymes with a molar ratio of 3.5 percent compared to the other amino acids, about double the amount of any other aromatic amino acid Proline is one of the cyclic aliphatic amino acids that is a major component of the protein collagen, the connective tissue structure that binds and supports all other tissues. Proline is synthesized from glutamic acid prior to its incorporation into pro-collagen during messenger RNA translation. After the pro-collagen protein is synthesized, it is converted by posttranslational modification into hydroxyproline. On a molar basis proline is incorporated into protein at a rate of 4.2 percent with respect to other amino acids. Serine .The methyl side chain of serine contains a hydroxy group making this one of two amino acids that are also alcohols. Serine plays a major role in a variety of biosynthetic pathways including those involving pyrimidines, purines, creatine, and porphyrins. Serine is also found at the active site in an important class of enzymes termed "serine proteases" that include trypsin and chymotrypsin. These enzymes catalyze the hydrolysis of peptide bonds in polypeptides and proteins, a major function in the digestive process. On a molar basis, serine is incorporated into proteins at a rate of 7.1 percent compared to the other amino acids

Taurine is a non-essential sulfur-containing amino acid that functions with glycine and gammaaminobutyric acid as a neuroinhibitory transmitter. While taurine does not have a genetic codon and is not incorporated into proteins and enzymes, it does play an important role in bile acid metabolism. Taurine is incorporated into one of the most abundant bile acids, chenodeoxychloic acid where it serves to emulsify dietary lipids in the intestine, promoting digestion.

Threonine is another alcohol-containing amino acid that can not be produced by metabolism and must be taken in the diet. This amino acid plays an important role along with glycine and serine in porphyrin metabolism. Threonine is incorporated into proteins and enzymes at a molar rate of 6 percent compared to the other amino acids

Tryptophan is an essential amino acid that must be obtained from the diet. The unusual indole side chain of tryptophan is also the nucleus of the important neurotransmitter serotonin, which is biosynthesized from tryptophan. The aromatic portion of tryptophan also serves as an ultraviolet marker for detection of this amino acid either separately, or incorporated into proteins and enzymes, via ultraviolet spectrophotometry. Tryptophan is incorporated into proteins and enzymes at the molar rate of 1.1 percent compared to other amino acids making it the rarest amino acid found in proteins.

Tyrosine is metabolically synthesized from phenylalanine to become the para-hydroxy derivative of that important amino acid. This hydroxylated amino acid participates in the synthesis of many important biochemicals including the thyroid hormones, the melanin biological pigments, and the catecholamines, an important class of biological regulators. Tyrosine is incorporated into proteins and enzymes at the molar rate of 3.5 percent with respect to the other amino acids.

Valine is an aliphatic amino acid that is closely related to leucine and isoleucine both in structure and function. These amino acids are extremely hydrophobic and are almost always found in the interior of proteins. They are also seldom useful in routine biochemical reactions, but are relegated to the duty of determining the three-dimensional structure of proteins due to their hydrophobic nature. They are also essential amino acids and must be obtained in the diet. Important sources of valine include soy flour, cottage cheese, fish, meats, and vegetables. Valine is incorporated into proteins and enzymes at the molar rate of 6.9 percent when compared to the other amino acids.