If you compare groupings of amino acids in different textbooks, you will see different names for the categories and (sometimes) the same amino acid being categorized differently by different authors. We separate the amino acids into categories based on the chemistry of their R-groups. Table 2.2 - Amino acid categories (based on R-group properties) It is sometimes used as a dietary supplement to reduce muscle fatigue. The latter reaction produces nitric oxide, an important signaling molecule. Ornithine is a metabolic precursor of arginine and citrulline can be produced by the breakdown of arginine. Both of these compounds are intermediates in the urea cycle. Common ones include ornithine and citrulline. There are also α-amino acids found in cells that are not incorporated into proteins. Table 2.1 - Essential and non-essential amino acids Individuals who do not synthesize sufficient amounts of arginine, cysteine, glutamine, proline, selenocysteine, serine, and tyrosine, due to illness, for example, may need dietary supplements containing these amino acids. Some amino acids that are normally nonessential, may need to be obtained from the diet in certain cases. Table 2.1 shows essential and non-essential amino acids in humans. Essential amino acids vary considerable from one organism to another and even differ in humans, depending on whether they are adults or children. This classification of amino acids has little to do with the structure of amino acids. Nutritionists divide amino acids into two groups - essential amino acids (must be in the diet because cells can’t synthesize them) and non-essential amino acids (can be made by cells). Pyrrolysine-containing proteins are much rarer and are mostly confined to archaea. Enzymes containing selenocysteine, for example, include glutathione peroxidases, tetraiodothyronine 5' deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, and selenophosphate synthetase. When this happens, these unusual amino acids can be incorporated into proteins.
The others, selenocysteine and pyrrolysine use tRNAs that are able to base pair with stop codons in the mRNA during translation. There are 22 amino acids that are found in proteins and of these, only 20 are specified by the universal genetic code. Figure 2.1 - General amino acid structure With only very minor exceptions, every amino acid found in cells and in proteins is in the L configuration. (A minor exception to this structure is that of proline, in which the end of the R-group is attached to the α-amine.) With the exception of glycine, which has an R-group consisting of a hydrogen atom, all of the amino acids in proteins have four different groups attached to them and consequently can exist in two mirror image forms, L and D. The α carbon, carboxyl, and amino groups are common to all amino acids, so the R-group is the only unique feature in each amino acid. At the “center” of each amino acid is a carbon called the α carbon and attached to it are four groups - a hydrogen, an α- carboxyl group, an α-amine group, and an R-group, sometimes referred to as a side chain. that the twenty amino acids and the four bases, are, with minor reservations, the same throughout Nature." - Francis CrickĪll amino acids have the same basic structure, which is shown in Figure 2.1. "It is one of the more striking generalizations of biochemistry.
Linked together in long chains called polypeptides, amino acids are the building blocks for the vast assortment of proteins found in all living cells.
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