Amino acid

Last updated

The structure of an alpha amino acid in its un-ionized form AminoAcidball.svg
The structure of an alpha amino acid in its un-ionized form

Amino acids are organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid. [1] [2] The key elements of an amino acid are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N), although other elements are found in the side chains of certain amino acids. About 500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be classified in many ways. [3] They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid residues form the second-largest component (water is the largest) of human muscles and other tissues. [4] Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis.


In biochemistry, amino acids having both the amine and the carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases, [lower-alpha 1] where R is an organic substituent known as a "side chain"); [5] often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids, [6] [7] [8] which combine into peptide chains ("polypeptides") to form the building-blocks of a vast array of proteins. [9] These are all L-stereoisomers ("left-handed" isomers), although a few D-amino acids ("right-handed") occur in bacterial envelopes, as a neuromodulator (D-serine), and in some antibiotics. [10]

Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are selenocysteine (present in many prokaryotes as well as most eukaryotes, but not coded directly by DNA), and pyrrolysine (found only in some archaea and one bacterium). Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. [11] [12] [13] N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts) is generally considered as a form of methionine rather than as a separate proteinogenic amino acid. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and form novel proteins known as alloproteins incorporating non-proteinogenic amino acids. [14] [15] [16]

Many important proteinogenic and non-proteinogenic amino acids have biological functions. For example, in the human brain, glutamate (standard glutamic acid) and gamma-amino-butyric acid ("GABA", non-standard gamma-amino acid) are, respectively, the main excitatory and inhibitory neurotransmitters. [17] Hydroxyproline, a major component of the connective tissue collagen, is synthesised from proline. Glycine is a biosynthetic precursor to porphyrins used in red blood cells. Carnitine is used in lipid transport.

Nine proteinogenic amino acids are called "essential" for humans because they cannot be produced from other compounds by the human body and so must be taken in as food. Others may be conditionally essential for certain ages or medical conditions. Essential amino acids may also differ between species. [lower-alpha 2]

Because of their biological significance, amino acids are important in nutrition and are commonly used in nutritional supplements, fertilizers, feed, and food technology. Industrial uses include the production of drugs, biodegradable plastics, and chiral catalysts.


The first few amino acids were discovered in the early 19th century. [18] [19] In 1806, French chemists Louis-Nicolas Vauquelin and Pierre Jean Robiquet isolated a compound in asparagus that was subsequently named asparagine, the first amino acid to be discovered. [20] [21] Cystine was discovered in 1810, [22] although its monomer, cysteine, remained undiscovered until 1884. [21] [23] Glycine and leucine were discovered in 1820. [24] The last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose, who also determined the essential amino acids and established the minimum daily requirements of all amino acids for optimal growth. [25] [26]

The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to it. [27] First use of the term "amino acid" in the English language dates from 1898, [28] while the German term, Aminosäure, was used earlier. [29] Proteins were found to yield amino acids after enzymatic digestion or acid hydrolysis. In 1902, Emil Fischer and Franz Hofmeister independently proposed that proteins are formed from many amino acids, whereby bonds are formed between the amino group of one amino acid with the carboxyl group of another, resulting in a linear structure that Fischer termed "peptide". [30]

General structure

The 21 proteinogenic a-amino acids found in eukaryotes, grouped according to their side chains' pKa values and charges carried at physiological pH (7.4) Amino Acids.svg
The 21 proteinogenic α-amino acids found in eukaryotes, grouped according to their side chains' pKa values and charges carried at physiological pH (7.4)

In the structure shown at the top of the page, R represents a side chain specific to each amino acid. The carbon atom next to the carboxyl group (which is therefore numbered 2 in the carbon chain starting from that functional group) is called the α–carbon. Amino acids containing an amino group bonded directly to the alpha carbon are referred to as alpha amino acids. [31] These include amino acids such as proline which contain secondary amines, which used to be often referred to as "imino acids". [32] [33] [34]


The alpha amino acids are the most common form found in nature, but only when occurring in the L-isomer. The alpha carbon is a chiral carbon atom, with the exception of glycine which has two indistinguishable hydrogen atoms on the alpha carbon. [35] Therefore, all alpha amino acids but glycine can exist in either of two enantiomers, called L or D amino acids (relative configuration), which are mirror images of each other (see also Chirality ). While L-amino acids represent all of the amino acids found in proteins during translation in the ribosome, D-amino acids are found in some proteins produced by enzyme posttranslational modifications after translation and translocation to the endoplasmic reticulum, as in exotic sea-dwelling organisms such as cone snails. [36] They are also abundant components of the peptidoglycan cell walls of bacteria, [37] and D-serine may act as a neurotransmitter in the brain. [38] D-amino acids are used in racemic crystallography to create centrosymmetric crystals, which (depending on the protein) may allow for easier and more robust protein structure determination. [39] The L and D convention for amino acid configuration refers not to the optical activity of the amino acid itself but rather to the optical activity of the isomer of glyceraldehyde from which that amino acid can, in theory, be synthesized (D-glyceraldehyde is dextrorotatory; L-glyceraldehyde is levorotatory). In alternative fashion, the (S) and (R) designators are used to indicate the absolute configuration. Almost all of the amino acids in proteins are (S) at the α carbon, with cysteine being (R) and glycine non-chiral. [40] Cysteine has its side chain in the same geometric position as the other amino acids, but the R/S terminology is reversed because of the higher atomic number of sulfur compared to the carboxyl oxygen gives the side chain a higher priority by the Cahn–Ingold–Prelog rules, whereas the atoms in other side chains give them lower priority compared to the carboxyl group.

Side chains

Amino acids are designated as α- when the nitrogen atom is attached to the carbon atom adjacent to the carboxyl group: in this case the compound contains the sub-structure N-C-CO2. Amino acids with the sub-structure N-C-C-CO2 are classified as β- amino acids. γ- amino acids contain the sub-structure N-C-C-C-CO2, and so on. [41]

Amino acids are usually classified by the properties of their side chain into four groups. The side chain can make an amino acid a weak acid or a weak base, and a hydrophile if the side chain is polar or a hydrophobe if it is nonpolar. [35] The chemical structures of the 22 standard amino acids, along with their chemical properties, are described more fully in the article on these proteinogenic amino acids.

The phrase "branched-chain amino acids" or BCAA refers to the amino acids having aliphatic side chains that are linear; these are leucine, isoleucine, and valine. Proline is the only proteinogenic amino acid whose side-group links to the α-amino group and, thus, is also the only proteinogenic amino acid containing a secondary amine at this position. [35] In chemical terms, proline is, therefore, an imino acid, since it lacks a primary amino group, [42] although it is still classed as an amino acid in the current biochemical nomenclature, [43] and may also be called an "N-alkylated alpha-amino acid". [44]


An amino acid in its (1) molecular and (2) zwitterionic forms Amino acid zwitterions.svg
An amino acid in its (1) molecular and (2) zwitterionic forms

In aqueous solution amino acids exist in two forms (as illustrated at the right), the molecular form and the zwitterion form in equilibrium with each other. The two forms co-exist over the pH range pK1 - 2 to pK2 + 2, which for glycine is pH 0-12. The ratio of the concentrations of the two isomers is independent of pH. The value of this ratio cannot be determined experimentally.

Because all amino acids contain amine and carboxylic acid functional groups, they are amphiprotic. [35] At pH = pK1 (ca. 2.2) there will be equal concentration of the species NH3+CH(R)CO2H and NH3+CH(R)CO2- and at pH = pK2 (ca. 10) there will be equal concentration of the species NH3+CH(R)CO2- and NH2CH(R)CO2-. It follows that the neutral molecule and the zwitterion are effectively the only species present at biological pH. [45]

It is generally assumed that the concentration of the zwitterion is much greater than the concentration of the neutral molecule on the basis of comparisons with the known pK values of amines and carboxylic acids.

Isoelectric point

Composite of titration curves of twenty proteinogenic amino acids grouped by side chain category Amino Acid Titration Curves By Side Chain.png
Composite of titration curves of twenty proteinogenic amino acids grouped by side chain category

The variation in titration curves when the amino acids can be grouped by category.[ clarification needed ] With the exception of tyrosine, using titration to distinguish among hydrophobic amino acids is problematic.

At pH values between the two pKa values, the zwitterion predominates, but coexists in dynamic equilibrium with small amounts of net negative and net positive ions. At the exact midpoint between the two pKa values, the trace amount of net negative and trace of net positive ions exactly balance, so that average net charge of all forms present is zero. [46] This pH is known as the isoelectric point pI, so pI = ½(pKa1 + pKa2). The individual amino acids all have slightly different pKa values and therefore have different isoelectric points. For amino acids with charged side chains, the pKa of the side chain is involved. Thus for Asp or Glu with negative side chains, pI = ½(pKa1 + pKaR), where pKaR is the side chain pKa. Cysteine also has potentially negative side chain with pKaR = 8.14, so pI should be calculated as for Asp and Glu, even though the side chain is not significantly charged at physiological pH. For His, Lys, and Arg with positive side chains, pI = ½(pKaR + pKa2). Amino acids have zero mobility in electrophoresis at their isoelectric point, although this behaviour is more usually exploited for peptides and proteins than single amino acids. Zwitterions have minimum solubility at their isoelectric point, and some amino acids (in particular, with non-polar side chains) can be isolated by precipitation from water by adjusting the pH to the required isoelectric point.

Occurrence and functions in biochemistry

Protein primary structure.svg
A polypeptide is an unbranched chain of amino acids
Beta alanine comparison.svg
β-alanine and its α-alanine isomer
Selenocysteine skeletal 3D.svg
The amino acid selenocysteine

Proteinogenic amino acids

Amino acids are the structural units (monomers) that make up proteins. They join together to form short polymer chains called peptides or longer chains called either polypeptides or proteins. These polymers are linear and unbranched, with each amino acid within the chain attached to two neighboring amino acids. The process of making proteins encoded by DNA/RNA genetic material is called translation and involves the step-by-step addition of amino acids to a growing protein chain by a ribozyme that is called a ribosome. [47] The order in which the amino acids are added is read through the genetic code from an mRNA template, which is an RNA copy of one of the organism's genes.

Twenty-two amino acids are naturally incorporated into polypeptides and are called proteinogenic or natural amino acids. [35] Of these, 20 are encoded by the universal genetic code. The remaining 2, selenocysteine and pyrrolysine, are incorporated into proteins by unique synthetic mechanisms. Selenocysteine is incorporated when the mRNA being translated includes a SECIS element, which causes the UGA codon to encode selenocysteine instead of a stop codon. [48] Pyrrolysine is used by some methanogenic archaea in enzymes that they use to produce methane. It is coded for with the codon UAG, which is normally a stop codon in other organisms. [49] This UAG codon is followed by a PYLIS downstream sequence. [50]

Non-proteinogenic amino acids

Aside from the 22 proteinogenic amino acids, many non-proteinogenic amino acids are known. Those either are not found in proteins (for example carnitine, GABA, levothyroxine) or are not produced directly and in isolation by standard cellular machinery (for example, hydroxyproline and selenomethionine).

Non-proteinogenic amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis. These modifications are often essential for the function or regulation of a protein. For example, the carboxylation of glutamate allows for better binding of calcium cations, [51] and collagen contains hydroxyproline, generated by hydroxylation of proline. [52] Another example is the formation of hypusine in the translation initiation factor EIF5A, through modification of a lysine residue. [53] Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane. [54]

Some non-proteinogenic amino acids are not found in proteins. Examples include 2-aminoisobutyric acid and the neurotransmitter gamma-aminobutyric acid. Non-proteinogenic amino acids often occur as intermediates in the metabolic pathways for standard amino acids – for example, ornithine and citrulline occur in the urea cycle, part of amino acid catabolism (see below). [55] A rare exception to the dominance of α-amino acids in biology is the β-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B5), a component of coenzyme A. [56]

D-amino acid natural abundance

Although D-isomers are uncommon in live organisms, gramicidin is a polypeptide made up from mixture of D- and L-amino acids. [57] Other compounds containing D-amino acids are tyrocidine and valinomycin. These compounds disrupt bacterial cell walls, particularly in Gram-positive bacteria. As of 2011, only 837 D-amino acids were found in the Swiss-Prot database out of a total of 187 million amino acids analysed. [58]

Non-standard amino acids

The 20 amino acids that are encoded directly by the codons of the universal genetic code are called standard or canonical amino acids. A modified form of methionine (N-formylmethionine) is often incorporated in place of methionine as the initial amino acid of proteins in bacteria, mitochondria and chloroplasts. Other amino acids are called non-standard or non-canonical. Most of the non-standard amino acids are also non-proteinogenic (i.e. they cannot be incorporated into proteins during translation), but two of them are proteinogenic, as they can be incorporated translationally into proteins by exploiting information not encoded in the universal genetic code.

The two non-standard proteinogenic amino acids are selenocysteine (present in many non-eukaryotes as well as most eukaryotes, but not coded directly by DNA) and pyrrolysine (found only in some archaea and one bacterium). The incorporation of these non-standard amino acids is rare. For example, 25 human proteins include selenocysteine (Sec) in their primary structure, [59] and the structurally characterized enzymes (selenoenzymes) employ Sec as the catalytic moiety in their active sites. [60] Pyrrolysine and selenocysteine are encoded via variant codons. For example, selenocysteine is encoded by stop codon and SECIS element. [11] [12] [13]

In human nutrition

Share of amino acid in different human diets and the resulting mix of amino acids in human blood serum. Glutamate and glutamine are the most frequent in food at over 10%, while alanine, glutamine, and glycine are the most common in blood. Amino acids in food and blood.png
Share of amino acid in different human diets and the resulting mix of amino acids in human blood serum. Glutamate and glutamine are the most frequent in food at over 10%, while alanine, glutamine, and glycine are the most common in blood.

When taken up into the human body from the diet, the 20 standard amino acids either are used to synthesize proteins, other biomolecules, or are oxidized to urea and carbon dioxide as a source of energy. [61] The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea cycle. The other product of transamidation is a keto acid that enters the citric acid cycle. [62] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis. [63] Of the 20 standard amino acids, nine (His, Ile, Leu, Lys, Met, Phe, Thr, Trp and Val) are called essential amino acids because the human body cannot synthesize them from other compounds at the level needed for normal growth, so they must be obtained from food. [64] [65] [66] In addition, cysteine, tyrosine, and arginine are considered semiessential amino acids, and taurine a semiessential aminosulfonic acid in children. The metabolic pathways that synthesize these monomers are not fully developed. [67] [68] The amounts required also depend on the age and health of the individual, so it is hard to make general statements about the dietary requirement for some amino acids. Dietary exposure to the non-standard amino acid BMAA has been linked to human neurodegenerative diseases, including ALS. [69] [70]

Muscle protein synthesis signaling cascades.jpg
Diagram of the molecular signaling cascades that are involved in myofibrillar muscle protein synthesis and mitochondrial biogenesis in response to physical exercise and specific amino acids or their derivatives (primarily L-leucine and HMB). [71] Many amino acids derived from food protein promote the activation of mTORC1 and increase protein synthesis by signaling through Rag GTPases. [71] [72]
Abbreviations and representations:
 PLD: phospholipase D
 PA: phosphatidic acid
 mTOR: mechanistic target of rapamycin
 AMP: adenosine monophosphate
 ATP: adenosine triphosphate
 AMPK: AMP-activated protein kinase
 PGC‐1α: peroxisome proliferator-activated receptor gamma coactivator-1α
 S6K1: p70S6 kinase
 4EBP1: eukaryotic translation initiation factor 4E-binding protein 1
 eIF4E: eukaryotic translation initiation factor 4E
 RPS6: ribosomal protein S6
 eEF2: eukaryotic elongation factor 2
 RE: resistance exercise; EE: endurance exercise
 Myo: myofibrillar; Mito: mitochondrial
 AA: amino acids
 HMB: β-hydroxy β-methylbutyric acid
 ↑ represents activation
 Τ represents inhibition
Resistance exercise-induced muscle protein synthesis.jpg
Resistance training stimulates muscle protein synthesis (MPS) for a period of up to 48 hours following exercise (shown by lighter dotted line). [73] Ingestion of a protein-rich meal at any point during this period will augment the exercise-induced increase in muscle protein synthesis (shown by solid lines). [73]

Non-protein functions

In humans, non-protein amino acids also have important roles as metabolic intermediates, such as in the biosynthesis of the neurotransmitter gamma-amino-butyric acid (GABA). Many amino acids are used to synthesize other molecules, for example:

Some non-standard amino acids are used as defenses against herbivores in plants. [82] For example, canavanine is an analogue of arginine that is found in many legumes, [83] and in particularly large amounts in Canavalia gladiata (sword bean). [84] This amino acid protects the plants from predators such as insects and can cause illness in people if some types of legumes are eaten without processing. [85] The non-protein amino acid mimosine is found in other species of legume, in particular Leucaena leucocephala . [86] This compound is an analogue of tyrosine and can poison animals that graze on these plants.

Uses in industry

Amino acids are used for a variety of applications in industry, but their main use is as additives to animal feed. This is necessary, since many of the bulk components of these feeds, such as soybeans, either have low levels or lack some of the essential amino acids: lysine, methionine, threonine, and tryptophan are most important in the production of these feeds. [87] In this industry, amino acids are also used to chelate metal cations in order to improve the absorption of minerals from supplements, which may be required to improve the health or production of these animals. [88]

The food industry is also a major consumer of amino acids, in particular, glutamic acid, which is used as a flavor enhancer, [89] and aspartame (aspartyl-phenylalanine-1-methyl ester) as a low-calorie artificial sweetener. [90] Similar technology to that used for animal nutrition is employed in the human nutrition industry to alleviate symptoms of mineral deficiencies, such as anemia, by improving mineral absorption and reducing negative side effects from inorganic mineral supplementation. [91]

The chelating ability of amino acids has been used in fertilizers for agriculture to facilitate the delivery of minerals to plants in order to correct mineral deficiencies, such as iron chlorosis. These fertilizers are also used to prevent deficiencies from occurring and improving the overall health of the plants. [92] The remaining production of amino acids is used in the synthesis of drugs and cosmetics. [87]

Similarly, some amino acids derivatives are used in pharmaceutical industry. They include 5-HTP (5-hydroxytryptophan) used for experimental treatment of depression, [93] L-DOPA (L-dihydroxyphenylalanine) for Parkinson's treatment, [94] and eflornithine drug that inhibits ornithine decarboxylase and used in the treatment of sleeping sickness. [95]

Expanded genetic code

Since 2001, 40 non-natural amino acids have been added into protein by creating a unique codon (recoding) and a corresponding transfer-RNA:aminoacyl – tRNA-synthetase pair to encode it with diverse physicochemical and biological properties in order to be used as a tool to exploring protein structure and function or to create novel or enhanced proteins. [14] [15]


Nullomers are codons that in theory code for an amino acid, however in nature there is a selective bias against using this codon in favor of another, for example bacteria prefer to use CGA instead of AGA to code for arginine. [96] This creates some sequences that do not appear in the genome. This characteristic can be taken advantage of and used to create new selective cancer-fighting drugs [97] and to prevent cross-contamination of DNA samples from crime-scene investigations. [98]

Chemical building blocks

Amino acids are important as low-cost feedstocks. These compounds are used in chiral pool synthesis as enantiomerically pure building-blocks. [99]

Amino acids have been investigated as precursors chiral catalysts, e.g., for asymmetric hydrogenation reactions, although no commercial applications exist. [100]

Biodegradable plastics

Amino acids have been considered as components of biodegradable polymers, which have applications as environmentally friendly packaging and in medicine in drug delivery and the construction of prosthetic implants. [101] An interesting example of such materials is polyaspartate, a water-soluble biodegradable polymer that may have applications in disposable diapers and agriculture. [102] Due to its solubility and ability to chelate metal ions, polyaspartate is also being used as a biodegradeable anti-scaling agent and a corrosion inhibitor. [103] [104] In addition, the aromatic amino acid tyrosine has been considered as a possible replacement for phenols such as bisphenol A in the manufacture of polycarbonates. [105]


The Strecker amino acid synthesis Strecker amino acid synthesis scheme.svg
The Strecker amino acid synthesis

Chemical synthesis

The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in one industrial synthesis of L-cysteine for example. Aspartic acid is produced by the addition of ammonia to fumarate using a lyase. [106]


In plants, nitrogen is first assimilated into organic compounds in the form of glutamate, formed from alpha-ketoglutarate and ammonia in the mitochondrion. For other amino acids, plants use transaminases to move the amino group from glutamate to another alpha-keto acids. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate. [107] Other organisms use transaminases for amino acid synthesis, too.

Nonstandard amino acids are usually formed through modifications to standard amino acids. For example, homocysteine is formed through the transsulfuration pathway or by the demethylation of methionine via the intermediate metabolite S-adenosyl methionine, [108] while hydroxyproline is made by a posttranslational modification of proline. [109]

Microorganisms and plants synthesize many uncommon amino acids. For example, some microbes make 2-aminoisobutyric acid and lanthionine, which is a sulfide-bridged derivative of alanine. Both of these amino acids are found in peptidic lantibiotics such as alamethicin. [110] However, in plants, 1-aminocyclopropane-1-carboxylic acid is a small disubstituted cyclic amino acid that is a key intermediate in the production of the plant hormone ethylene. [111]


Amino acids undergo the reactions expected of the constituent functional groups. [112] [113] The types of these reactions are determined by the groups on these side chains and are, therefore, different between the various types of amino acid.

Peptide bond formation

The condensation of two amino acids to form a dipeptide through a peptide bond Peptidformationball.svg
The condensation of two amino acids to form a dipeptide through a peptide bond

As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This polymerization of amino acids is what creates proteins. This condensation reaction yields the newly formed peptide bond and a molecule of water. In cells, this reaction does not occur directly; instead, the amino acid is first activated by attachment to a transfer RNA molecule through an ester bond. This aminoacyl-tRNA is produced in an ATP-dependent reaction carried out by an aminoacyl tRNA synthetase. [114] This aminoacyl-tRNA is then a substrate for the ribosome, which catalyzes the attack of the amino group of the elongating protein chain on the ester bond. [115] As a result of this mechanism, all proteins made by ribosomes are synthesized starting at their N-terminus and moving toward their C-terminus.

However, not all peptide bonds are formed in this way. In a few cases, peptides are synthesized by specific enzymes. For example, the tripeptide glutathione is an essential part of the defenses of cells against oxidative stress. This peptide is synthesized in two steps from free amino acids. [116] In the first step, gamma-glutamylcysteine synthetase condenses cysteine and glutamic acid through a peptide bond formed between the side chain carboxyl of the glutamate (the gamma carbon of this side chain) and the amino group of the cysteine. This dipeptide is then condensed with glycine by glutathione synthetase to form glutathione. [117]

In chemistry, peptides are synthesized by a variety of reactions. One of the most-used in solid-phase peptide synthesis uses the aromatic oxime derivatives of amino acids as activated units. These are added in sequence onto the growing peptide chain, which is attached to a solid resin support. [118] The ability to easily synthesize vast numbers of different peptides by varying the types and order of amino acids (using combinatorial chemistry) has made peptide synthesis particularly important in creating libraries of peptides for use in drug discovery through high-throughput screening. [119]

The combination of functional groups allow amino acids to be effective polydentate ligands for metal-amino acid chelates. [120] The multiple side chains of amino acids can also undergo chemical reactions.


Catabolism of proteinogenic amino acids. Amino acids can be classified according to the properties of their main products as either of the following:
* Glucogenic, with the products having the ability to form glucose by gluconeogenesis
* Ketogenic, with the products not having the ability to form glucose. These products may still be used for ketogenesis or lipid synthesis.
* Amino acids catabolized into both glucogenic and ketogenic products. Amino acid catabolism revised.png
Catabolism of proteinogenic amino acids. Amino acids can be classified according to the properties of their main products as either of the following:
* Glucogenic, with the products having the ability to form glucose by gluconeogenesis
* Ketogenic, with the products not having the ability to form glucose. These products may still be used for ketogenesis or lipid synthesis.
* Amino acids catabolized into both glucogenic and ketogenic products.

Amino acids must first pass out of organelles and cells into blood circulation via amino acid transporters, since the amine and carboxylic acid groups are typically ionized. Degradation of an amino acid, occurring in the liver and kidneys, often involves deamination by moving its amino group to alpha-ketoglutarate, forming glutamate. This process involves transaminases, often the same as those used in amination during synthesis. In many vertebrates, the amino group is then removed through the urea cycle and is excreted in the form of urea. However, amino acid degradation can produce uric acid or ammonia instead. For example, serine dehydratase converts serine to pyruvate and ammonia. [81] After removal of one or more amino groups, the remainder of the molecule can sometimes be used to synthesize new amino acids, or it can be used for energy by entering glycolysis or the citric acid cycle, as detailed in image at right.


Amino acids are bidentate ligands, forming transition metal amino acid complexes. [122]


Physicochemical properties of amino acids

The ca. 20 canonical amino acids can be classified according to their properties. Important factors are charge, hydrophilicity or hydrophobicity, size, and functional groups. [35] These properties are important for protein structure and protein–protein interactions. The water-soluble proteins tend to have their hydrophobic residues (Leu, Ile, Val, Phe, and Trp) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. (Note that in biochemistry, a residue refers to a specific monomer within the polymeric chain of a polysaccharide, protein or nucleic acid.) The integral membrane proteins tend to have outer rings of exposed hydrophobic amino acids that anchor them into the lipid bilayer. In the case part-way between these two extremes, some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that locks onto the membrane. In similar fashion, proteins that have to bind to positively charged molecules have surfaces rich with negatively charged amino acids like glutamate and aspartate, while proteins binding to negatively charged molecules have surfaces rich with positively charged chains like lysine and arginine. There are different hydrophobicity scales of amino acid residues. [123]

Some amino acids have special properties such as cysteine, that can form covalent disulfide bonds to other cysteine residues, proline that forms a cycle to the polypeptide backbone, and glycine that is more flexible than other amino acids.

Many proteins undergo a range of posttranslational modifications, when additional chemical groups are attached to the amino acids in proteins. Some modifications can produce hydrophobic lipoproteins, [124] or hydrophilic glycoproteins. [125] These type of modification allow the reversible targeting of a protein to a membrane. For example, the addition and removal of the fatty acid palmitic acid to cysteine residues in some signaling proteins causes the proteins to attach and then detach from cell membranes. [126]

Table of standard amino acid abbreviations and properties

Amino acid3-letter [127] 1-letter [127] Side chain


Side chain

polarity [127]

Side chain

charge (pH 7.4) [127]


λmax(nm) [129]

ε at

λmax (mM−1 cm−1) [129]




in proteins (%) [130]

Coding in the Standard Genetic Code (using IUPAC notation)
Alanine AlaAaliphaticnonpolarneutral1.889.0948.76GCN
Arginine ArgRbasicbasic polarpositive−4.5174.2035.78MGN, CGY (coding codons can also be expressed by: CGN, AGR)
Asparagine AsnNamidepolarneutral−3.5132.1193.93AAY
Aspartic acid AspDacidacidic polarnegative−3.5133.1045.49GAY
Cysteine CysCsulfur-containingnonpolarneutral2.52500.3121.1541.38UGY
Glutamine GlnQamidepolarneutral−3.5146.1463.9CAR
Glutamic acid GluEacidacidic polarnegative−3.5147.1316.32GAR
Glycine GlyGaliphaticnonpolarneutral−0.475.0677.03GGN
Histidine HisHbasic aromaticbasic polarpositive(10%)
Isoleucine IleIaliphaticnonpolarneutral4.5131.1755.49AUH
Leucine LeuLaliphaticnonpolarneutral3.8131.1759.68YUR, CUY (coding codons can also be expressed by: CUN, UUR)
Lysine LysKbasicbasic polarpositive−3.9146.1895.19AAR
Methionine MetMsulfur-containingnonpolarneutral1.9149.2082.32AUG
Phenylalanine PheFaromaticnonpolarneutral2.8257, 206, 1880.2, 9.3, 60.0165.1923.87UUY
Proline ProPcyclicnonpolarneutral−1.6115.1325.02CCN
Serine SerShydroxyl-containingpolarneutral−0.8105.0937.14UCN, AGY
Threonine ThrThydroxyl-containingpolarneutral−0.7119.1195.53ACN
Tryptophan TrpWaromaticnonpolarneutral−0.9280, 2195.6, 47.0204.2281.25UGG
Tyrosine TyrYaromaticpolarneutral−1.3274, 222, 1931.4, 8.0, 48.0181.1912.91UAY
Valine ValValiphaticnonpolarneutral4.2117.1486.73GUN

Two additional amino acids are in some species coded for by codons that are usually interpreted as stop codons:

21st and 22nd amino acids3-letter1-letter MW (weight)
Selenocysteine SecU168.064
Pyrrolysine PylO255.313

In addition to the specific amino acid codes, placeholders are used in cases where chemical or crystallographic analysis of a peptide or protein cannot conclusively determine the identity of a residue. They are also used to summarise conserved protein sequence motifs. The use of single letters to indicate sets of similar residues is similar to the use of abbreviation codes for degenerate bases. [131] [132]

Ambiguous amino acids3-letter1-letterAmino Acids IncludedCodons Included
Any / unknownXaaXAllNNN
Asparagine or aspartic acidAsxBD, NRAY
Glutamine or glutamic acidGlxZE, QSAR
Leucine or IsoleucineXleJI, LYTR, ATH, CTY (coding codons can also be expressed by: CTN, ATH, TTR; MTY, YTR, ATA; MTY, HTA, YTG)
Hydrophobic ΦV, I, L, F, W, Y, MNTN, TAY, TGG
Aromatic ΩF, W, Y, HYWY, TTY, TGG (coding codons can also be expressed by: TWY, CAY, TGG)
Aliphatic (non-aromatic)ΨV, I, L, MVTN, TTR (coding codons can also be expressed by: NTR, VTY)
SmallπP, G, A, SBCN, RGY, GGR
Hydrophilic ζS, T, H, N, Q, E, D, K, RVAN, WCN, CGN, AGY (coding codons can also be expressed by: VAN, WCN, MGY, CGP)
Positively charged +K, R, HARR, CRY, CGR
Negatively charged D, EGAN

Unk is sometimes used instead of Xaa, but is less standard.

In addition, many non-standard amino acids have a specific code. For example, several peptide drugs, such as Bortezomib and MG132, are artificially synthesized and retain their protecting groups, which have specific codes. Bortezomib is Pyz-Phe-boroLeu, and MG132 is Z-Leu-Leu-Leu-al. To aid in the analysis of protein structure, photo-reactive amino acid analogs are available. These include photoleucine (pLeu) and photomethionine (pMet). [133]

See also


  1. Proline is an exception to this general formula. It lacks the NH2 group because of the cyclization of the side chain and is known as an imino acid; it falls under the category of special structured amino acids.
  2. For example, ruminants such as cows obtain a number of amino acids via microbes in the first two stomach chambers.

Related Research Articles

Genetic code scheme, defines how sequences of codons specify which amino acid will be added next during protein synthesis; set of rules by which information encoded within genetic material (DNA or mRNA sequences) is translated into proteins by living cells.

The genetic code is the set of rules used by living cells to translate information encoded within genetic material into proteins. Translation is accomplished by the ribosome, which links amino acids in an order specified by messenger RNA (mRNA), using transfer RNA (tRNA) molecules to carry amino acids and to read the mRNA three nucleotides at a time. The genetic code is highly similar among all organisms and can be expressed in a simple table with 64 entries.

Protein Biological molecule consisting of chains of amino acid residues

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells, and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.

Selenocysteine chemical compound

Selenocysteine is the 21st proteinogenic amino acid.

Phenylalanine chemical compound

Phenylalanine is an essential α-amino acid with the formula C
. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins, coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the skin pigment melanin. It is encoded by the codons UUU and UUC.

Proline group of stereoisomers

Proline (symbol Pro or P) is a proteinogenic amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated NH2+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a side chain pyrrolidine, classifying it as a nonpolar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG).

Cysteine chemical compound

Cysteine (symbol Cys or C; ) is a semiessential proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH. The thiol side chain in cysteine often participates in enzymatic reactions, as a nucleophile. The thiol is susceptible to oxidation to give the disulfide derivative cystine, which serves an important structural role in many proteins. When used as a food additive, it has the E number E920. It is encoded by the codons UGU and UGC.

Methionine group of stereoisomers

Methionine is an essential amino acid in humans. As the substrate for other amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans. It is encoded by the codon AUG.

Pyrrolysine chemical compound

Pyrrolysine is an α-amino acid that is used in the biosynthesis of proteins in some methanogenic archaea and bacteria; it is not present in humans. It contains an α-amino group, a carboxylic acid group. Its pyrroline side-chain is similar to that of lysine in being basic and positively charged at neutral pH.

Serine is an ɑ-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC.

Threonine amino acid

Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC.

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized de novo by the organism at a rate commensurate with its demand, and thus must be supplied in its diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine.

Translation (biology) Cellular process of protein synthesis

In molecular biology and genetics, translation is the process in which ribosomes in the cytoplasm or ER synthesize proteins after the process of transcription of DNA to RNA in the cell's nucleus. The entire process is called gene expression.

Biomolecule Molecule that is produced by a living organism

A biomolecule or biological molecule is a loosely used term for molecules and ions present in organisms that are essential to one or more typically biological processes, such as cell division, morphogenesis, or development. Biomolecules include large macromolecules such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites, and natural products. A more general name for this class of material is biological materials. Biomolecules are usually endogenous, produced within the organism but organisms usually need exogenous biomolecules, for example certain nutrients, to survive.

Proteinogenic amino acid amino acid that is incorporated biosynthetically into proteins during translation

Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 that can be incorporated by special translation mechanisms.

Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined together to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

Xenobiology (XB) is a subfield of synthetic biology, the study of synthesizing and manipulating biological devices and systems. The name "xenobiology" derives from the Greek word xenos, which means "stranger, alien". Xenobiology is a form of biology that is not (yet) familiar to science and is not found in nature. In practice it describes novel biological systems and biochemistries that differ from the canonical DNA-RNA-20 amino acid system. For example, instead of DNA or RNA, XB explores nucleic acid analogues, termed Xeno Nucleic Acid (XNA) as information carriers. It also focuses on an expanded genetic code and the incorporation of non-proteinogenic amino acids into proteins.

EF-Tu Prokaryotic elongation factor

EF-Tu is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochrondria as TUFM.

Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism.

Expanded genetic code

An expanded genetic code is an artificially modified genetic code in which one or more specific codons have been re-allocated to encode an amino acid that is not among the 22 common naturally-encoded proteinogenic amino acids.

Non-proteinogenic amino acids class of chemical compounds

In biochemistry, non-coded or non-proteinogenic amino acids are those not naturally encoded or found in the genetic code of any organism. Despite the use of only 22 amino acids by the translational machinery to assemble proteins, over 140 amino acids are known to occur naturally in proteins and thousands more may occur in nature or be synthesized in the laboratory. Many non-proteinogenic amino acids are noteworthy because they are;


  1. Nelson, David L.; Cox, Michael M. (2005), Principles of Biochemistry (4th ed.), New York: W. H. Freeman, ISBN   0-7167-4339-6
  2. "amino acid". Cambridge Dictionaries Online. Cambridge University Press. 2015. Retrieved 3 July 2015.
  3. Wagner I, Musso H (November 1983). "New Naturally Occurring Amino Acids". Angewandte Chemie International Edition in English . 22 (11): 816–28. doi:10.1002/anie.198308161. Closed Access logo transparent.svg
  4. Latham MC (1997). "Chapter 8. Body composition, the functions of food, metabolism and energy". Human nutrition in the developing world. Food and Nutrition Series – No. 29. Rome: Food and Agriculture Organization of the United Nations.
  5. Clark, Jim (August 2007). "An introduction to amino acids". chemguide. Retrieved 4 July 2015.
  6. Jakubke H, Sewald N (2008). "Amino acids". Peptides from A to Z: A Concise Encyclopedia. Germany: Wiley-VCH. p. 20. ISBN   9783527621170 via Google Books.
  7. Pollegioni L, Servi S, eds. (2012). Unnatural Amino Acids: Methods and Protocols. Methods in Molecular Biology – Volume 794. 794. Humana Press. p. v. doi:10.1007/978-1-61779-331-8. ISBN   978-1-61779-331-8. OCLC   756512314.
  8. Hertweck C (October 2011). "Biosynthesis and Charging of Pyrrolysine, the 22nd Genetically Encoded Amino Acid". Angewandte Chemie International Edition . 50 (41): 9540–1. doi:10.1002/anie.201103769. PMID   21796749. Closed Access logo transparent.svg
  9. "Chapter 1: Proteins are the Body's Worker Molecules". The Structures of Life. National Institute of General Medical Sciences. 27 October 2011. Retrieved 20 May 2008.
  10. Michal G, Schomburg D, eds. (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd ed.). Oxford: Wiley-Blackwell. p. 5. ISBN   978-0-470-14684-2.
  11. 1 2 Tjong H (2008). Modeling Electrostatic Contributions to Protein Folding and Binding (PhD thesis). Florida State University. p. 1 footnote.
  12. 1 2 Stewart L, Burgin AB (2005). Atta-Ur-Rahman, Springer BA, Caldwell GW (eds.). "Whole Gene Synthesis: A Gene-O-Matic Future". Frontiers in Drug Design and Discovery. Bentham Science Publishers. 1: 299. doi:10.2174/1574088054583318. ISBN   978-1-60805-199-1. ISSN   1574-0889.
  13. 1 2 Elzanowski A, Ostell J (7 April 2008). "The Genetic Codes". National Center for Biotechnology Information (NCBI). Retrieved 10 March 2010.
  14. 1 2 Xie J, Schultz PG (December 2005). "Adding amino acids to the genetic repertoire". Current Opinion in Chemical Biology. 9 (6): 548–54. doi:10.1016/j.cbpa.2005.10.011. PMID   16260173.
  15. 1 2 Wang Q, Parrish AR, Wang L (March 2009). "Expanding the genetic code for biological studies". Chemistry & Biology. 16 (3): 323–36. doi:10.1016/j.chembiol.2009.03.001. PMC   2696486 . PMID   19318213.
  16. Simon M (2005). Emergent computation: emphasizing bioinformatics. New York: AIP Press/Springer Science+Business Media. pp. 105–106. ISBN   978-0-387-22046-8.
  17. Petroff OA (December 2002). "GABA and glutamate in the human brain". The Neuroscientist. 8 (6): 562–73. doi:10.1177/1073858402238515. PMID   12467378.
  18. Vickery HB, Schmidt CL (1931). "The history of the discovery of the amino acids". Chem. Rev. 9 (2): 169–318. doi:10.1021/cr60033a001.
  19. Hansen S (May 2015). "Die Entdeckung der proteinogenen Aminosäuren von 1805 in Paris bis 1935 in Illinois" (PDF) (in German). Berlin. Archived from the original (PDF) on 1 December 2017.
  20. Vauquelin LN, Robiquet PJ (1806). "The discovery of a new plant principle in Asparagus sativus". Annales de Chimie. 57: 88–93.
  21. 1 2 Anfinsen CB, Edsall JT, Richards FM (1972). Advances in Protein Chemistry. New York: Academic Press. pp.  99, 103. ISBN   978-0-12-034226-6.
  22. Wollaston WH (1810). "On cystic oxide, a new species of urinary calculus". Philosophical Transactions of the Royal Society. 100: 223–30. doi:10.1098/rstl.1810.0015.
  23. Baumann E (1884). "Über cystin und cystein". Z Physiol Chem. 8 (4): 299–305. Archived from the original on 14 March 2011. Retrieved 28 March 2011.
  24. Braconnot HM (1820). "Sur la conversion des matières animales en nouvelles substances par le moyen de l'acide sulfurique". Annales de Chimie et de Physique. 2nd Series. 13: 113–25.
  25. Simoni RD, Hill RL, Vaughan M (September 2002). "The discovery of the amino acid threonine: the work of William C. Rose [classical article]". The Journal of Biological Chemistry. 277 (37): E25. PMID   12218068.
  26. McCoy RH, Meyer CE, Rose WC (1935). "Feeding Experiments with Mixtures of Highly Purified Amino Acids. VIII. Isolation and Identification of a New Essential Amino Acid". Journal of Biological Chemistry. 112: 283–302.
  27. Menten, P. Dictionnaire de chimie: Une approche étymologique et historique. De Boeck, Bruxelles. link.
  28. Harper D. "amino-". Online Etymology Dictionary. Retrieved 19 July 2010.
  29. Paal C (1894). "Ueber die Einwirkung von Phenyl‐i‐cyanat auf organische Aminosäuren". Berichte der Deutschen Chemischen Gesellschaft. 27: 974–979. doi:10.1002/cber.189402701205.[ permanent dead link ]
  30. Fruton JS (1990). "Chapter 5- Emil Fischer and Franz Hofmeister". Contrasts in Scientific Style: Research Groups in the Chemical and Biochemical Sciences. 191. American Philosophical Society. pp. 163–165. ISBN   978-0-87169-191-0.
  31. "Alpha amino acid". The Medical Dictionary. Merriam-Webster Inc.
  32. Proline at the US National Library of Medicine Medical Subject Headings (MeSH)
  33. Matts RL (2005). "Amino acids". Biochemistry 5753: Principles of Biochemistry. Archived from the original on 18 January 2008. Retrieved 3 January 2015.
  34. IUPAC , Compendium of Chemical Terminology , 2nd ed. (the "Gold Book") (1997). Online corrected version:  (2006) " Imino acids ". doi : 10.1351/goldbook.I02959
  35. 1 2 3 4 5 6 Creighton TH (1993). "Chapter 1" . Proteins: structures and molecular properties. San Francisco: W. H. Freeman. ISBN   978-0-7167-7030-5.
  36. Pisarewicz K, Mora D, Pflueger FC, Fields GB, Marí F (May 2005). "Polypeptide chains containing D-gamma-hydroxyvaline". Journal of the American Chemical Society. 127 (17): 6207–15. doi:10.1021/ja050088m. PMID   15853325.
  37. van Heijenoort J (March 2001). "Formation of the glycan chains in the synthesis of bacterial peptidoglycan". Glycobiology. 11 (3): 25R–36R. doi:10.1093/glycob/11.3.25R. PMID   11320055.
  38. Wolosker H, Dumin E, Balan L, Foltyn VN (July 2008). "D-amino acids in the brain: D-serine in neurotransmission and neurodegeneration". The FEBS Journal. 275 (14): 3514–26. doi:10.1111/j.1742-4658.2008.06515.x. PMID   18564180.
  39. Matthews BW (June 2009). "Racemic crystallography—easy crystals and easy structures: What's not to like?". Protein Science. 18 (6): 1135–8. doi:10.1002/pro.125. PMC   2774423 . PMID   19472321.
  40. Hatem SM (2006). "Gas chromatographic determination of Amino Acid Enantiomers in tobacco and bottled wines". University of Giessen. Archived from the original on 22 January 2009. Retrieved 17 November 2008.
  41. "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 17 November 2008.
  42. Jodidi SL (1 March 1926). "The Formol Titration of Certain Amino Acids". Journal of the American Chemical Society. 48 (3): 751–753. doi:10.1021/ja01414a033.
  43. Liebecq C, ed. (1992). Biochemical Nomenclature and Related Documents (2nd ed.). Portland Press. pp. 39–69. ISBN   978-1-85578-005-7.
  44. Smith AD (1997). Oxford dictionary of biochemistry and molecular biology. Oxford: Oxford University Press. p. 535. ISBN   978-0-19-854768-6. OCLC   37616711.
  45. Simmons WJ, Meisenberg G (2006). Principles of medical biochemistry. Mosby Elsevier. p.  19. ISBN   978-0-323-02942-1.
  46. Fennema OR (19 June 1996). Food Chemistry 3rd Ed. CRC Press. pp. 327–8. ISBN   978-0-8247-9691-4.
  47. Rodnina MV, Beringer M, Wintermeyer W (January 2007). "How ribosomes make peptide bonds". Trends in Biochemical Sciences. 32 (1): 20–6. doi:10.1016/j.tibs.2006.11.007. PMID   17157507.
  48. Driscoll DM, Copeland PR (2003). "Mechanism and regulation of selenoprotein synthesis". Annual Review of Nutrition. 23 (1): 17–40. doi:10.1146/annurev.nutr.23.011702.073318. PMID   12524431.
  49. Krzycki JA (December 2005). "The direct genetic encoding of pyrrolysine". Current Opinion in Microbiology. 8 (6): 706–12. doi:10.1016/j.mib.2005.10.009. PMID   16256420.
  50. Théobald-Dietrich A, Giegé R, Rudinger-Thirion J (2005). "Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins". Biochimie. 87 (9–10): 813–7. doi:10.1016/j.biochi.2005.03.006. PMID   16164991.
  51. Vermeer C (March 1990). "Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase". The Biochemical Journal. 266 (3): 625–36. doi:10.1042/bj2660625. PMC   1131186 . PMID   2183788.
  52. Bhattacharjee A, Bansal M (March 2005). "Collagen structure: the Madras triple helix and the current scenario". IUBMB Life. 57 (3): 161–72. doi:10.1080/15216540500090710. PMID   16036578.
  53. Park MH (February 2006). "The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)". Journal of Biochemistry. 139 (2): 161–9. doi:10.1093/jb/mvj034. PMC   2494880 . PMID   16452303.
  54. Blenis J, Resh MD (December 1993). "Subcellular localization specified by protein acylation and phosphorylation". Current Opinion in Cell Biology. 5 (6): 984–9. doi:10.1016/0955-0674(93)90081-Z. PMID   8129952.
  55. Curis E, Nicolis I, Moinard C, Osowska S, Zerrouk N, Bénazeth S, Cynober L (November 2005). "Almost all about citrulline in mammals". Amino Acids. 29 (3): 177–205. doi:10.1007/s00726-005-0235-4. PMID   16082501.
  56. Coxon KM, Chakauya E, Ottenhof HH, Whitney HM, Blundell TL, Abell C, Smith AG (August 2005). "Pantothenate biosynthesis in higher plants". Biochemical Society Transactions. 33 (Pt 4): 743–6. doi:10.1042/BST0330743. PMID   16042590.
  57. Ketchem RR, Hu W, Cross TA (September 1993). "High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR". Science. 261 (5127): 1457–60. Bibcode:1993Sci...261.1457K. doi:10.1126/science.7690158. PMID   7690158.
  58. Khoury GA, Baliban RC, Floudas CA (September 2011). "Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database". Scientific Reports. 1 (90): 90. Bibcode:2011NatSR...1E..90K. doi:10.1038/srep00090. PMC   3201773 . PMID   22034591.
  59. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigó R, Gladyshev VN (May 2003). "Characterization of mammalian selenoproteomes". Science. 300 (5624): 1439–43. Bibcode:2003Sci...300.1439K. doi:10.1126/science.1083516. PMID   12775843.
  60. Gromer S, Urig S, Becker K (January 2004). "The thioredoxin system—from science to clinic". Medicinal Research Reviews. 24 (1): 40–89. doi:10.1002/med.10051. PMID   14595672.
  61. Sakami W, Harrington H (1963). "Amino acid metabolism". Annual Review of Biochemistry. 32 (1): 355–98. doi:10.1146/ PMID   14144484.
  62. Brosnan JT (April 2000). "Glutamate, at the interface between amino acid and carbohydrate metabolism". The Journal of Nutrition. 130 (4S Suppl): 988S–90S. doi:10.1093/jn/130.4.988S. PMID   10736367.
  63. Young VR, Ajami AM (September 2001). "Glutamine: the emperor or his clothes?". The Journal of Nutrition. 131 (9 Suppl): 2449S–59S, discussion 2486S–7S. doi:10.1093/jn/131.9.2449S. PMID   11533293.
  64. Young VR (August 1994). "Adult amino acid requirements: the case for a major revision in current recommendations". The Journal of Nutrition. 124 (8 Suppl): 1517S–1523S. doi:10.1093/jn/124.suppl_8.1517S. PMID   8064412.
  65. Fürst P, Stehle P (June 2004). "What are the essential elements needed for the determination of amino acid requirements in humans?". The Journal of Nutrition. 134 (6 Suppl): 1558S–1565S. doi:10.1093/jn/134.6.1558S. PMID   15173430.
  66. Reeds PJ (July 2000). "Dispensable and indispensable amino acids for humans". The Journal of Nutrition. 130 (7): 1835S–40S. doi:10.1093/jn/130.7.1835S. PMID   10867060.
  67. Imura K, Okada A (January 1998). "Amino acid metabolism in pediatric patients". Nutrition. 14 (1): 143–8. doi:10.1016/S0899-9007(97)00230-X. PMID   9437700.
  68. Lourenço R, Camilo ME (2002). "Taurine: a conditionally essential amino acid in humans? An overview in health and disease". Nutricion Hospitalaria. 17 (6): 262–70. PMID   12514918.
  69. Holtcamp W (March 2012). "The emerging science of BMAA: do cyanobacteria contribute to neurodegenerative disease?". Environmental Health Perspectives. 120 (3): A110–6. doi:10.1289/ehp.120-a110. PMC   3295368 . PMID   22382274.
  70. Cox PA, Davis DA, Mash DC, Metcalf JS, Banack SA (January 2016). "Dietary exposure to an environmental toxin triggers neurofibrillary tangles and amyloid deposits in the brain". Proceedings: Biological Sciences. 283 (1823): 20152397. doi:10.1098/rspb.2015.2397. PMC   4795023 . PMID   26791617.
  71. 1 2 Brook MS, Wilkinson DJ, Phillips BE, Perez-Schindler J, Philp A, Smith K, Atherton PJ (January 2016). "Skeletal muscle homeostasis and plasticity in youth and ageing: impact of nutrition and exercise". Acta Physiologica. 216 (1): 15–41. doi:10.1111/apha.12532. PMC   4843955 . PMID   26010896.
  72. Lipton JO, Sahin M (October 2014). "The neurology of mTOR". Neuron. 84 (2): 275–91. doi:10.1016/j.neuron.2014.09.034. PMC   4223653 . PMID   25374355.
    Figure 2: The mTOR Signaling Pathway
  73. 1 2 Phillips SM (May 2014). "A brief review of critical processes in exercise-induced muscular hypertrophy". Sports Medicine. 44 Suppl 1: S71–7. doi:10.1007/s40279-014-0152-3. PMC   4008813 . PMID   24791918.
  74. Broadley KJ (March 2010). "The vascular effects of trace amines and amphetamines". Pharmacol. Ther. 125 (3): 363–375. doi:10.1016/j.pharmthera.2009.11.005. PMID   19948186.
  75. Lindemann L, Hoener MC (May 2005). "A renaissance in trace amines inspired by a novel GPCR family". Trends Pharmacol. Sci. 26 (5): 274–281. doi:10.1016/ PMID   15860375.
  76. Wang X, Li J, Dong G, Yue J (February 2014). "The endogenous substrates of brain CYP2D". Eur. J. Pharmacol. 724: 211–218. doi:10.1016/j.ejphar.2013.12.025. PMID   24374199.
  77. Savelieva KV, Zhao S, Pogorelov VM, Rajan I, Yang Q, Cullinan E, Lanthorn TH (2008). Bartolomucci A (ed.). "Genetic disruption of both tryptophan hydroxylase genes dramatically reduces serotonin and affects behavior in models sensitive to antidepressants". PLOS One. 3 (10): e3301. Bibcode:2008PLoSO...3.3301S. doi:10.1371/journal.pone.0003301. PMC   2565062 . PMID   18923670.
  78. Shemin D, Rittenberg D (December 1946). "The biological utilization of glycine for the synthesis of the protoporphyrin of hemoglobin". The Journal of Biological Chemistry. 166 (2): 621–5. PMID   20276176.
  79. Tejero J, Biswas A, Wang ZQ, Page RC, Haque MM, Hemann C, Zweier JL, Misra S, Stuehr DJ (November 2008). "Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase". The Journal of Biological Chemistry. 283 (48): 33498–507. doi:10.1074/jbc.M806122200. PMC   2586280 . PMID   18815130.
  80. Rodríguez-Caso C, Montañez R, Cascante M, Sánchez-Jiménez F, Medina MA (August 2006). "Mathematical modeling of polyamine metabolism in mammals". The Journal of Biological Chemistry. 281 (31): 21799–812. doi:10.1074/jbc.M602756200. PMID   16709566.
  81. 1 2 Stryer L, Berg JM, Tymoczko JL (2002). Biochemistry (5th ed.). New York: W.H. Freeman. pp.  693–8. ISBN   978-0-7167-4684-3.
  82. Hylin, John W. (1969). "Toxic peptides and amino acids in foods and feeds". Journal of Agricultural and Food Chemistry. 17 (3): 492–6. doi:10.1021/jf60163a003.
  83. Turner BL, Harborne JB (1967). "Distribution of canavanine in the plant kingdom". Phytochemistry. 6 (6): 863–66. doi:10.1016/S0031-9422(00)86033-1.
  84. Ekanayake S, Skog K, Asp NG (May 2007). "Canavanine content in sword beans (Canavalia gladiata): analysis and effect of processing". Food and Chemical Toxicology. 45 (5): 797–803. doi:10.1016/j.fct.2006.10.030. PMID   17187914.
  85. Rosenthal GA (2001). "L-Canavanine: a higher plant insecticidal allelochemical". Amino Acids. 21 (3): 319–30. doi:10.1007/s007260170017. PMID   11764412.
  86. Hammond AC (May 1995). "Leucaena toxicosis and its control in ruminants". Journal of Animal Science. 73 (5): 1487–92. doi:10.2527/1995.7351487x. PMID   7665380.[ permanent dead link ]
  87. 1 2 Leuchtenberger W, Huthmacher K, Drauz K (November 2005). "Biotechnological production of amino acids and derivatives: current status and prospects". Applied Microbiology and Biotechnology. 69 (1): 1–8. doi:10.1007/s00253-005-0155-y. PMID   16195792.
  88. Ashmead HD (1993). The Role of Amino Acid Chelates in Animal Nutrition. Westwood: Noyes Publications.
  89. Garattini S (April 2000). "Glutamic acid, twenty years later". The Journal of Nutrition. 130 (4S Suppl): 901S–9S. doi:10.1093/jn/130.4.901S. PMID   10736350.
  90. Stegink LD (July 1987). "The aspartame story: a model for the clinical testing of a food additive". The American Journal of Clinical Nutrition. 46 (1 Suppl): 204–15. doi:10.1093/ajcn/46.1.204. PMID   3300262.
  91. Albion Laboratories, Inc. "Albion Ferrochel Website" . Retrieved 12 July 2011.
  92. Ashmead HD (1986). Foliar Feeding of Plants with Amino Acid Chelates. Park Ridge: Noyes Publications.
  93. Turner EH, Loftis JM, Blackwell AD (March 2006). "Serotonin a la carte: supplementation with the serotonin precursor 5-hydroxytryptophan". Pharmacology & Therapeutics. 109 (3): 325–38. doi:10.1016/j.pharmthera.2005.06.004. PMID   16023217.
  94. Kostrzewa RM, Nowak P, Kostrzewa JP, Kostrzewa RA, Brus R (March 2005). "Peculiarities of L: -DOPA treatment of Parkinson's disease". Amino Acids. 28 (2): 157–64. doi:10.1007/s00726-005-0162-4. PMID   15750845.
  95. Heby O, Persson L, Rentala M (August 2007). "Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis". Amino Acids. 33 (2): 359–66. doi:10.1007/s00726-007-0537-9. PMID   17610127.
  96. Cruz-Vera LR, Magos-Castro MA, Zamora-Romo E, Guarneros G (2004). "Ribosome stalling and peptidyl-tRNA drop-off during translational delay at AGA codons". Nucleic Acids Research. 32 (15): 4462–8. doi:10.1093/nar/gkh784. PMC   516057 . PMID   15317870.
  97. Andy C (October 2012). "Molecules 'too dangerous for nature' kill cancer cells". New Scientist.
  98. "Lethal DNA tags could keep innocent people out of jail". New Scientist. 2 May 2013.
  99. Hanessian S (1993). "Reflections on the total synthesis of natural products: Art, craft, logic, and the chiron approach". Pure and Applied Chemistry. 65 (6): 1189–204. doi:10.1351/pac199365061189.
  100. Blaser HU (1992). "The chiral pool as a source of enantioselective catalysts and auxiliaries". Chemical Reviews. 92 (5): 935–52. doi:10.1021/cr00013a009.
  101. Sanda F, Endo T (1999). "Syntheses and functions of polymers based on amino acids". Macromolecular Chemistry and Physics. 200 (12): 2651–61. doi:10.1002/(SICI)1521-3935(19991201)200:12<2651::AID-MACP2651>3.0.CO;2-P.
  102. Gross RA, Kalra B (August 2002). "Biodegradable polymers for the environment". Science. 297 (5582): 803–7. Bibcode:2002Sci...297..803G. doi:10.1126/science.297.5582.803. PMID   12161646.
  103. Low KC, Wheeler AP, Koskan LP (1996). Commercial poly(aspartic acid) and Its Uses. Advances in Chemistry Series. 248. Washington, D.C.: American Chemical Society.
  104. Thombre SM, Sarwade BD (2005). "Synthesis and Biodegradability of Polyaspartic Acid: A Critical Review". Journal of Macromolecular Science, Part A. 42 (9): 1299–1315. doi:10.1080/10601320500189604.
  105. Bourke SL, Kohn J (April 2003). "Polymers derived from the amino acid L-tyrosine: polycarbonates, polyarylates and copolymers with poly(ethylene glycol)". Advanced Drug Delivery Reviews. 55 (4): 447–66. doi:10.1016/S0169-409X(03)00038-3. PMID   12706045.
  106. Drauz K, Grayson I, Kleemann A, Krimmer H, Leuchtenberger W, Weckbecker C (2006). Ullmann's Encyclopedia of Industrial Chemistry . Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2.
  107. Jones RC, Buchanan BB, Gruissem W (2000). Biochemistry & molecular biology of plants. Rockville, Md: American Society of Plant Physiologists. pp.  371–2. ISBN   978-0-943088-39-6.
  108. Brosnan JT, Brosnan ME (June 2006). "The sulfur-containing amino acids: an overview". The Journal of Nutrition. 136 (6 Suppl): 1636S–1640S. doi:10.1093/jn/136.6.1636S. PMID   16702333.
  109. Kivirikko KI, Pihlajaniemi T (1998). Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases. Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology – and Related Areas of Molecular Biology. 72. pp. 325–98. doi:10.1002/9780470123188.ch9. ISBN   9780470123188. PMID   9559057.
  110. Whitmore L, Wallace BA (May 2004). "Analysis of peptaibol sequence composition: implications for in vivo synthesis and channel formation". European Biophysics Journal. 33 (3): 233–7. doi:10.1007/s00249-003-0348-1. PMID   14534753.
  111. Alexander L, Grierson D (October 2002). "Ethylene biosynthesis and action in tomato: a model for climacteric fruit ripening". Journal of Experimental Botany. 53 (377): 2039–55. doi:10.1093/jxb/erf072. PMID   12324528.
  112. Elmore DT, Barrett GC (1998). Amino acids and peptides. Cambridge, UK: Cambridge University Press. pp. 48–60. ISBN   978-0-521-46827-5.
  113. Gutteridge A, Thornton JM (November 2005). "Understanding nature's catalytic toolkit". Trends in Biochemical Sciences. 30 (11): 622–9. doi:10.1016/j.tibs.2005.09.006. PMID   16214343.
  114. Ibba M, Söll D (May 2001). "The renaissance of aminoacyl-tRNA synthesis". EMBO Reports. 2 (5): 382–7. doi:10.1093/embo-reports/kve095. PMC   1083889 . PMID   11375928.
  115. Lengyel P, Söll D (June 1969). "Mechanism of protein biosynthesis". Bacteriological Reviews. 33 (2): 264–301. doi:10.1128/MMBR.33.2.264-301.1969. PMC   378322 . PMID   4896351.
  116. Wu G, Fang YZ, Yang S, Lupton JR, Turner ND (March 2004). "Glutathione metabolism and its implications for health". The Journal of Nutrition. 134 (3): 489–92. doi:10.1093/jn/134.3.489. PMID   14988435.
  117. Meister A (November 1988). "Glutathione metabolism and its selective modification". The Journal of Biological Chemistry. 263 (33): 17205–8. PMID   3053703.
  118. Carpino LA (1992). "1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive". Journal of the American Chemical Society. 115 (10): 4397–8. doi:10.1021/ja00063a082.
  119. Marasco D, Perretta G, Sabatella M, Ruvo M (October 2008). "Past and future perspectives of synthetic peptide libraries". Current Protein & Peptide Science. 9 (5): 447–67. doi:10.2174/138920308785915209. PMID   18855697.
  120. Konara S, Gagnona K, Clearfield A, Thompson C, Hartle J, Ericson C, Nelson C (2010). "Structural determination and characterization of copper and zinc bis-glycinates with X-ray crystallography and mass spectrometry". Journal of Coordination Chemistry. 63 (19): 3335–47. doi:10.1080/00958972.2010.514336.
  121. Stipanuk, M. H. (2006). Biochemical, physiological, & molecular aspects of human nutrition (2 ed.): Saunders Elsevier.
  122. Severin, K.; Bergs, R.; Beck, W. (1998). "Bioorganometallic Chemistry-Transition Metal Complexes with α-Amino Acids and Peptides". Angew. Chem. Int. Ed. 37 (12): 1635–1654. doi:10.1002/(SICI)1521-3773(19980703)37:12<1634::AID-ANIE1634>3.0.CO;2-C.CS1 maint: uses authors parameter (link)
  123. Urry DW (2004). "The change in Gibbs free energy for hydrophobic association: Derivation and evaluation by means of inverse temperature transitions". Chemical Physics Letters. 399 (1–3): 177–83. Bibcode:2004CPL...399..177U. doi:10.1016/S0009-2614(04)01565-9.
  124. Magee T, Seabra MC (April 2005). "Fatty acylation and prenylation of proteins: what's hot in fat". Current Opinion in Cell Biology. 17 (2): 190–6. doi:10.1016/ PMID   15780596.
  125. Pilobello KT, Mahal LK (June 2007). "Deciphering the glycocode: the complexity and analytical challenge of glycomics". Current Opinion in Chemical Biology. 11 (3): 300–5. doi:10.1016/j.cbpa.2007.05.002. PMID   17500024.
  126. Smotrys JE, Linder ME (2004). "Palmitoylation of intracellular signaling proteins: regulation and function". Annual Review of Biochemistry. 73 (1): 559–87. doi:10.1146/annurev.biochem.73.011303.073954. PMID   15189153.
  127. 1 2 3 4 Hausman RE, Cooper GM (2004). The cell: a molecular approach. Washington, D.C: ASM Press. p. 51. ISBN   978-0-87893-214-6.
  128. Kyte J, Doolittle RF (May 1982). "A simple method for displaying the hydropathic character of a protein". Journal of Molecular Biology. 157 (1): 105–32. CiteSeerX . doi:10.1016/0022-2836(82)90515-0. PMID   7108955.
  129. 1 2 Freifelder D (1983). Physical Biochemistry (2nd ed.). W. H. Freeman and Company. ISBN   978-0-7167-1315-9.[ page needed ]
  130. Kozlowski LP (January 2017). "Proteome-pI: proteome isoelectric point database". Nucleic Acids Research. 45 (D1): D1112–D1116. doi:10.1093/nar/gkw978. PMC   5210655 . PMID   27789699.
  131. Aasland R, Abrams C, Ampe C, Ball LJ, Bedford MT, Cesareni G, Gimona M, Hurley JH, Jarchau T, Lehto VP, Lemmon MA, Linding R, Mayer BJ, Nagai M, Sudol M, Walter U, Winder SJ (February 2002). "Normalization of nomenclature for peptide motifs as ligands of modular protein domains". FEBS Letters. 513 (1): 141–4. doi:10.1111/j.1432-1033.1968.tb00350.x. PMID   11911894.
  132. IUPAC-IUB Commission on Biochemical Nomenclature (1972). "A one-letter notation for amino acid sequences". Pure and Applied Chemistry. 31 (4): 641–5. doi:10.1351/pac197231040639. PMID   5080161.
  133. Suchanek M, Radzikowska A, Thiele C (April 2005). "Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells". Nature Methods. 2 (4): 261–7. doi:10.1038/nmeth752. PMID   15782218.

Further reading