Instruct: Given a question, retrieve relevant documents that can help answer the question.
Query: What is the most abundant amino acid in the human body?
In human blood, glutamine is the most abundant free amino acid.[6]
A typical Brochmann body is mass of whitish nodules of variable sizes, ranging from 1 to 8 mm in diameter. The nodules are composed of polygonal and elongated cells. The cells are enveloped with connective tissues. They are separated into two major islets: one is found near the spleen and the other is located inside the wall of the duodenum, at the pyloric junction. Both islet groups contain insulin, glucagon, peptide YY and somatostatin, but these proteins are secreted only in the pyloric Brockmann bodies. The amino acid sequence and primary structure of the hormones are slightly different from their counterparts in higher vertebrates. For example, tilapia and human insulin differs by 17 amino acids. There are also amino acid variation among different species; for example, glutamine residue, at position 5 in the A-chain of insulin in most teleosts, is replaced by glutamic acid in tilapia.
Proteins are chains of amino acids. Nine of these proteinogenic amino acids are considered essential for humans because they cannot be produced from other compounds by the human body and so must be taken in as food. Recommended intakes, expressed as milligrams per kilogram of body weight per day, have been established. Other amino acids may be conditionally essential for certain ages or medical conditions. Amino acids, individually and in combinations, are sold as dietary supplements. The claim for supplementing with the branched chain amino acids leucine, valine and isoleucine is for stimulating muscle protein synthesis. A review of the literature concluded this claim was unwarranted. In elderly people, supplementation with just leucine resulted in a modest (0.99 kg) increase in lean body mass. The non-essential amino acid arginine, consumed in sufficient amounts, is thought to act as a donor for the synthesis of nitric oxide, a vasodilator. A review confirmed blood pressure lowering. Taurine, a popular dietary supplement ingredient with claims made for sports performance, is technically not an amino acid. It is synthesized in the body from the amino acid cysteine.
Leucine is the most abundant amino acid by volume (15.37%). TMEM251 has very low abundance of Cysteine, Asparagine, and Aspartic acid. It has one negative charge cluster from amino acid 67-82. No repeats are identified. The same patterns are observed in TMEM251's primate orthologs.
Proline is predicted to be the most abundant amino acid in proline-rich protein 23C "Homo sapiens". In comparison to the prevalence of amino acids in other human proteins, it is predicted that proline-rich protein 23C "Homo sapiens" has a higher abundance of proline along with very low abundances of asparagine, threonine, and lysine. Orthologs for this protein are predicted to also have a high abundance of proline.
Six other amino acids are considered conditionally essential in the human diet, meaning their synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, and selenocysteine. The amino acid, pyrrolysine, considered the 22nd one, is not used by humans; thus, it is non-essential.
Protein is a nutrient needed by the human body for growth and maintenance. Aside from water, proteins are the most abundant kind of molecules in the body. Protein can be found in all cells of the body and is the major structural component of all cells in the body, especially muscle. This also includes body organs, hair and skin. Proteins are also used in membranes, such as glycoproteins. When broken down into amino acids, they are used as precursors to nucleic acid, co-enzymes, hormones, immune response, cellular repair, and other molecules essential for life. Additionally, protein is needed to form blood cells.
Glutamine is the most abundant naturally occurring, nonessential amino acid in the human body, and one of the few amino acids that can directly cross the blood–brain barrier.[6] Humans obtain glutamine through catabolism of proteins in foods they eat.[16] In states where tissue is being built or repaired, like growth of babies, or healing from wounds or severe illness, glutamine becomes conditionally essential.[16]
While GCDH deficiency is a rare disease, GLO deficiency is the most common of metabolic diseases affecting children, limiting ascorbic acid biosynthesis to a minute fraction of what other non-primate species synthesize. It was thus called by OMIM (Online Mendeleian Inheritance in Man) a "public" error of metabolism. Ascorbic acid (Vitamin C) is a necessary cofactor for the utilization of lysine in collagen synthesis. Collagen, the most abundant protein in the human body, requires great amounts of lysine, the most abundant amino acids in proteins. Ascorbic acid, the main hydroxyl radical quencher, works as the cofactor providing the hydroxyl radical required to collagen cross-linking; lysine thus becomes hydroxylysine.
Most microorganisms and plants can biosynthesize all 20 standard amino acids, while animals (including humans) must obtain some of the amino acids from the diet. The amino acids that an organism cannot synthesize on its own are referred to as essential amino acids. Key enzymes that synthesize certain amino acids are not present in animals—such as aspartokinase, which catalyses the first step in the synthesis of lysine, methionine, and threonine from aspartate. If amino acids are present in the environment, microorganisms can conserve energy by taking up the amino acids from their surroundings and downregulating their biosynthetic pathways.
It is estimated that approximately half of all proteins contain a metal. In another estimate, about one quarter to one third of all proteins are proposed to require metals to carry out their functions. Thus, metalloproteins have many different functions in cells, such as storage and transport of proteins, enzymes and signal transduction proteins, or infectious diseases. The abundance of metal binding proteins may be inherent to the amino acids that proteins use, as even artificial proteins without evolutionary history will readily bind metals. 
Most metals in the human body are bound to proteins. For instance, the relatively high concentration of iron in the human body is mostly due to the iron in hemoglobin.
In metalloproteins, metal ions are usually coordinated by nitrogen, oxygen or sulfur centers belonging to amino acid residues of the protein. These donor groups are often provided by side-chains on the amino acid residues. Especially important are the imidazole substituent in histidine residues, thiolate substituents in cysteine residues, and carboxylate groups provided by aspartate. Given the diversity of the metalloproteome, virtually all amino acid residues have been shown to bind metal centers. The peptide backbone also provides donor groups; these include deprotonated amides and the amide carbonyl oxygen centers. Lead(II) binding in natural and artificial proteins has been reviewed.
The daily requirement for humans to remain in nitrogen balance is relatively small. The median human adult requirement for good quality protein is approximately 0.65 gram per kilogram body weight per day and the 97.5 percentile is 0.83 grams per kilogram body weight per day.[7] Children require more protein, depending on the growth phase. A 70kg adult human who was in the middle of the range would require approximately 45 grams of protein per day to be in nitrogen balance. This would represent less than 10% of kilocalories in a notional 2,200 kilocalorie ration. William Cumming Rose and his team studied the essential amino acids, helping to define minimum amounts needed for normal health. For adults, the recommended minimum amounts of each essential amino acid varies from 4 to 39 milligrams per kilogram of body weight per day. To be of good quality, protein only needs to come from a wide variety of foods; there is neither a need to mix animal and plant food together nor a need to complement specific plant foods, such as rice and beans.[8] The notion that such specific combinations of plant protein need to be made to give good quality protein stems from the book Diet for a Small Planet. Plant protein is often described as incomplete, suggesting that they lack one or more of the essential amino acids. Apart from rare examples, such as Taro,[8][9] each plant provides an amount of all the essential amino acids. However, the relative abundance of the essential amino acids is more variable in plants than that found in animals, which tend to be very similar in essential amino acid abundance, and this has led to the misconception that plant proteins are deficient in some way.
Glutamic acid (symbol Glu or E) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is non-essential in humans, meaning the body can synthesize it. It is also an excitatory neurotransmitter, in fact the most abundant one, in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons.
DIAAS determines amino acid digestibility, at the end of the small intestine, providing a more accurate measure of the amounts of amino acids absorbed by the body and the protein’s contribution to human amino acid and nitrogen requirements. PDCAAS is based on an estimate of crude protein digestibility determined over the total digestive tract, and values stated using this method generally overestimate the amount of amino acids absorbed.
Due to proline’s cyclic structure, only few peptidases could cleave the bond between proline and other amino acids. Along with prolinase, prolidase are the only known enzymes that can break down dipeptides to yield free proline. Prolidase serve to hydrolyze both dietary and endogenous Xaa-Pro dipeptides. More specifically, it is essential in catalyzing the last step of the degradation of procollagen, collagen, and other proline-containing peptides into free amino acids to be used for cellular growth. Additionally, it also participates in the process of recycling proline from Xaa-Pro dipeptides for collagen resynthesis. Proline and hydroyxyproline make up a quarter of the amino acid residues in collagen, which is the most abundant protein in the body by mass and plays an important role in maintaining connective tissue in the body.
Glutamate is a major constituent of a wide variety of proteins; consequently it is one of the most abundant amino acids in the human body. Under ordinary conditions enough is obtained from the diet that there is no need for any to be synthesized. Nevertheless, glutamate is formally classified as a non-essential amino acid, because it can be synthesized from alpha-Ketoglutaric acid, which is produced as part of the citric acid cycle by a series of reactions whose starting point is citrate. Glutamate cannot cross the blood-brain barrier unassisted, but it is actively transported into the nervous system by a high affinity transport system, which maintains its concentration in brain fluids at a fairly constant level.
In humans, two amino acids are exclusively ketogenic:In humans, five amino acids are both ketogenic and glucogenic:In humans, the remaining thirteen amino acids are exclusively glucogenic (i.e. are not ketogenic).
Nitrogen is the lightest member of group 15 of the periodic table, often called the pnictogens. The name comes from the Greek πνίγειν "to choke", directly referencing nitrogen's asphyxiating properties. It is a common element in the universe, estimated at about seventh in total abundance in the Milky Way and the Solar System. At standard temperature and pressure, two atoms of the element bind to form dinitrogen, a colourless and odorless diatomic gas with the formula N. Dinitrogen forms about 78% of Earth's atmosphere, making it the most abundant uncombined element. Nitrogen occurs in all organisms, primarily in amino acids (and thus proteins), in the nucleic acids (DNA and RNA) and in the energy transfer molecule adenosine triphosphate. The human body contains about 3% nitrogen by mass, the fourth most abundant element in the body after oxygen, carbon, and hydrogen. The nitrogen cycle describes movement of the element from the air, into the biosphere and organic compounds, then back into the atmosphere.
Proteins are structural materials in much of the animal body (e.g. muscles, skin, and hair). They also form the enzymes that control chemical reactions throughout the body. Each protein molecule is composed of amino acids, which are characterized by inclusion of nitrogen and sometimes sulphur (these components are responsible for the distinctive smell of burning protein, such as the keratin in hair). The body requires amino acids to produce new proteins (protein retention) and to replace damaged proteins (maintenance). As there is no protein or amino acid storage provision, amino acids must be present in the diet. Excess amino acids are discarded, typically in the urine. For all animals, some amino acids are "essential" (an animal cannot produce them internally) and some are "non-essential" (the animal can produce them from other nitrogen-containing compounds). About twenty amino acids are found in the human body, and about ten of these are essential and, therefore, must be included in the diet. A diet that contains adequate amounts of amino acids (especially those that are essential) is particularly important in some situations: during early development and maturation, pregnancy, lactation, or injury (a burn, for instance). A "complete" protein source contains all the essential amino acids; an "incomplete" protein source lacks one or more of the essential amino acids.
Computational analysis revealed the most abundant amino acid to be leucine at 10.1% of the total protein. The second most abundant was serine which contributes to 8.6% of the total protein. Glutamic acid was third most abundant and contributes to 7.7% of the protein. This analysis also revealed that the protein appears to be deficient in tryptophan as it only contributes to 1.1% of the protein. Based on the distribution of other amino acid types, there were five high scoring hydrophobic segments. There were also two transmembrane domains located at 82-98aa and 432-449aa.
When taken up into the human body from the diet, the 20 standard amino acids either are used to synthesize proteins and other biomolecules or are oxidized to urea and carbon dioxide as a source of energy.[64] 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.[65] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis.[66] 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.[67][68][69] In addition, cysteine, taurine, tyrosine, and arginine are considered semiessential amino-acids in children (though taurine is not technically an amino acid), because the metabolic pathways that synthesize these amino acids are not fully developed.[70][71] 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.[72][73]
A possible way to prevent the build-up of metabolites is to limit lysine and hydroxylysine degradation, as lysine is one of the most abundant amino acids and tryptophan is one of the least abundant amino acids.
In plants and animals, the amino acids cysteine and methionine contain most of the sulfur, and the element is present in all polypeptides, proteins, and enzymes that contain these amino acids. In humans, methionine is an essential amino acid that must be ingested. However, save for the vitamins biotin and thiamine, cysteine and all sulfur-containing compounds in the human body can be synthesized from methionine. The enzyme sulfite oxidase is needed for the metabolism of methionine and cysteine in humans and animals.
The primary sequence for FAM227A is isoform 1 with accession number: NP_001013669.1. It is 570 amino acids long. There are 9 isoforms. The molecular weight is 66kD, and the isoelectric point is 9.6. Compared to other proteins in humans, FAM227A has less abundant glycine and more abundant hydrophobic amino acids and positively charges amino acids. The protein is predicted to be in the nuclear region of the cell. Three nuclear signals include HKKK at 129(pat 4), KKK at 130(pat4), and PKKTKIK at 410(pat7). An FWWh region, where h signifies hydrophobic, runs from amino acids 135-296 in Homo sapiens. Most eukaryotic proteins contain this sequence. The function of this region is still unknown. Motifs in FAM227A include KRK, SGK, and RRE.
Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. Similar to all other amino acids it contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO under physiological conditions. Aspartic acid has an acidic side chain (CHCOOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO. It is a non-essential amino acid in humans, meaning the body can synthesize it as needed. It is encoded by all the codons GAU and GAC.