Essential amino acid

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized de novo (from scratch) by the organism, and thus must be supplied in its diet. The nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine (i.e., F V T W M L I K H).[1][2]

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.[2] These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine (i.e., R C G Q P Y). Five amino acids are dispensable in humans, meaning they can be synthesized in the body. These five are alanine, aspartic acid, asparagine, glutamic acid and serine (i.e., A D N E S).[2]

Essentiality in humans

Essential Non-Essential
Histidine (H) Alanine (A)
Isoleucine (I) Arginine* (R)
Leucine (L) Aspartic acid (D)
Lysine (K) Cysteine* (C)
Methionine (M) Glutamic acid (E)
Phenylalanine (F) Glutamine* (Q)
Threonine (T) Glycine* (G)
Tryptophan (W) Proline* (P)
Valine (V) Serine* (S)
Tyrosine* (Y)
Asparagine* (N)
Selenocysteine (U)
Pyrrolysine** (O)

(*) Essential only in certain cases.[3][4]

(**) Pyrrolysine, sometimes considered "the 22nd amino acid", is not used by humans.[5]

Eukaryotes can synthesize some of the amino acids from other substrates. Consequently, only a subset of the amino acids used in protein synthesis are essential nutrients.

Estimating the daily requirement for the indispensable amino acids has proven to be difficult; these numbers have undergone considerable revision over the last 20 years. The following table lists the WHO and United States recommended daily amounts currently in use for essential amino acids in adult humans, together with their standard one-letter abbreviations.[6][7] Food sources are identified based on the USDA National Nutrient Database Release.

Amino acid(s) WHO mg per kg body weight WHO mg per 70 kg US mg per kg body weight
H Histidine 10 700 14
I Isoleucine 20 1400 19
L Leucine 39 2730 42
K Lysine 30 2100 38
M Methionine

+ C Cysteine

 10.4 + 4.1 (15 total) 1050 total 19 total
F Phenylalanine

+ Y Tyrosine

 25 (total) 1750 total 33 total
T Threonine 15 1050 20
W Tryptophan 4 280 5
V Valine 26 1820 4

The recommended daily intakes for children aged three years and older is 10% to 20% higher than adult levels and those for infants can be as much as 150% higher in the first year of life. Cysteine (or sulphur-containing amino acids), tyrosine (or aromatic amino acids), and arginine are always required by infants and growing children.[6][8]

Relative amino acid composition of protein sources

Various attempts have been made to express the "quality" or "value" of various kinds of protein. Measures include the biological value, net protein utilization, protein efficiency ratio, protein digestibility-corrected amino acid score and complete proteins concept. These concepts are important in the livestock industry, because the relative lack of one or more of the essential amino acids in animal feeds would have a limiting effect on growth and thus on feed conversion ratio. Thus, various feedstuffs may be fed in combination to increase net protein utilization, or a supplement of an individual amino acid (methionine, lysine, threonine, or tryptophan) can be added to the feed.

Although proteins from plant sources tend to have a relatively lower concentrations of protein by mass in comparison to protein from eggs or milk, they are nevertheless "complete" in that they contain at least trace amounts of all of the amino acids that are essential in human nutrition.[9] Eating various plant foods in combination can provide a protein of higher biological value.[10] Certain native combinations of foods, such as corn and beans, soybeans and rice, or red beans and rice, contain the essential amino acids necessary for humans in adequate amounts.[11]

Additionally, certain types of algae and marine phytoplankton predate the division between animal and plant life on the planet; they have both chlorophyll as do plants, and also all the essential amino acids, as do animal proteins.

Protein per calorie

It can be shown that common vegetable sources contain adequate protein, often more protein per Calorie than the standard reference, whole raw egg, while other plant sources, particularly fruits contain less. For example, while 100 g of raw broccoli only provides 28 kcal and 3 g of protein, it has over 100 mg of protein per kcal. An egg contains five times as many calories (143 kcal) but only four times as much protein, roughly 90 mg of protein per kcal. However, a carrot has only 23 mg protein per kcal or twice the minimum recommendation, a banana meets the minimum, and an apple is below recommendation.[12] It is recommended that adult humans obtain 10–35% of their calories as protein, or roughly 11–39 mg of protein per kcal per day (22–78 g for 2000 kcal).[13] The US FDA daily reference value of 50 g protein per 2000 kcal is 25 mg/kcal per day.[14]

Source protein (g) Calories (kcal) protein/Calorie
(mg / kcal)		 L (mg) T (mg) W (mg) M+C (mg)
Apples, raw (100 g) 0.26 52 5 12 6 1 2
Minimum daily reference 22 2000 11
Bananas, raw (100 g) 1 89 11 500 28 9 17
Carrot, raw (100 g) 1 41 24 101 191 12 103
US FDA daily / WHO (70 kg) 50 2000 25 2730 1050 280 1050
Upper daily reference 78 2000 39
Peanut, valencia, raw (100 g) 48 570 84 1,627 859 244 630
Soybeans, mature seeds, dry roasted (100 g) 43 449 96 3223 1719 575 1172
Egg, whole, raw (100 g) 13 143 91 912 556 167 652
Broccoli, raw (100 g) 3 28 107 141 91 29 54
Soy Sauce, typical (100 g) 11 60 183 729 403 182 576
Beef, Australian, imported, grass-fed, ground, 85% lean / 15% fat, raw (100 g) 18 234 77 1430 780 200 690

Complete proteins in non-human animals

Scientists had known since the early 20th century that rats could not survive on a diet whose only protein source was zein, which comes from maize (corn), but recovered if they were fed casein from cow's milk. This led William Cumming Rose to the discovery of the essential amino acid threonine.[15] Through manipulation of rodent diets, Rose was able to show that ten amino acids are essential for rats: lysine, tryptophan, histidine, phenylalanine, leucine, isoleucine, methionine, valine, and arginine, in addition to threonine. Rose's later work showed that eight amino acids are essential for adult human beings, with histidine also being essential for infants. Longer term studies established histidine as also essential for adult humans.[16]

Interchangeability

The distinction between essential and non-essential amino acids is somewhat unclear, as some amino acids can be produced from others. The sulfur-containing amino acids, methionine and homocysteine, can be converted into each other but neither can be synthesized de novo in humans. Likewise, cysteine can be made from homocysteine but cannot be synthesized on its own. So, for convenience, sulfur-containing amino acids are sometimes considered a single pool of nutritionally equivalent amino acids as are the aromatic amino acid pair, phenylalanine and tyrosine. Likewise arginine, ornithine, and citrulline, which are interconvertible by the urea cycle, are considered a single group.

Effects of deficiency

If one of the essential amino acids is less than needed for an individual the utilization of other amino acids will be hindered and thus protein synthesis will be less than what it usually is, even in the presence of adequate total nitrogen intake.[2]

Protein deficiency has been shown to affect all of the body's organs and many of its systems, including the brain and brain function of infants and young children; the immune system, thus elevating risk of infection; gut mucosal function and permeability, which affects absorption and vulnerability to systemic disease; and kidney function.[2] The physical signs of protein deficiency include edema, failure to thrive in infants and children, poor musculature, dull skin, and thin and fragile hair. Biochemical changes reflecting protein deficiency include low serum albumin and low serum transferrin.[2]

The amino acids that are essential in the human diet were established in a series of experiments led by William Cumming Rose. The experiments involved elemental diets to healthy male graduate students. These diets consisted of cornstarch, sucrose, butterfat without protein, corn oil, inorganic salts, the known vitamins, a large brown "candy" made of liver extract flavored with peppermint oil (to supply any unknown vitamins), and mixtures of highly purified individual amino acids. The main outcome measure was nitrogen balance. Rose noted that the symptoms of nervousness, exhaustion, and dizziness were encountered to a greater or lesser extent whenever human subjects were deprived of an essential amino acid.[17]

Essential amino acid deficiency should be distinguished from protein-energy malnutrition, which can manifest as marasmus or kwashiorkor. Kwashiorkor was once attributed to pure protein deficiency in individuals who were consuming enough calories ("sugar baby syndrome"). However, this theory has been challenged by the finding that there is no difference in the diets of children developing marasmus as opposed to kwashiorkor.[18] Still, for instance in Dietary Reference Intakes (DRI) maintained by the USDA, lack of one or more of the essential amino acids is described as protein-energy malnutrition.[2]

See also

References

  1. ↑ Young VR (1994). "Adult amino acid requirements: the case for a major revision in current recommendations" (PDF). J. Nutr. 124 (8 Suppl): 1517S–1523S. PMID 8064412.
  2. 1 2 3 4 5 6 7 Dietary Reference Intakes: The Essential Guide to Nutrient Requirements. Institute of Medicine's Food and Nutrition Board. usda.gov
  3. ↑ Fürst P, Stehle P (1 June 2004). "What are the essential elements needed for the determination of amino acid requirements in humans?". Journal of Nutrition. 134 (6 Suppl): 1558S–1565S. PMID 15173430.
  4. ↑ Reeds PJ (1 July 2000). "Dispensable and indispensable amino acids for humans". J. Nutr. 130 (7): 1835S–40S. PMID 10867060.
  5. ↑ Richard Cammack. "Newsletter 2009, Biochemical Nomenclature Committee of IUPAC and NC-IUBMB".
  6. 1 2 FAO/WHO/UNU (2007). "PROTEIN AND AMINO ACID REQUIREMENTS IN HUMAN NUTRITION" (PDF). WHO Press., page 150
  7. ↑ Institute of Medicine (2002). "Protein and Amino Acids". Dietary Reference Intakes for Energy, Carbohydrates, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids. Washington, DC: The National Academies Press. pp. 589–768.
  8. ↑ Imura K, Okada A (1998). "Amino acid metabolism in pediatric patients". Nutrition. 14 (1): 143–8. PMID 9437700. doi:10.1016/S0899-9007(97)00230-X.
  9. ↑ McDougall J. Plant foods have a complete amino acid composition. Circulation. 2002;105(25):e197
  10. ↑ Woolf, P. J.; Fu, L. L.; Basu, A. (2011). Haslam, Niall James, ed. "VProtein: Identifying Optimal Amino Acid Complements from Plant-Based Foods". PLoS ONE. 6 (4): e18836. PMC 3081312 Freely accessible. PMID 21526128. doi:10.1371/journal.pone.0018836.
  11. ↑ Essential Amino Acids. phy-astr.gsu.edu: "Tillery points out that a number of popular ethnic foods involve such a combination, so that in a single dish, one might hope to get the ten essential amino acids. Mexican corn and beans, Japanese rice and soybeans, and Cajun red beans and rice are examples of such fortuitous combinations."
  12. ↑ "USDA National Nutrient Database". USDA.gov. 2015-03-31. Retrieved 2015-03-31.
  13. ↑ "Web MD Protein: Are You Getting Enough?". webmd.com. 2014-09-05. Retrieved 2015-03-31.
  14. ↑ "Information for Consumers (Drugs)". Fda.gov. 2008-10-29. Retrieved 2011-03-30.
  15. ↑ Rose WC, Haines WJ, Warner DT, Johnson JE (1951). "The amino acid requirements of man. II. The role of threonine and histidine". The Journal of biological chemistry. 188 (1): 49–58. PMID 14814112.
  16. ↑ Kopple JD, Swendseid ME (May 1975). "Evidence that histidine is an essential amino acid in normal and chronically uremic man.". J Clin Invest. 55 (5): 881–891. PMC 301830 Freely accessible. PMID 1123426. doi:10.1172/JCI108016.
  17. ↑ Rose, WC; Haines, WJ; Warner, DT (1951). "The amino acid requirements of man. III. The role of isoleucine; additional evidence concerning histidine" (PDF). J Biol Chem. 193 (2): 605–612. PMID 14907749. Retrieved 15 Dec 2012.
  18. ↑ Ahmed T, Rahman S, Cravioto A (2009). "Oedematous malnutrition". The Indian journal of medical research. 130 (5): 651–4. PMID 20090122.

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