Alanine - ala - A

Structural Formula:

Discovery Story: Alanine was first synthesized in 1850 when Adolph Strecker combined
acetaldehyde and ammonia with hydrogen cyanide. The amino acid was named Alanin
in German, in reference to aldehyde, with the infix -an- for ease of pronunciation, the
German ending -in used in chemical compounds being analogous to English -ine.
Major Function/s: Used in the biosynthesis of proteins.
Sources: Alanine can be synthesized from pyruvate and branched chain amino acids
such as valine, leucine, and isoleucine. Alanine is produced by reductive amination of
pyruvate, a two-step process. In the first step, α-ketoglutarate, ammonia and NADH are
converted by glutamate dehydrogenase to glutamate, NAD+ and water. In the second
step, the amino group of the newly-formed glutamate is transferred to pyruvate by an
aminotransferase enzyme, regenerating the α-ketoglutarate, and converting the
pyruvate to alanine. The net result is that pyruvate and ammonia are converted to
alanine, consuming one reducing equivalent. Because transamination reactions are
readily reversible and pyruvate is present in all cells, alanine can be easily formed and
thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the
citric acid cycle.
Arginine - arg - R

Structural Formula:

Discovery Story: Arginine was first isolated in 1886 from yellow lupin seedlings by the
German chemist Ernst Schulze and his assistant Ernst Steiger. He named it from the
Greek árgyros (ἄργυρος) meaning "silver" due to the silver-white appearance of
arginine nitrate crystals. In 1897, Schulze and Ernst Winterstein (1865–1949)
determined the structure of arginine. Schulze and Winterstein synthesized arginine from
ornithine and cyanamide in 1899, but some doubts about arginine's structure lingered
until Sørensen's synthesis of 1910.
Major Function/s: Arginine plays an important role in cell division, wound healing,
removing ammonia from the body, immune function, and the release of hormones. It is
a precursor for the synthesis of nitric oxide (NO), making it important in the regulation
of blood pressure.
Sources: Arginine is a conditionally essential amino acid in humans and rodents, as it
may be required depending on the health status or lifecycle of the individual. For
example, while healthy adults can supply their own requirement for arginine, immature
and rapidly growing individuals require arginine in their diet, and it is also essential
under physiological stress, for example during recovery from burns, injury, and sepsis,
or when the small intestine and kidneys, which are the major sites of arginine
biosynthesis, have been damaged. It is, however, an essential amino acid for birds, as
they do not have a urea cycle. For some carnivores, for example cats, dogs and ferrets,
arginine is essential, because after a meal, their highly efficient protein catabolism
produces large quantities of ammonia which need to be processed through the urea
cycle, and if not enough arginine is present, the resulting ammonia toxicity can be
lethal. This is not a problem in practice, because meat contains sufficient arginine to
avoid this situation. Animal sources of arginine include meat, dairy products, and eggs,
and plant sources include seeds of all types, for example grains, beans, and nuts.
Asparagine - asn - N

Structural Formula:

Discovery Story: Asparagine was first isolated in 1806 in a crystalline form by French
chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet (then a young assistant)
from asparagus juice, in which it is abundant, hence the chosen name. It was the first
amino acid to be isolated. The empirical formula for asparagine was first determined in
1833 by the French chemists Antoine François Boutron Charlard and Théophile-Jules
Pelouze; in the same year, the German chemist Justus Liebig provided a more accurate
formula. In 1846 the Italian chemist Raffaele Piria treated asparagine with nitrous acid,
which removed the molecule's amine (–NH2) groups and transformed asparagine into
malic acid. This revealed the molecule's fundamental structure: a chain of four carbon
atoms. Piria thought that asparagine was a diamide of malic acid; however, in 1862 the
German chemist Hermann Kolbe showed that this surmise was wrong; instead, Kolbe
concluded that asparagine was an amide of an amine of succinic acid. In 1886, the
Italian chemist Arnaldo Piutti (1857–1928) discovered a mirror image or "enantiomer"
of the natural form of asparagine, which shared many of asparagine's properties, but
which also differed from it. Since the structure of asparagine was still not fully known –
the location of the amine group within the molecule was still not settled – Piutti
synthesized asparagine and thus determined its true structure.
Major Function/s: Asparagine is required for development and function of the brain. It
also plays an important role in the synthesis of ammonia.
Sources: Asparagine is not essential for humans, which means that it can be
synthesized from central metabolic pathway intermediates and is not required in the
diet. The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to
aspartate using a transaminase enzyme. The enzyme transfers the amino group from
glutamate to oxaloacetate producing α-ketoglutarate and aspartate. The enzyme
asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from
aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to
activate aspartate, forming β-aspartyl-AMP. Glutamine donates an ammonium group,
which reacts with β-aspartyl-AMP to form asparagine and free AMP.
Aspartic acid - asp - D

Structural Formula:

Discovery Story: Aspartic acid was first discovered in 1827 by Auguste-Arthur Plisson
and Étienne Ossian Henry by hydrolysis of asparagine, which had been isolated from
asparagus juice in 1806. Their original method used lead hydroxide, but various other
acids or bases are more commonly used instead.
Major Function/s: Aspartic acid also participates in the ornithine cycle, in transamination
reactions, as well as in the formation of pyrimidines, purines, carnosine, and anserine.
This amino acid is necessary for stamina, brain and neural health.
Sources: Aspartic acid is not an essential amino acid, which means that it can be
synthesized from central metabolic pathway intermediates in humans. However,
aspartic acid is found in:
Animal sources: oysters, luncheon meats, sausage meat, wild game
Vegetable sources: sprouting seeds, oat flakes, avocado, asparagus, young
sugarcane, and molasses from sugar beets.
Dietary supplements, either as aspartic acid itself or salts (such as magnesium
aspartate)
The sweetener aspartame, an aspartic acid, phenylalanine, formaldehyde trimer
(brands: NutraSweet, Equal, Canderel, etc.)
Cysteine - cys - C

Structural Formula:

Discovery Story: Cystine can be converted to cysteine by reduction (in this case, the
addition of hydrogen). Discovered in 1810, cystine was not recognized as a component
of proteins until 1899, when it was isolated from animal horn.
Major Function/s: The cysteine sulfhydryl group is nucleophilic and easily oxidized. The
reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have
pKa values close to neutrality, so are often in their reactive thiolate form in the cell.
Because of its high reactivity, the sulfhydryl group of cysteine has numerous biological
functions, and cysteine may have played an important role in the development of
primitive life on Earth.
Sources: Like other common amino acids, cysteine (and its oxidized dimeric form
cystine) is found in high-protein foods. Although classified as a nonessential amino acid,
in rare cases, cysteine may be essential for infants, the elderly, and individuals with
certain metabolic diseases or who suffer from malabsorption syndromes. Cysteine can
usually be synthesized by the human body under normal physiological conditions if a
sufficient quantity of methionine is available.
Glutamine - gln - Q
Structural Formula:

Discovery Story: Glutamine was first discovered by Schulze in 1883, who managed to
isolate it from the beet juice. Later on, it turned out that glutamine can also be found in
abundance in a wheat gliadin. Finally, in 1935, the synthesis of glutamine from
ammonium and glutamate was explained and described by Krebs, who used the guinea
pig and the rat kidney in his research.
Major Function/s: Protein synthesis, as any other of the 20 proteinogenic amino acids,
Lipid synthesis, especially by cancer cells. Regulation of acid-base balance in the kidney
by producing ammonium, Cellular energy, as a source, next to glucose, Nitrogen
donation for many anabolic processes, including the synthesis of purines, Carbon
donation, as a source, refilling the citric acid cycle, Nontoxic transporter of ammonia in
the blood circulation, and Precursor to the neurotransmitter glutamate. On the level of
tissue, glutamine plays a role in maintaining the normal integrity of the intestinal
mucosa, but randomized trials provide no evidence of any benefit of nutritional
supplementation.
Sources: Glutamine is produced industrially using mutants of Brevibacterium flavum,
which gives ca. 40 g/L in 2 days using glucose as a carbon source.[13] Glutamine is
synthesized by the enzyme glutamine synthetase from glutamate and ammonia. The
most relevant glutamine-producing tissue is the muscle mass, accounting for about
90% of all glutamine synthesized. Glutamine is also released, in small amounts, by the
lungs and brain.[14] Although the liver is capable of relevant glutamine synthesis, its
role in glutamine metabolism is more regulatory than producing, since the liver takes up
large amounts of glutamine derived from the gut.
Glutamic acid - glu - E
Structural Formula:

Discovery Story: Although they occur naturally in many foods, the flavor contributions
made by glutamic acid and other amino acids were only scientifically identified early in
the twentieth century. The substance was discovered and identified in the year 1866,
by the German chemist Karl Heinrich Ritthausen who treated wheat gluten (for which it
was named) with sulfuric acid. In 1908 Japanese researcher Kikunae Ikeda of the Tokyo
Imperial University identified brown crystals left behind after the evaporation of a large
amount of kombu broth as glutamic acid. These crystals, when tasted, reproduced the
ineffable but undeniable flavor he detected in many foods, most especially in seaweed.
Professor Ikeda termed this flavor umami. He then patented a method of mass-
producing a crystalline salt of glutamic acid, monosodium glutamate.
Major Function/s: Metabolism- Glutamate is a key compound in cellular metabolism. In
humans, dietary proteins are broken down by digestion into amino acids, which serve
as metabolic fuel for other functional roles in the body. Neurotransmitter- Glutamate is
the most abundant excitatory neurotransmitter in the vertebrate nervous system. At
chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of
glutamate from the presynaptic cell. Flavor enhancer- Glutamic acid, being a constituent
of protein, is present in foods that contain protein, but it can only be tasted when it is
present in an unbound form. Significant amounts of free glutamic acid are present in a
wide variety of foods, including cheeses and soy sauce, and glutamic acid is responsible
for umami, one of the five basic tastes of the human sense of taste. Glutamic acid often
is used as a food additive and flavor enhancer in the form of its sodium salt, known as
monosodium glutamate (MSG).
Sources: All meats, poultry, fish, eggs, dairy products, and kombu are excellent sources
of glutamic acid. Some protein-rich plant foods also serve as sources. 30% to 35% of
gluten (much of the protein in wheat) is glutamic acid.
Glycine - gly - G
Structural Formula:

Discovery Story: Glycine was discovered in 1820 by the French chemist Henri Braconnot
when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar
of gelatin", but the French chemist Jean-Baptiste Boussingault showed that it contained
nitrogen. The American scientist Eben Norton Horsford, then a student of the German
chemist Justus von Liebig, proposed the name "glycocoll"; however, the Swedish
chemist Berzelius suggested the simpler name "glycine". The name comes from the
Greek word γλυκύς "sweet tasting" (which is also related to the prefixes glyco- and
gluco-, as in glycoprotein and glucose). In 1858, the French chemist Auguste Cahours
determined that glycine was an amine of acetic acid.
Major Function/s: The principal function of glycine is as a precursor to proteins. Most
proteins incorporate only small quantities of glycine, a notable exception being collagen,
which contains about 35% glycine due to its periodically repeated role in the formation
of collagen's helix structure in conjunction with hydroxyproline. In the genetic code,
glycine is coded by all codons starting with GG, namely GGU, GGC, GGA and GGG.
Sources: We also consume glycine through food. This amino acid is found in high-
protein foods including meat, fish, eggs, dairy and legumes.
Histidine - his - H
Structural Formula:

Discovery Story: The amino acid L-histidine (His) was discovered independently by
Kossel and Hedin in 1896. ... The unprotonated imidazole group is nucleophilic, and can
thus act as a general base, for example in catalytic triads where the basic N abstracts
protons from Ser, Thr or Cys residues, while the protonated form is a general acid.
Major Function/s: Histidine, is an essential amino acid that is not synthesized de novo in
humans. Humans and other animals must ingest histidine or histidine-containing
proteins. The biosynthesis of histidine has been widely studied in prokaryotes such as E.
coli. Histidine synthesis in E. coli involves eight gene products (His1, 2, 3, 4, 5, 6, 7,
and 8) and it occurs in ten steps. This is possible because a single gene product has the
ability to catalyze more than one reaction. For example, as shown in the pathway, His4
catalyzes 4 different steps in the pathway.
Sources: Meat, fish, poultry, nuts, seeds, and whole grains contain large amounts of
histidine. Cottage cheese and wheat germ contain high quantities of threonine.
Methionine is in eggs, grains, nuts, and seeds.
Isoleucine - ile - I
Structural Formula:

Discovery Story: Isoleucine. Ehrlich was the first one who discovered Isoleucine in 1904,
with its composition being established three years later obtained by a degradation to d-
isoamylamine and consequent synthesis through the Strecker reaction with d-
isovaleraldehyde.
Major Function/s: Biosynthesis- As an essential nutrient, it is not synthesized in the
body, hence it must be ingested, usually as a component of proteins. In plants and
microorganisms, it is synthesized via several steps, starting from pyruvic acid and
alpha-ketoglutarate. Catabolism- Isoleucine is both a glucogenic and a ketogenic amino
acid. After transamination with alpha-ketoglutarate the carbon skeleton can be
converted into either succinyl CoA, and fed into the TCA cycle for oxidation or converted
into oxaloacetate for gluconeogenesis (hence glucogenic). It can also be converted into
acetyl CoA and fed into the TCA cycle by condensing with oxaloacetate to form citrate.
In mammals Acetyl CoA cannot be converted back to carbohydrate but can be used in
the synthesis of ketone bodies or fatty acids, hence ketogenic.
Sources: Even though this amino acid is not produced in animals, it is stored in high
quantities. Foods that have high amounts of isoleucine include eggs, soy protein,
seaweed, turkey, chicken, lamb, cheese, and fish.
Leucine - leu - L
Structural Formula:

Discovery Story: Leucine is an amino acid which was discovered in its impure form in
cheese back in 1819, and just a year later - in its crystalline form from muscles and
wool. ... Only in the end of the 19th century the structure of Leucine was established by
laboratory synthesis.
Major Function/s: Leucine is considered a vital amino acid for the protein synthesis and
various metabolic functions - in other words, it is an essential amino acid, which helps
in regulating the blood-sugar levels, promotes the growth and the recovery of muscle
and bone tissues, as well as the production of the growth hormone.
Sources: Whey protein concentrate, dry powder
Soy protein concentrate, dry powder
Pea protein concentrate, dry powder
Soybeans, mature seeds, roasted, salted
Hemp seed, hulled
Lysine - lys - K
Structural Formula:

Discovery Story: The past 50 years following the discovery of C.glutamicum were
characterized by a huge progress towards understanding the physiology of this
organism and developing and optimizing industrial production strains. This has resulted
in effective biotechnological processes currently used for producing about 750 000 tons
of lysine per year.
Major Function/s: Determines gene expression, genomic stability, stem cell maturation,
cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.
Sources: Meat, specifically red meat, pork, and poultry. Cheese, particularly parmesan.
Certain fish, such as cod and sardines. Eggs. Soybeans, particularly tofu, isolated soy
protein, and defatted soybean flour. Spirulina. Fenugreek seed.
Methionine - met - M
Structural Formula:

Discovery Story: Methionine was discovered in 1921 by Mueller in the course of his
search for a growth-promoting factor found in some proteins. The isolation of
methionine from enzymatic digests of protein removes any doubt that methionine is a
primary protein decom- position product and not the result of secondary reactions.
Major Function/s: Methionine is sometimes given as a supplement to dogs; It helps to
reduce the chances of stones in dogs. Methionine is also known to increase the urinary
excretion of quinidine by acidifying the urine. Aminoglycoside antibiotics used to treat
urinary tract infections work best in alkaline conditions, and urinary acidification from
using methionine can reduce its effectiveness. If a dog is on a diet that acidifies the
urine, methionine should not be used. Methionine is allowed as a supplement to organic
poultry feed under the US certified organic program. Methionine can be used as a
nontoxic pesticide option against giant swallowtail caterpillars, which are a serious pest
to orange crops.
Sources: High levels of methionine can be found in eggs, meat, and fish; sesame seeds,
Brazil nuts, and some other plant seeds; and cereal grains. Most fruits and vegetables
contain very little. Most legumes, though protein dense, are low in methionine.
Phenylalanine - phe - F
Structural Formula:

Discovery Story: The first description of phenylalanine was made in 1879, when Schulze
and Barbieri identified a compound with the empirical formula, C9H11NO2, in yellow
lupine (Lupinus luteus) seedlings. In 1882, Erlenmeyer and Lipp first synthesized
phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia. The genetic
codon for phenylalanine was first discovered by J. Heinrich Matthaei and Marshall W.
Nirenberg in 1961. They showed that by using mRNA to insert multiple uracil repeats
into the genome of the bacterium E. coli, they could cause the bacterium to produce a
polypeptide consisting solely of repeated phenylalanine amino acids. This discovery
helped to establish the nature of the coding relationship that links information stored in
genomic nucleic acid with protein expression in the living cell.
Major Function/s: Phenylalanine is biologically converted into L-tyrosine, another one of
the DNA-encoded amino acids. L-tyrosine in turn is converted into L-DOPA, which is
further converted into dopamine, norepinephrine (noradrenaline), and epinephrine
(adrenaline). The latter three are known as the catecholamines.
Sources: Good sources of phenylalanine are eggs, chicken, liver, beef, milk, and
soybeans. Another common source of phenylalanine is anything sweetened with the
artificial sweetener aspartame, such as diet drinks, diet foods and medication; the
metabolism of aspartame produces phenylalanine as one of the compound's
metabolites.
Proline - pro - P
Structural Formula:

Discovery Story: Proline was first isolated in 1900 by Richard Willstätter who obtained
the amino acid while studying N-methylproline. The year after Emil Fischer published
the synthesis of proline from phthalimide propylmalonic ester. The name proline comes
from pyrrolidine, one of its constituents.
Major Function/s: Proline and its derivatives are often used as asymmetric catalysts in
proline organocatalysis reactions. The CBS reduction and proline catalysed aldol
condensation are prominent examples. In brewing, proteins rich in proline combine with
polyphenols to produce haze (turbidity). L-Proline is an osmoprotectant and therefore is
used in many pharmaceutical, biotechnological applications. The growth medium used
in plant tissue culture may be supplemented with proline. This can increase growth,
perhaps because it helps the plant tolerate the stresses of tissue culture.
Sources: Pork Products, Lamb, Veal, and Game Products, Sausages and Luncheon
Meats, Dairy and Egg Products
Serine - ser - S
Structural Formula:

Discovery Story: Serine was first discovered in nature, specifically in silk protein, by
German chemist Emil Cramer in 1865.
Major Function/s: Serine deficiency disorders are rare defects in the biosynthesis of the
amino acid L-serine. At present three disorders have been reported: 3-
phosphoglycerate dehydrogenase deficiency, 3-phosphoserine phosphatase deficiency
and Phosphoserine aminotransferase deficiency. These enzyme defects lead to severe
neurological symptoms such as congenital microcephaly and severe psychomotor
retardation and in addition in patients with 3-phosphoglycerate dehydrogenase
deficiency to intractable seizures. These symptoms respond to a variable degree to
treatment with L-serine, sometimes combined with glycine.
Sources: Serine is found in soybeans, nuts (especially peanuts, almonds, and walnuts),
eggs, chickpeas, lentils, meat, and fish (especially shellfish).
Threonine - thr - T
Structural Formula:

Discovery Story: Threonine was the last of the 20 common proteinogenic amino acids to
be discovered. It was discovered in 1936 by William Cumming Rose, collaborating with
Curtis Meyer. The amino acid was named threonine because it was similar in structure
to threonic acid, a four-carbon monosaccharide with molecular formula C4H8O5.
Major Function/s: As an essential amino acid, threonine is not synthesized in humans,
and needs to be present in proteins in the diet. Adult humans require about 20 mg/kg
body weight/day. In plants and microorganisms, threonine is synthesized from aspartic
acid via α-aspartyl-semialdehyde and homoserine.
Sources: Foods high in threonine include cottage cheese, poultry, fish, meat, lentils,
black turtle bean and sesame seeds. Racemic threonine can be prepared from crotonic
acid by alpha-functionalization using mercury(II) acetate.
Tryptophan - trp - W
Structural Formula:

Discovery Story: Tryptophan was first isolated in 1901, from the milk protein casein, by
Sir Frederick Gowland Hopkins. He was awarded the Nobel Prize for his discovery of
vitamins, produced by amino acids like tryptophan. Tryptophan was widely available as
a nutritional supplement throughout the 1980's.
Major Function/s: Tryptophan is among the less common amino acids found in proteins,
but it plays important structural or functional roles whenever it occurs. For instance,
tryptophan and tyrosine residues play special roles in "anchoring" membrane proteins
within the cell membrane.
Sources: Tryptophan is present in most protein-based foods or dietary proteins. It is
particularly plentiful in chocolate, oats, dried dates, milk, yogurt, cottage cheese, red
meat, eggs, fish, poultry, sesame, chickpeas, almonds, sunflower seeds, pumpkin
seeds, buckwheat, spirulina, and peanuts. Contrary to the popular belief that cooked
turkey contains an abundance of tryptophan (with this being used as an explanation for
sleepiness following consumption of the meat), the tryptophan content in turkey is
typical of poultry.
Tyrosine - tyr - Y
Structural Formula:

Discovery Story: Like most natural amino acids, the α carbon atom in tyrosine has the L-
configuration; but its enantiomer, D-tyrosine, also occurs in nature. In 1846, German
chemist J. von Liebig discovered L-tyrosine in casein obtained from cheese. In plants,
the amino acid is an electron donor in the process of photosynthesis.
Major Function/s: Aside from being a proteinogenic amino acid, tyrosine has a special
role by virtue of the phenol functionality. It occurs in proteins that are part of signal
transduction processes and functions as a receiver of phosphate groups that are
transferred by way of protein kinases. Phosphorylation of the hydroxyl group can
change the activity of the target protein, or may form part of a signaling cascade via
SH2 domain binding. A tyrosine residue also plays an important role in photosynthesis.
In chloroplasts (photosystem II), it acts as an electron donor in the reduction of
oxidized chlorophyll. In this process, it loses the hydrogen atom of its phenolic OH-
group. This radical is subsequently reduced in the photosystem II by the four core
manganese clusters.
Sources: The Dietary Reference Intake (recommended dietary allowance, RDA) for
phenylalanine and tyrosine is 33 mg per kilogram of body weight, or 15 mg per pound
for a 70 kg person, this is 2.31 g (phenylalanine + tyrosine). Tyrosine, which can also
be synthesized in the body from phenylalanine, is found in many high-protein food
products such as chicken, turkey, fish, milk, yogurt, cottage cheese, cheese, peanuts,
almonds, pumpkin seeds, sesame seeds, soy products and lima beans, but also in
avocados and bananas. For example, the white of an egg has about 250 mg per egg,
while lean beef/lamb/pork/salmon/chicken/turkey contains about 1 g per 3 ounces (85
g) portion.
Valine - val - V
Structural Formula:

Discovery Story: Valine was first isolated from casein in 1901 by Hermann Emil Fischer.
The name valine comes from valeric acid, which in turn is named after the plant
valerian due to the presence of the acid in the roots of the plant.
Major Function/s: Insulin resistance- Valine, like other branched-chain amino acids, is
associated with insulin resistance: higher levels of valine are observed in the blood of
diabetic mice, rats, and humans. Mice fed a valine deprivation diet for one day have
improved insulin sensitivity, and feeding of a valine deprivation diet for one week
significantly decreases blood glucose levels. In diet-induced obese and insulin resistant
mice, a diet with decreased levels of valine and the other branched-chain amino acids
results in reduced adiposity and improved insulin sensitivity. The valine catabolite 3-
hydroxyisobutyrate promotes skeletal muscle insulin resistance in mice by stimulating
fatty acid uptake into muscle and lipid accumulation. In humans, a protein restricted
diet lowers blood levels of valine and decreases fasting blood glucose levels.
Hematopoietic stem cells- Dietary valine is essential for hematopoietic stem cell (HSC)
self-renewal, as demonstrated by experiments in mice. Dietary valine restriction
selectively depletes long-term repopulating HSC in mouse bone marrow. Successful
stem cell transplantation was achieved in mice without irradiation after 3 weeks on a
valine restricted diet. Long term survival of the transplanted mice was achieved when
valine was returned to the diet gradually over a 2-week period to avoid refeeding
syndrome.
Sources: Valine is in soy, cheese, peanuts, mushrooms, whole grains, and vegetables.
Isoleucine is plentiful in meat, fish, poultry, eggs, cheese, lentils, nuts, and seeds.
Dairy, soy, beans, and legumes are sources of leucine.