Nepedia
Back to Discover
Advanced Reader
🧬

Tryptophan

life science Maturity 11-13 climate Next article →

This article covers sensitive topics: climate. Parents can manage visibility in Parental Controls.

Tryptophan is a specific type of alpha-amino acid used in the biosynthesis of proteins.

Tryptophan-spin
Tryptophan-spin

Proteins are the fundamental building blocks required to sustain all forms of life. Tryptophan is considered a polar molecule, but it features a non-polar aromatic beta carbon substituent. It is one of the less common amino acids found within proteins. However, it performs vital structural and functional roles whenever it is present. For example, tryptophan and tyrosine residues help anchor membrane proteins within a cell membrane. It is also important for glycan-protein interactions.

Tryptophan serves as a biochemical precursor for several critical substances in the body. A precursor is a starting material that is transformed into something else through chemical reactions. First, it is converted into serotonin, which is a neurotransmitter used to carry messages in the brain. This conversion is performed by the enzyme tryptophan hydroxylase. Next, serotonin can be synthesized into melatonin, a neurohormone, via the enzymes N-acetyltransferase and 5-hydroxyindole-O-methyltransferase.

Tryptophan metabolism
Tryptophan metabolism

Tryptophan can also be used to produce niacin, which is also known as vitamin B3. Most tryptophan, specifically more than 95 percent, is metabolized into a substance called kynurenine.

The metabolism of tryptophan involves several specific enzymatic pathways. The synthesis of kynurenine from tryptophan is handled by two different enzymes. One is indoleamine 2,3-dioxygenase, or IDO, which functions in the brain and the immune system. The other is tryptophan 2,3-dioxygenase, or TDO, which is responsible for synthesis in the liver. Changes in the kynurenine pathway are linked to various psychiatric disorders. These include major depressive disorder, bipolar disorder, and schizophrenia. Additionally, tryptophan is used by plants to synthesize a class of phytohormones known as auxins.

In the world of microbiology, bacteria use a highly regulated system to manage tryptophan levels. This system involves the trp operon, which is a specific segment of DNA. When cellular levels of tryptophan become high, a repressor protein is activated. This protein binds to the trp operon to prevent the transcription of DNA. This DNA is what codes for the enzymes used in tryptophan biosynthesis. This process creates a negative feedback loop to prevent the cell from wasting energy. When levels drop, the transcription of the operon resumes to restore balance.

History shows that tryptophan was first isolated in 1901 by Frederick Hopkins. He recovered the substance from hydrolyzed casein proteins. From 600 grams of crude casein, he was able to recover between 4 and 8 grams of tryptophan. The name is derived from trypsin, a digestive enzyme used in its isolation. It is assigned the one-letter symbol W in scientific notation. This is because its bulky double-ring structure is visually similar to the letter W.

Because humans and many animals cannot synthesize tryptophan internally, it is an essential amino acid. This means it must be obtained through the diet. In 2002, the U.S. Institute of Medicine set a Recommended Dietary Allowance of 5 mg per kilogram of body weight per day for adults. Tryptophan is found in many protein-based foods. It is particularly plentiful in oats, chocolate, milk, and yogurt. It is also found in red meat, eggs, fish, and various seeds like chia and pumpkin seeds.

Tryptophan-spin
Tryptophan-spin

There is a popular belief that eating turkey causes drowsiness due to high tryptophan levels. However, the amount of tryptophan in turkey is actually typical for poultry. The drowsiness might actually result from eating large amounts of carbohydrates with the meal. Ingesting carbohydrates triggers the release of insulin. Insulin stimulates the uptake of branched-chain amino acids into the muscles, but it does not affect tryptophan. This leaves a higher ratio of tryptophan in the bloodstream. This increased ratio allows more tryptophan to cross the blood-brain barrier into the cerebrospinal fluid. Once there, it is converted into serotonin and then into melatonin, which helps regulate sleep cycles.

Industrial production of tryptophan relies on biosynthetic methods. Scientists use the fermentation of indole and serine to create it. This process often uses bacteria such as E. coli, B. subtilis, or C. glutamicum.

Tryptophan biosynthesis (en)
Tryptophan biosynthesis (en)

These bacteria are sometimes genetically modified to prevent them from reabsorbing aromatic amino acids. This allows for a more efficient harvest of the amino acid. While tryptophan is used in many supplements, users should be aware of potential side effects. These can include nausea, drowsiness, headache, or even involuntary eye movements called nystagmus.

728 words

Where will your curiosity go next?

Keep exploring at your chosen reading level.

🖼️ Images & Media (3)
File:Tryptophan-spin.gif
Tryptophan-spin.gif
File:Tryptophan metabolism.svg
Tryptophan metabolism.svg
File:Tryptophan biosynthesis (en).svg
Tryptophan biosynthesis (en).svg
More to explore

✨ What else?

Related topics you might enjoy

🔬 Go deeper

More advanced topics to explore

🪜 Step back

Simpler topics to build understanding

What is Nepedia?

A free, ad-free encyclopedia for children. Every article is written at five reading levels, so the same page works for a five-year-old and a fifteen-year-old — use the level switcher above to see this one change. No account needed to read.