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Tyrosine
L-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.
The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available. Note that T was assigned to the structurally simpler threonine, U was avoided for its similarity with V for valine, W was assigned to tryptophan, while X was reserved for undetermined or atypical amino acids. The mnemonic tYrosine was also proposed.
Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. Its hydroxy group is able to form the ester linkage, with phosphate in particular. Phosphate groups are transferred to tyrosine residues by way of protein kinases. This is one of the post-translational modifications. Phosphorylated tyrosine occurs in proteins that are part of signal transduction processes.
Similar functionality is also presented in serine and threonine, whose side chains have a hydroxy group, but are alcohols. Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, which is greater than the negative charge of the only negatively charged aspartic and glutamic acids. Phosphorylated proteins keep these same properties—which are useful for more reliable protein-protein interactions—by means of phosphotyrosine, phosphoserine and phosphothreonine.
Binding sites for a signalling phosphoprotein may be diverse in their chemical structure.
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.
The Dietary Reference Intake for tyrosine is usually estimated together with phenylalanine. It varies depending on an estimate method, however the ideal proportion of these two amino acids is considered to be 60:40 (phenylalanine:tyrosine) as a human body has such composition. Tyrosine, which can also be synthesized in the body from phenylalanine, is found in many high-protein food products such as meat, fish, cheese, cottage cheese, milk, yogurt, peanuts, almonds, pumpkin seeds, sesame seeds, soy protein and lima beans. For example, the white of an egg has about 250 mg per egg, while beef, lamb, pork, tuna, salmon, chicken, and turkey contain about 500–1000 mg per 3 ounces (85 g) portion.
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Tyrosine
L-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.
The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available. Note that T was assigned to the structurally simpler threonine, U was avoided for its similarity with V for valine, W was assigned to tryptophan, while X was reserved for undetermined or atypical amino acids. The mnemonic tYrosine was also proposed.
Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. Its hydroxy group is able to form the ester linkage, with phosphate in particular. Phosphate groups are transferred to tyrosine residues by way of protein kinases. This is one of the post-translational modifications. Phosphorylated tyrosine occurs in proteins that are part of signal transduction processes.
Similar functionality is also presented in serine and threonine, whose side chains have a hydroxy group, but are alcohols. Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, which is greater than the negative charge of the only negatively charged aspartic and glutamic acids. Phosphorylated proteins keep these same properties—which are useful for more reliable protein-protein interactions—by means of phosphotyrosine, phosphoserine and phosphothreonine.
Binding sites for a signalling phosphoprotein may be diverse in their chemical structure.
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.
The Dietary Reference Intake for tyrosine is usually estimated together with phenylalanine. It varies depending on an estimate method, however the ideal proportion of these two amino acids is considered to be 60:40 (phenylalanine:tyrosine) as a human body has such composition. Tyrosine, which can also be synthesized in the body from phenylalanine, is found in many high-protein food products such as meat, fish, cheese, cottage cheese, milk, yogurt, peanuts, almonds, pumpkin seeds, sesame seeds, soy protein and lima beans. For example, the white of an egg has about 250 mg per egg, while beef, lamb, pork, tuna, salmon, chicken, and turkey contain about 500–1000 mg per 3 ounces (85 g) portion.