Tyrosine

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Tyrosine
L-Tyrosin - L-Tyrosine.svg
Skeletal formula of L-tyrosine
L-Tyrosin phys.svg
L-Tyrosine at physiological pH
Tyrosine-from-xtal-3D-bs-17.png
Tyrosine-from-xtal-3D-sf.png
Names
IUPAC name
(S)-Tyrosine
Other names
L-2-Amino-3-(4-hydroxyphenyl)propanoic acid
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.000.419 OOjs UI icon edit-ltr-progressive.svg
KEGG
PubChem CID
UNII
  • InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1 Yes check.svgY
    Key: OUYCCCASQSFEME-QMMMGPOBSA-N Yes check.svgY
  • Key: OUYCCCASQSFEME-UHFFFAOYSA-N
  • Key: OUYCCCASQSFEME-MRVPVSSYSA-N
  • N[C@@H](Cc1ccc(O)cc1)C(O)=O
  • Zwitterion:[NH3+][C@@H](Cc1ccc(O)cc1)C([O-])=O
Properties
C9H11NO3
Molar mass 181.191 g·mol−1
Appearancewhite solid
.0453 g/100 mL
-105.3·10−6 cm3/mol
Hazards
NFPA 704 (fire diamond)
NFPA 704.svgHealth 1: Exposure would cause irritation but only minor residual injury. E.g. turpentineFlammability 1: Must be pre-heated before ignition can occur. Flash point over 93 °C (200 °F). E.g. canola oilInstability 0: Normally stable, even under fire exposure conditions, and is not reactive with water. E.g. liquid nitrogenSpecial hazards (white): no code
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1
0
Supplementary data page
Tyrosine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

L-Tyrosine or tyrosine (symbol Tyr or Y) [2] 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. [3] [4] 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. [5] 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. [6] The mnemonic tYrosine was also proposed. [7]

Functions

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, that 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. [8]

Binding sites for a signalling phosphoprotein may be diverse in their chemical structure. [9]

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. [10]

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. [11]

Dietary requirements and sources

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. [12] 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. [13] [14] For example, the white of an egg has about 250 mg per egg, [15] while beef, lamb, pork, tuna, salmon, chicken, and turkey contain about 500–1000 mg per 3 ounces (85 g) portion. [15] [16]

Biosynthesis

Plant biosynthesis of tyrosine from prephenate. Tyrosine biosynthesis.svg
Plant biosynthesis of tyrosine from prephenate.

In plants and most microorganisms, tyrosine is produced via prephenate, an intermediate on the shikimate pathway. Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and α-ketoglutarate.

Mammals synthesize tyrosine from the essential amino acid phenylalanine (Phe), which is derived from food. The conversion of Phe to Tyr is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase. This enzyme catalyzes the reaction causing the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine.

Metabolism

Conversion of phenylalanine and tyrosine to its biologically important derivatives. Conversion of phenylalanine and tyrosine to its biologically important derivatives.png
Conversion of phenylalanine and tyrosine to its biologically important derivatives.

Phosphorylation and sulfation

Some of the tyrosine residues can be tagged (at the hydroxyl group) with a phosphate group (phosphorylated) by protein kinases. In its phosphorylated form, tyrosine is called phosphotyrosine. Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. Phosphotyrosine can be detected through specific antibodies. Tyrosine residues may also be modified by the addition of a sulfate group, a process known as tyrosine sulfation. [17] Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST). Like the phosphotyrosine antibodies mentioned above, antibodies have recently been described that specifically detect sulfotyrosine. [18]

Precursor to neurotransmitters and hormones

In dopaminergic cells in the brain, tyrosine is converted to L-DOPA by the enzyme tyrosine hydroxylase (TH). TH is the rate-limiting enzyme involved in the synthesis of the neurotransmitter dopamine. Dopamine can then be converted into other catecholamines, such as norepinephrine (noradrenaline) and epinephrine (adrenaline).

The thyroid hormones triiodothyronine (T3) and thyroxine (T4) in the colloid of the thyroid are also derived from tyrosine.

Biosynthetic pathways for catecholamines and trace amines in the human brain [19] [20] [21]
Interactive icon.svg
Tyrosine is a precursor to trace amine compounds and the catecholamines.

Precursor to other compounds

The latex of Papaver somniferum , the opium poppy, has been shown to convert tyrosine into the alkaloid morphine and the bio-synthetic pathway has been established from tyrosine to morphine by using Carbon-14 radio-labelled tyrosine to trace the in-vivo synthetic route. [22] Tyrosine ammonia lyase (TAL) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid. Tyrosine is also the precursor to the pigment melanin . Tyrosine (or its precursor phenylalanine) is needed to synthesize the benzoquinone structure which forms part of coenzyme Q10. [23] [24]

Degradation

The decomposition of tyrosine to acetoacetate and fumarate. Two dioxygenases are necessary for the decomposition path. The end products can then enter into the citric acid cycle. Tyrosinedegradation2.png
The decomposition of tyrosine to acetoacetate and fumarate. Two dioxygenases are necessary for the decomposition path. The end products can then enter into the citric acid cycle.

[ citation needed ]

The decomposition of L-tyrosine (syn. para-hydroxyphenylalanine) begins with an α-ketoglutarate dependent transamination through the tyrosine transaminase to para-hydroxyphenylpyruvate. The positional description para, abbreviated p, mean that the hydroxyl group and side chain on the phenyl ring are across from each other (see the illustration below).

The next oxidation step catalyzes by p-hydroxyphenylpyruvate dioxygenase and splitting off CO2 homogentisate (2,5-dihydroxyphenyl-1-acetate). [25] In order to split the aromatic ring of homogentisate, a further dioxygenase, homogentisate 1,2-dioxygenase is required. Thereby, through the incorporation of a further O2 molecule, maleylacetoacetate is created.

Fumarylacetoacetate is created by maleylacetoacetate cis-trans-isomerase through rotation of the carboxyl group created from the hydroxyl group via oxidation. This cis-trans-isomerase contains glutathione as a coenzyme. Fumarylacetoacetate is finally split by the enzyme fumarylacetoacetate hydrolase through the addition of a water molecule.

Thereby fumarate (also a metabolite of the citric acid cycle) and acetoacetate (3-ketobutyroate) are liberated. Acetoacetate is a ketone body, which is activated with succinyl-CoA, and thereafter it can be converted into acetyl-CoA, which in turn can be oxidized by the citric acid cycle or be used for fatty acid synthesis.

Phloretic acid is also a urinary metabolite of tyrosine in rats. [26]

Ortho- and meta-tyrosine

Enzymatic oxidation of tyrosine by phenylalanine hydroxylase (top) and non-enyzmatic oxidation by hydroxyl free radicals (middle and bottom). Phe Tyr.png
Enzymatic oxidation of tyrosine by phenylalanine hydroxylase (top) and non-enyzmatic oxidation by hydroxyl free radicals (middle and bottom).

Three structural isomers of L-tyrosine are known. In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature. The m-tyr and o-tyr isomers, which are rare, arise through non-enzymatic free-radical hydroxylation of phenylalanine under conditions of oxidative stress. [27] [28]

Medical use

Tyrosine is a precursor to neurotransmitters and increases plasma neurotransmitter levels (particularly dopamine and norepinephrine), [29] but has little if any effect on mood in normal subjects. [30] [31] [32]

A 2015 systematic review found that "tyrosine loading acutely counteracts decrements in working memory and information processing that are induced by demanding situational conditions such as extreme weather or cognitive load" and therefore "tyrosine may benefit healthy individuals exposed to demanding situational conditions". [33]

Industrial synthesis

L-tyrosine is used in pharmaceuticals, dietary supplements, and food additives. Two methods were formerly used to manufacture L-tyrosine. The first involves the extraction of the desired amino acid from protein hydrolysates using a chemical approach. The second utilizes enzymatic synthesis from phenolics, pyruvate, and ammonia through the use of tyrosine phenol-lyase. [34] Advances in genetic engineering and the advent of industrial fermentation have shifted the synthesis of L-tyrosine to the use of engineered strains of E. coli. [35] [34]

See also

Related Research Articles

A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg2+- or Mn2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. The protein pseudophosphatases form part of the larger phosphatase family, and in most cases are thought to be catalytically inert, instead functioning as phosphate-binding proteins, integrators of signalling or subcellular traps. Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. A complete comparative analysis of human phosphatases and pseudophosphatases has been completed by Manning and colleagues, forming a companion piece to the ground-breaking analysis of the human kinome, which encodes the complete set of ~536 human protein kinases.

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

<span class="mw-page-title-main">3-Dehydroquinic acid</span> Chemical compound

3-Dehydroquinic acid (DHQ) is the first carbocyclic intermediate of the shikimate pathway. It is created from 3-deoxyarabinoheptulosonate 7-phosphate, a 7-carbon ulonic acid, by the enzyme DHQ synthase. The mechanism of ring closure is complex, but involves an aldol condensation at C-2 and C-7.

<span class="mw-page-title-main">Amino acid synthesis</span> The set of biochemical processes by which amino acids are produced

Amino acid biosynthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids.

<span class="mw-page-title-main">Tryptophan hydroxylase</span> Class of enzymes

Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin. Tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases. TPH catalyzes the following chemical reaction

<span class="mw-page-title-main">Aromatic amino acid</span> Amino acid having an aromatic ring

An aromatic amino acid is an amino acid that includes an aromatic ring.

<span class="mw-page-title-main">Phenylalanine racemase (ATP-hydrolysing)</span>

The enzyme phenylalanine racemase is the enzyme that acts on amino acids and derivatives. It activates both the L & D stereo isomers of phenylalanine to form L-phenylalanyl adenylate and D-phenylalanyl adenylate, which are bound to the enzyme. These bound compounds are then transferred to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration of the two, with a 7 to 3 ratio between the two isomers. The racemisation reaction of phenylalanine is coupled with the highly favorable hydrolysis of adenosine triphosphate (ATP) to adenosine monophosphate (AMP) and pyrophosphate (PP), thermodynamically allowing it to proceed. This reaction is then drawn forward by further hydrolyzing PP to inorganic phosphate (Pi), via Le Chatelier's principle.

<span class="mw-page-title-main">Tyrosine aminotransferase</span> Mammalian protein found in Homo sapiens

Tyrosine aminotransferase is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate.

<span class="mw-page-title-main">Fumarylacetoacetate hydrolase</span>

Fumarylacetoacetase is an enzyme that in humans is encoded by the FAH gene located on chromosome 15. The enzyme is involved in the catabolism of the amino acid tyrosine in humans.

<span class="mw-page-title-main">Tyrosylprotein sulfotransferase</span> Enzyme

Tyrosylprotein sulfotransferase is an enzyme that catalyzes tyrosine sulfation.

<span class="mw-page-title-main">Prephenate dehydrogenase</span> Class of enzymes

Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine.

<span class="mw-page-title-main">UDP-glucose 4-epimerase</span> Class of enzymes

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

<span class="mw-page-title-main">Phenylalanine ammonia-lyase</span>

The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:

In enzymology, glutamate-prephenate aminotransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Shikimate kinase</span> Class of enzymes

Shikimate kinase (EC 2.7.1.71) is an enzyme that catalyzes the ATP-dependent phosphorylation of shikimate to form shikimate 3-phosphate. This reaction is the fifth step of the shikimate pathway, which is used by plants and bacteria to synthesize the common precursor of aromatic amino acids and secondary metabolites. The systematic name of this enzyme class is ATP:shikimate 3-phosphotransferase. Other names in common use include shikimate kinase (phosphorylating), and shikimate kinase II.

A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation). These enzymes regulate many cellular functions by switching on or switching off other enzymes in a cell.

<span class="mw-page-title-main">Biopterin-dependent aromatic amino acid hydroxylase</span>

Biopterin-dependent aromatic amino acid hydroxylases (AAAH) are a family of aromatic amino acid hydroxylase enzymes which includes phenylalanine 4-hydroxylase, tyrosine 3-hydroxylase, and tryptophan 5-hydroxylase. These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively.

<span class="mw-page-title-main">Shikimate pathway</span> Biosynthetic Pathway

The shikimate pathway is a seven-step metabolic pathway used by bacteria, archaea, fungi, algae, some protozoans, and plants for the biosynthesis of folates and aromatic amino acids. This pathway is not found in mammals.

<span class="mw-page-title-main">EPSP synthase</span> Enzyme produced by plants and microorganisms

5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. EPSPS catalyzes the chemical reaction:

<span class="mw-page-title-main">Tyrosine phosphorylation</span> Phosphorylation of peptidyl-tyrosine

Tyrosine phosphorylation is the addition of a phosphate (PO43−) group to the amino acid tyrosine on a protein. It is one of the main types of protein phosphorylation. This transfer is made possible through enzymes called tyrosine kinases. Tyrosine phosphorylation is a key step in signal transduction and the regulation of enzymatic activity.

References

  1. 1 2 Frey MN, Koetzle TF, Lehmann MS, Hamilton WC (1973). "Precision neutron diffraction structure determination of protein and nucleic acid components. X. A comparison between the crystal and molecular structures of L-tyrosine and L-tyrosine hydrochloride". J. Chem. Phys. 58 (6): 2547–2556. Bibcode:1973JChPh..58.2547F. doi:10.1063/1.1679537.
  2. ↑ "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.
  3. ↑ "Tyrosine". The Columbia Electronic Encyclopedia, 6th ed. Infoplease.com — Columbia University Press. 2007. Retrieved 2008-04-20.
  4. ↑ Harper D (2001). "Tyrosine". Online Etymology Dictionary. Retrieved 2008-04-20.
  5. ↑ "Amino Acids - Tyrosine". www.biology.arizona.edu. Retrieved 2018-01-31.
  6. ↑ "IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences". Journal of Biological Chemistry. 243 (13): 3557–3559. 10 July 1968. doi: 10.1016/S0021-9258(19)34176-6 .
  7. ↑ Saffran M (April 1998). "Amino acid names and parlor games: from trivial names to a one-letter code, amino acid names have strained students' memories. Is a more rational nomenclature possible?". Biochemical Education. 26 (2): 116–118. doi:10.1016/S0307-4412(97)00167-2.
  8. ↑ Hunter T (2012-09-19). "Why nature chose phosphate to modify proteins". Philosophical Transactions of the Royal Society B: Biological Sciences. 367 (1602): 2513–2516. doi:10.1098/rstb.2012.0013. ISSN   0962-8436. PMC   3415839 . PMID   22889903.
  9. ↑ Lu ZC, Jiang F, Wu YD (2021-12-11). "Phosphate binding sites prediction in phosphorylation-dependent protein-protein interactions". Bioinformatics. 37 (24): 4712–4718. doi:10.1093/bioinformatics/btab525. ISSN   1367-4811. PMID   34270697.
  10. ↑ Liu BA, Nash PD (2012-09-19). "Evolution of SH2 domains and phosphotyrosine signalling networks". Philosophical Transactions of the Royal Society B: Biological Sciences. 367 (1602): 2556–2573. doi:10.1098/rstb.2012.0107. ISSN   0962-8436. PMC   3415846 . PMID   22889907.
  11. ↑ Barry BA (January 2015). "Reaction dynamics and proton coupled electron transfer: studies of tyrosine-based charge transfer in natural and biomimetic systems". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1847 (1): 46–54. doi:10.1016/j.bbabio.2014.09.003. ISSN   0006-3002. PMID   25260243.
  12. ↑ Pencharz PB, Hsu JW, Ball RO (June 2007). "Aromatic amino acid requirements in healthy human subjects". The Journal of Nutrition. 137 (6 Suppl 1): 1576S–1578S, discussion 1597S-1598S. doi: 10.1093/jn/137.6.1576S . PMID   17513429.
  13. ↑ Nutient Ranking Tool. MyFoodData.com. https://tools.myfooddata.com/nutrient-ranking-tool/tyrosine/all/highest
  14. ↑ "Tyrosine". University of Maryland Medical Center. Archived from the original on 2013-06-04. Retrieved 2011-03-17.
  15. 1 2 Top 10 Foods Highest in Tyrosine
  16. ↑ Nutient Ranking Tool. MyFoodData.com. https://tools.myfooddata.com https://tools.myfooddata.com/nutrient-ranking-tool/tyrosine/meats/highest/ounces/common/no
  17. ↑ Hoffhines AJ, Damoc E, Bridges KG, Leary JA, Moore KL (December 2006). "Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody". The Journal of Biological Chemistry. 281 (49): 37877–87. doi: 10.1074/jbc.M609398200 . PMC   1764208 . PMID   17046811.
  18. ↑ Kanan Y, Hamilton RA, Sherry DM, Al-Ubaidi MR (December 2012). "Focus on molecules: sulfotyrosine". Experimental Eye Research. 105: 85–6. doi:10.1016/j.exer.2012.02.014. PMC   3629733 . PMID   22406006.
  19. ↑ Broadley KJ (March 2010). "The vascular effects of trace amines and amphetamines". Pharmacology & Therapeutics. 125 (3): 363–375. doi:10.1016/j.pharmthera.2009.11.005. PMID   19948186.
  20. ↑ Lindemann L, Hoener MC (May 2005). "A renaissance in trace amines inspired by a novel GPCR family". Trends in Pharmacological Sciences. 26 (5): 274–281. doi:10.1016/j.tips.2005.03.007. PMID   15860375.
  21. ↑ Wang X, Li J, Dong G, Yue J (February 2014). "The endogenous substrates of brain CYP2D". European Journal of Pharmacology. 724: 211–218. doi:10.1016/j.ejphar.2013.12.025. PMID   24374199.
  22. ↑ Battersby AR, Binks R, Harper BJ (1962-01-01). "692. Alkaloid biosynthesis. Part II. The biosynthesis of morphine". Journal of the Chemical Society: 3534–3544. doi:10.1039/JR9620003534. ISSN   0368-1769.
  23. ↑ Bentinger M, Tekle M, Dallner G (May 2010). "Coenzyme Q--biosynthesis and functions". Biochemical and Biophysical Research Communications. 396 (1): 74–9. doi:10.1016/j.bbrc.2010.02.147. PMID   20494114.
  24. ↑ Acosta MJ, Vazquez Fonseca L, Desbats MA, Cerqua C, Zordan R, Trevisson E, et al. (2016). "Coenzyme Q biosynthesis in health and disease". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857 (8): 1079–1085. doi: 10.1016/j.bbabio.2016.03.036 . PMID   27060254.
  25. ↑ Zea-Rey AV, Cruz-Camino H, Vazquez-Cantu DL, Gutiérrez-García VM, Santos-Guzmán J, Cantú-Reyna C (27 November 2017). "The Incidence of Transient Neonatal Tyrosinemia Within a Mexican Population". Journal of Inborn Errors of Metabolism and Screening. 5: 232640981774423. doi: 10.1177/2326409817744230 .
  26. ↑ Booth AN, Masri MS, Robbins DJ, Emerson OH, Jones FT, DeEds F (1960). "Urinary phenolic acid metabolities of tyrosine". Journal of Biological Chemistry. 235 (9): 2649–2652. doi: 10.1016/S0021-9258(19)76930-0 .
  27. ↑ Molnár GA, Wagner Z, Markó L, Kó Szegi T, Mohás M, Kocsis B, et al. (November 2005). "Urinary ortho-tyrosine excretion in diabetes mellitus and renal failure: evidence for hydroxyl radical production". Kidney International. 68 (5): 2281–7. doi: 10.1111/j.1523-1755.2005.00687.x . PMID   16221230.
  28. ↑ Molnár GA, Nemes V, Biró Z, Ludány A, Wagner Z, Wittmann I (December 2005). "Accumulation of the hydroxyl free radical markers meta-, ortho-tyrosine and DOPA in cataractous lenses is accompanied by a lower protein and phenylalanine content of the water-soluble phase". Free Radical Research. 39 (12): 1359–66. doi:10.1080/10715760500307107. PMID   16298866. S2CID   31154432.
  29. ↑ Rasmussen DD, Ishizuka B, Quigley ME, Yen SS (October 1983). "Effects of tyrosine and tryptophan ingestion on plasma catecholamine and 3,4-dihydroxyphenylacetic acid concentrations". The Journal of Clinical Endocrinology and Metabolism. 57 (4): 760–3. doi:10.1210/jcem-57-4-760. PMID   6885965.
  30. ↑ Leathwood PD, Pollet P (1982). "Diet-induced mood changes in normal populations". Journal of Psychiatric Research. 17 (2): 147–54. doi:10.1016/0022-3956(82)90016-4. PMID   6764931.
  31. ↑ Deijen JB, Orlebeke JF (1994). "Effect of tyrosine on cognitive function and blood pressure under stress". Brain Research Bulletin. 33 (3): 319–23. doi:10.1016/0361-9230(94)90200-3. PMID   8293316. S2CID   33823121.
  32. ↑ Lieberman HR, Corkin S, Spring BJ, Wurtman RJ, Growdon JH (August 1985). "The effects of dietary neurotransmitter precursors on human behavior". The American Journal of Clinical Nutrition. 42 (2): 366–70. doi:10.1093/ajcn/42.2.366. PMID   4025206.
  33. ↑ Jung SE, Hase A, ann het Rot M (2015). "Behavioral and cognitive effects of tyrosine intake in healthy human adults". Pharmacology Biochemistry and Behavior . 133: 1–6. doi:10.1016/j.pbb.2015.03.008. PMID   25797188. S2CID   30331663.
  34. 1 2 Lütke-Eversloh T, Santos CN, Stephanopoulos G (December 2007). "Perspectives of biotechnological production of L-tyrosine and its applications". Applied Microbiology and Biotechnology. 77 (4): 751–62. doi:10.1007/s00253-007-1243-y. PMID   17968539. S2CID   23088822.
  35. ↑ Chavez-Bejar M, Baez-Viveros J, Martinez A, Bolivar F, Gosset G (2012). "Biotechnological production of L-tyrosine and derived compounds". Process Biochemistry. 47 (7): 1017–1026. doi:10.1016/j.procbio.2012.04.005.
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