16870-43-2

Basic information

• Product Name: L-Tyrosine hydrochloride
• Synonyms: 3-[4-HYDROXYPHENYL]-L-ALANINE HYDROCHLORIDE;L-3-[4-HYDROXYPHENYL]ALANINE HYDROCHLORIDE;L-TYROSINE HYDROCHLORIDE;H-TYR-OH HCL;(S)-2-AMINO-3-(4-HYDROXYPHENYL)PROPIONIC ACID HYDROCHLORIDE;L-Tyrosine hydrochloride solution;L-TYROSINE HYDROCHLORIDE CELL CULTURE*TE STED;L -TYROSINE HYDROCHLORIDE CRYSTALLINE CELL CULTURE REAGENT
• CAS NO: 16870-43-2
• Molecular Formula: C₉H₁₂NO₃*Cl
• Molecular Weight: 217.65
• EINECS: 231-791-2
• Mol File: 16870-43-2.mol

Chemical Properties

• Melting Point: 239 °C (dec.)(lit.)
• Boiling Point: 385.2oC at 760 mmHg
• Flash Point: 186.7oC
• Appearance: /
• Vapor Pressure: 1.27E-06mmHg at 25°C
• Storage Temp.: 2-8°C
• CAS DataBase Reference: L-Tyrosine hydrochloride(CAS DataBase Reference)
• NIST Chemistry Reference: L-Tyrosine hydrochloride(16870-43-2)
• EPA Substance Registry System: L-Tyrosine hydrochloride(16870-43-2)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36
• RIDADR: UN 1789 8/PG 3
• WGK Germany: 3
• F: 10
• Hazardous Substances Data: 16870-43-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
L-Tyrosine hydrochloride is used as an active pharmaceutical ingredient for the treatment of various conditions related to neurotransmitter deficiencies. It is particularly beneficial for individuals suffering from stress, fatigue, or cognitive decline, as it helps in the synthesis of neurotransmitters like dopamine, norepinephrine, and epinephrine.
Used in Nutritional Supplements:
L-Tyrosine hydrochloride is used as a dietary supplement to support cognitive function, stress response, and overall mental well-being. It is especially popular among athletes and individuals undergoing high-stress situations, as it can help improve focus, alertness, and mental clarity.
Used in Food and Beverage Industry:
L-Tyrosine hydrochloride is used as a flavor enhancer and additive in the food and beverage industry. Its role in the synthesis of neurotransmitters can contribute to the overall taste and sensory experience of certain products.
Used in Cosmetics Industry:
L-Tyrosine hydrochloride is used in the cosmetics industry for its skin-lightening properties. It can help reduce the appearance of age spots, hyperpigmentation, and other skin discolorations by inhibiting the production of melanin.
Used in Research and Development:
L-Tyrosine hydrochloride is used as a research compound in the development of new drugs and therapies targeting neurotransmitter-related disorders, as well as in the study of cell signaling and protein synthesis.

Biochem/physiol Actions

Tyrosine is a nonessential amino acid found in mammal, fish and birds. It participates in protein modification, such as phosphorylation, nitrosation and sulfation. It is involved in immune response regulation and prevents the generation of inflammatory cytokines and superoxide. Tyrosine serves as a precursor for epinephrine, norepinephrine, dopamine, thyroid hormones and melanin biosynthesis. Tyrosine phosphorylation is associated with a number of cellular processes such as cell proliferation and migration, development of the embryo, cellular metabolism and transcription. Tyrosine phosphorylation also aids activation of the enzymatic function of a protein.

InChI:InChI=1/C9H11NO3.ClH/c10-8(9(12)13)5-6-1-3-7(11)4-2-6;/h1-4,8,11H,5,10H2,(H,12,13);1H/t8-;/m0./s1

Upstream product

• 1383580-56-0 (2S,4S)-N-((6R,9R,12S,15S,16R,Z)-3-ethylidene-6-(4-hydroxybenzyl)-12-isobutyl-9-isopropyl-16-methyl-2,5,8,11,14-pentaoxo-1-oxa-4,7,10,13-tetraazacyclohexadecan-15-yl)-2,4-dimethylheptanamide 
• 3417-91-2 tyrosine methyl ester hydrochloride 
• 60-18-4 L-tyrosine 
• 61342-80-1 tert-butyl (S)-3-(4-(tert-butoxy)phenyl)-2-aminopropanoate 

Downstream Products

• 51-67-2 tyrosamine 
• 1423401-50-6 (-)-4-[4-{2-hydroxy-1-(4-hydroxybenzyl)ethylaminomethyl}benzyloxy]-3,5-bis(hydroxymethyl)phenylacetylene 
• 5034-68-4 4-[(2S)-2-amino-3-hydroxypropyl]phenol 
• 83345-46-4 N-(tert-butyloxycarbonyl)-L-tyrosinol 
• 4326-36-7 (S)-N-(tert-butoxycarbonyl)tyrosine methyl ester 
• 1080-06-4 L-Tyr-OMe 
• 1043893-10-2 2-(3-acetyl-7-(N,N-dimethylamino)-2-oxo-2H-chromen-4-ylamino)-3-(4-hydroxyphenyl)propionic acid 
• 30811-19-9 L-3,5-²H₂-tyrosine 
• 7234-03-9 <3,5-(3)H2>-L-tyrosine 
• 1063716-02-8 C₉H₁₀⁽²⁾HNO₄ 
• 13127-57-6 [5'-3H]-L-DOPA 
• 1010686-07-3 C₉H₉⁽²⁾H₂NO₃*Cl⁽²⁾H 
• 53559-18-5 (S)-2-amino-3-(4-hydroxyphenyl)propanamide hydrochloride 

Relevant articles and documents

Low-wavenumber Raman spectra of L-tyrosine, L-tyrosine hydrochloride, and L-tyrosine hydrobromide crystals at high temperatures

Crystals of L-tyrosine and semiorganic L-tyrosine hydrochloride and L-tyrosine hydrobromide, known for their nonlinear optical properties, were studied by Raman spectroscopy in the temperature range from 298 to 453 K. Hydrogen bonding at room temperature

LAT-1 activity of meta-substituted phenylalanine and tyrosine analogs

The transporter protein Large-neutral Amino Acid Transporter 1 (LAT-1, SLC7A5) is responsible for transporting amino acids such as tyrosine and phenylalanine as well as thyroid hormones, and it has been exploited as a drug delivery mechanism. Recently its role in cancer has become increasingly appreciated, as it has been found to be up-regulated in many different tumor types, and its expression levels have been correlated with prognosis. Substitution at the meta position of aromatic amino acids has been reported to increase affinity for LAT-1; however, the SAR for this position has not previously been explored. Guided by newly refined computational models of the binding site, we hypothesized that groups capable of filling a hydrophobic pocket would increase binding to LAT-1, resulting in improved substrates relative to parent amino acid. Tyrosine and phenylalanine analogs substituted at the meta position with halogens, alkyl and aryl groups were synthesized and tested in cis-inhibition and trans-stimulation cell assays to determine activity. Contrary to our initial hypothesis we found that lipophilicity was correlated with diminished substrate activity and increased inhibition of the transporter. The synthesis and SAR of meta-substituted phenylalanine and tyrosine analogs is described.

LAT1 activity of carboxylic acid bioisosteres: Evaluation of hydroxamic acids as substrates

Large neutral amino acid transporter 1 (LAT1) is a solute carrier protein located primarily in the blood–brain barrier (BBB) that offers the potential to deliver drugs to the brain. It is also up-regulated in cancer cells, as part of a tumor's increased metabolic demands. Previously, amino acid prodrugs have been shown to be transported by LAT1. Carboxylic acid bioisosteres may afford prodrugs with an altered physicochemical and pharmacokinetic profile than those derived from natural amino acids, allowing for higher brain or tumor levels of drug and/or lower toxicity. The effect of replacing phenylalanine's carboxylic acid with a tetrazole, acylsulfonamide and hydroxamic acid (HA) bioisostere was examined. Compounds were tested for their ability to be LAT1 substrates using both cis-inhibition and trans-stimulation cell assays. As HA-Phe demonstrated weak substrate activity, its structure–activity relationship (SAR) was further explored by synthesis and testing of HA derivatives of other LAT1 amino acid substrates (i.e., Tyr, Leu, Ile, and Met). The potential for a false positive in the trans-stimulation assay caused by parent amino acid was evaluated by conducting compound stability experiments for both HA-Leu and the corresponding methyl ester derivative. We concluded that HA's are transported by LAT1. In addition, our results lend support to a recent account that amino acid esters are LAT1 substrates, and that hydrogen bonding may be as important as charge for interaction with the transporter binding site.

Enantiospecific C-H Activation Using Ruthenium Nanocatalysts

The activation of C-H bonds has revolutionized modern synthetic chemistry. However, no general strategy for enantiospecific C-H activation has been developed to date. We herein report an enantiospecific C-H activation reaction followed by deuterium incorporation at stereogenic centers. Mechanistic studies suggest that the selectivity for the α-position of the directing heteroatom results from a four-membered dimetallacycle as the key intermediate. This work paves the way to novel molecular chemistry on nanoparticles.

Tumescenamide C, an antimicrobial cyclic lipodepsipeptide from Streptomyces sp.

Tumescenamide C, a new cyclic lipodepsipeptide, was isolated from a culture broth of an actinomycete Streptomyces sp. KUSC-F05. Tumescenamide C was a congener of tumescenamides A and B, representing a sixteen-membered ring system, consisting of two proteinogenic and three non-proteinogenic amino acids, to which a methyl-branched fatty acid was attached. The planar structure was determined by spectroscopic analysis, while its absolute stereochemistry was determined by chemical degradation and asymmetric synthesis. Tumescenamide C exhibited antimicrobial activity with high selectivity against Streptomyces species.

Empirical rules for the enantiopreference of lipase from Aspergillus niger toward secondary alcohols and carboxylic acids, especially α-amino acids

Lipase from Aspergillus niger (ANL, Amano lipase AP) catalyzes enantioselective hydrolysis and acylation reactions. To aid in the design of new applications of this lipase, we propose two empirical rules that predict which enantiomer reacts faster. For secondary alcohols, a rule proposed previously for other lipases also works for ANL, but with lower reliability (77%, 37 of 48 examples). For carboxylic acids, we examined both crude and partially-purified ANL because commercial ANL contains contaminating hydrolases. Partial purification removed a contaminating amidase and increased the enantioselectivity of ANL toward many α-amino acids, including cyclic amino acids. Unlike other lipases, ANL readily accepts positively-charged substrates and shows the highest enantioselectivity towards α-amino acids. Although a rule based on the sizes of the substituents could not predict the fast-reacting enantiomer, a rule limited to α-amino acids did predict the fast-reacting enantiomer. We estimate that the charged α-amino group contributes a factor of 40-100 (ΔΔ≠ = 2.2-2.7 kcal/mol) to the enantioselectivity of ANL towards carboxylic acids.