21820-51-9

Basic information

• Product Name: O-PHOSPHO-L-TYROSINE
• Synonyms: H-TYR(H2PO3)-OH;H-TYR(P)-OH;H-TYR(PO3H2)-OH;L-3-[4-HYDROXYPHENYL]ALANINE 4'-PHOSPHATE;L-TYROSINE O-PHOSPHATE;(S)-2-AMINO-3-(4-PHOSPHONOOXY-PHENYL)-PROPIONIC ACID;PHOSPHOTYROSINE;O-PHOSPHORYL-L-TYROSINE
• CAS NO: 21820-51-9
• Molecular Formula: C₉H₁₂NO₆P
• Molecular Weight: 261.17
• Product Categories: Amino Acids;Biochemistry;Biological-modified Amino Acids;Amino Acids & Derivatives;Aromatics;Chiral Reagents;Phosphorylating and Phosphitylating Agents
• Mol File: 21820-51-9.mol

Chemical Properties

• Melting Point: 226-227°C
• Boiling Point: 590.1oC at 760 mmHg
• Flash Point: 310.7oC
• Appearance: /
• Density: 1.63g/cm3
• Vapor Pressure: 9.05E-15mmHg at 25°C
• Refractive Index: 1.635
• Storage Temp.: 2-8°C
• Solubility: Aqueous Acid (Slightly), Water (Slightly, Sonicated)
• PKA: 1.24±0.30(Predicted)
• BRN: 3150815
• CAS DataBase Reference: O-PHOSPHO-L-TYROSINE(CAS DataBase Reference)
• NIST Chemistry Reference: O-PHOSPHO-L-TYROSINE(21820-51-9)
• EPA Substance Registry System: O-PHOSPHO-L-TYROSINE(21820-51-9)

Safety Data

• Hazard Codes: Xn
• Statements: 21/22
• Safety Statements: 36/37
• WGK Germany: 3
• F: 10-21
• Hazardous Substances Data: 21820-51-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
O-PHOSPHO-L-TYROSINE is used as a research compound for understanding the role of tyrosine-phosphorylation in the malignant transformation of cells by RNA tumor viruses. This knowledge aids in the development of targeted therapies and potential treatments for cancer.
Used in Signal Transduction Studies:
O-PHOSPHO-L-TYROSINE is used as a key molecule in the study of signal transduction pathways. Its role in these pathways helps researchers understand how cells communicate and respond to their environment, which is essential for developing new therapeutic strategies.
Used in Biochemical Education:
O-PHOSPHO-L-TYROSINE serves as an educational tool in biochemistry, providing students with a practical example of a phosphorylated amino acid and its importance in cellular processes and disease mechanisms.
Used in Drug Development:
O-PHOSPHO-L-TYROSINE is used as a starting material or intermediate in the synthesis of potential drugs targeting tyrosine-phosphorylation pathways, which could lead to the development of novel therapeutics for various diseases, including cancer.
Used in Analytical Chemistry:
O-PHOSPHO-L-TYROSINE is used as a reference compound in analytical chemistry for the development and validation of methods to detect and quantify phosphorylated amino acids in biological samples, which is crucial for understanding the role of these molecules in disease processes.

Purification Methods

Purify it by recrystallisation from H2O or H2O/EtOH. [Levene & Schormüller J Biol Chem 100 583 1933, Posternak & Graff Helv Chim Acta 28 1258 1945, Beilstein 14 III 1510.]

InChI:InChI=1/C9H12NO6P/c11-7-3-1-6(2-4-7)5-8(9(12)13)10-17(14,15)16/h1-4,8,11H,5H2,(H,12,13)(H3,10,14,15,16)

Upstream product

• 916661-26-2 O,O-diethyl 4-(bromomethyl)phenyl phosphate 
• 81477-94-3 N-(diphenylmethylene)glycine tert-butyl ester 
• 129785-81-5 phospho-Tyr-Gly-Gly-Phe-Leu-OH 
• 4089-07-0 L-tyrosine ethyl ester monohydrochloride 
• 60-18-4 L-tyrosine 
• 13200-86-7 N-formyl-L-tyrosine 

Downstream Products

• 112883-29-1 N-Fmoc-Tyr-OH 
• 1125484-03-8 Fmoc-FpY 
• 147762-53-6 N-(fluorenylmethyloxycarbonyl)tyrosine-O-phosphate 
• 1345001-27-5 thymine-Phe-Phe-Tyr-phosphate 
• 1415206-59-5 C₄₄H₅₁N₈O₁₃P 
• 959465-07-7 2-(naphthalen-2-yl)acetyl-D-Phe-D-PheTyr(phosphate) 

Relevant articles and documents

Asymmetric catalytic synthesis method of L-tyrosine derivative

The invention relates to an asymmetric catalytic synthesis method of an L-tyrosine derivative, which comprises the following steps of: reacting a compound as shown in a formula (II) with a compound as shown in a formula (III) in the presence of a catalyst as shown in a formula (A), and hydrolyzing to obtain a compound as shown in a formula (I). When the method is used for preparing derivatives such as phosphoric acid or phosphate of L-tyrosine, a large amount of strong acid such as phosphoric acid does not need to be used, the equipment requirement is lowered, the production safety is improved, a large amount of alkali does not need to be adopted for neutralization in post-treatment, generation of a large amount of waste residues such as inorganic salt is avoided, and high economic and environment protection effects are achieved.

Enzymatically Forming Intranuclear Peptide Assemblies for Selectively Killing Human Induced Pluripotent Stem Cells

Tumorigenic risk of undifferentiated human induced pluripotent stem cells (iPSCs), being a major obstacle for clinical application of iPSCs, requires novel approaches for selectively eliminating undifferentiated iPSCs. Here, we show that an l-phosphopenta

Enzyme Instructed Self-assembly of Naphthalimide-dipeptide: Spontaneous Transformation from Nanosphere to Nanotubular Structures that Induces Hydrogelation

Understanding the structure-morphology relationships of self-assembled nanostructures is crucial for developing materials with the desired chemical and biological functions. Here, phosphate-based naphthalimide (NI) derivatives have been developed for the

Modified synthesis method of oxidative phosphorylation-L-tyrosine

The invention discloses a modified synthesis method of oxidative phosphorylation-L-tyrosine, and belongs to the field of organic chemistry. L-tyrosine and phosphorus pentoxide are reacted in 85% strong phosphoric acid, a molar ratio of the L-tyrosine to t

An in situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids

Higher-order assemblies of proteins, with a structural and dynamic continuum, is an important concept in biology, but these insights have yet to be applied in designing biomaterials. Dynamic assemblies of supramolecular phosphoglycopeptides (sPGPs) transf

Enzyme-instructed self-assembly with photo-responses for the photo-regulation of cancer cells

Using a short peptide precursor modified by the biaryltetrazole with intramolecular photo-click reactivity, we realized the photo-regulation of the pericellular nanofibers formed by the enzyme-instructed self-assembly on the cell membrane. Upon light irra

Synthesis of six phenylalanine derivatives and their cell toxicity effect on human colon cancer cell line HT-29

Some phenylalanine (Phe) derivatives had important roles in pharmacology and may be used as pharmaceutical materials and pharmaceutical intermediates. In order to understand the cell toxicity of phenylalanine derivatives, we synthesized L-4-bromo-phenylalanine (Brp), L-4-iodophenylalanine (Ip), L-4-nitro-phenylalanine (Np), L-4-sulfonic-phenylalanine (Sp), L-4-phosphophenylalanine (Pp) and L-4-amino-phenylalanine (Np). We used mass spectrometry (MS), Infrared Spectroscopy (IR) or hydrogen-1 nuclear magnetic resonance spectrum (1H-NMR), and high performance liquid chromatography (HPLC) to test the correction of these products, MTT assay and Hoechst 33258 staining to detect their cell toxic effect on human colon cancer cell HT-29 (HT-29 cells). The results showed that these products were correct and the cytotoxicity of Pp>Ip>Sp and Np>Brp, Ap almost had no effect on HT-29 cells. In addition, Pp, Ip and Sp induced cell apoptosis, the other three kinds of phenylalanine derivatives induced neither apoptosis nor necrosis.

Thiophosphorylation of free amino acids and enzyme protein by thiophosphoramidate ions

In search of an activity-preserving protein thiophosphorylation method, with thymidylate synthase recombinant protein used as a substrate, potassium thiophosphoramidate and diammonium thiophosphoramidate salts in Tris- and ammonium carbonate based buffer solutions were employed, proving to serve as a non-destructive environment. Using potassium phosphoramidate or diammonium thiophosphoramidate, a series of phosphorylated and thiophosphorylated amino acid derivatives was prepared, helping, together with computational (using density functional theory, DFT) estimation of 31P NMR chemical shifts, to assign thiophosphorylated protein NMR resonances and prove the presence of thiophosphorylated lysine, serine and histidine moieties. Methods useful for prediction of 31P NMR chemical shifts of thiophosphorylated amino acid moieties, and thiophosphates in general, are also presented. The preliminary results obtained from trypsin digestion of enzyme shows peak at m/z 1825.805 which is in perfect agreement with the simulated isotopic pattern distributions for monothiophosphate of TVQQQVHLNQDEYK where thiophosphate moiety is attached to histidine (His26) or lysine (Lys33) side-chain.

Phosphorylation of enkephalins enhances their proteolytic stability

Pharmacological action of enkephalins as opioid peptides is limited because of their rapid degradation by endoproteases. A novel approach is used in this study to prolong the life of those peptides. Phosphorylation of N-terminal tyrosine residue is found to have a profound influence in improving the stability of [Met]enkephalin and [Leu]enkephalin against the action of aminopeptidase M. Whereas, breakdown of [Met]enkephalin and [Leu]enkephalin is essentially complete in less than one min when incubated at 37°C with purified aminopeptidase M (EC 3.4.11.2; substrate:enzyme = 1:0.1) in Tris buffer (pH 7.02), the corresponding phospho analogs are still detected 60 min after start of incubation. The rate of disappearance of phospho-[Met]enkephalin and phospho-[Leu]enkephalin follows first-order kinetics with half-lives of 7.3 and 8.8 min, respectively.