73246-30-7

Basic information

• Product Name: 3,5-Difluoro-L-tyrosine
• Synonyms: 3,5-Difluoro-L-tyrosine;H-Tyr(3,5-F2)-OH;(S)-2-amino-3-(3,5-difluoro-4-hydroxyphenyl)propanoic acid
• CAS NO: 73246-30-7
• Molecular Formula: C₉H₉F₂NO₃
• Molecular Weight: 217.1694664
• Mol File: 73246-30-7.mol
• Article Data: 10

Chemical Properties

• Boiling Point: 387.9 °C at 760 mmHg
• Flash Point: 188.4 °C
• Appearance: /
• Density: 1.475 g/cm³
• PKA: 2.17±0.30(Predicted)
• CAS DataBase Reference: 3,5-Difluoro-L-tyrosine(CAS DataBase Reference)
• NIST Chemistry Reference: 3,5-Difluoro-L-tyrosine(73246-30-7)
• EPA Substance Registry System: 3,5-Difluoro-L-tyrosine(73246-30-7)

Safety Data

• Hazardous Substances Data: 73246-30-7(Hazardous Substances Data)

Usage

General Description

3,5-Difluoro-L-tyrosine is a chemical compound that is derived from the amino acid tyrosine. It is characterized by the presence of two fluorine atoms at the 3 and 5 positions on the phenyl ring of the tyrosine molecule. 3,5-Difluoro-L-tyrosine is of interest in pharmaceutical research and development, as it has potential applications in the synthesis of novel drug candidates and in the development of fluorine-containing pharmaceuticals. 3,5-Difluoro-L-tyrosine may also have therapeutic potential in the treatment of certain diseases, due to its ability to modulate biological pathways and interact with specific molecular targets. Its unique chemical structure and properties make it a valuable tool for investigating the role of fluorine-containing compounds in drug discovery and medicinal chemistry.

Upstream product

• 73210-56-7 N-(trifluoroacetyl)-3,5-difluoro-L-tyrosine methyl ester 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 73210-50-1 3-(3-Amino-4-hydroxy-phenyl)-2-(2,2,2-trifluoro-acetylamino)-propionic acid methyl ester 
• 73210-53-4 N-(trifluoroacetyl)-3-fluoro-L-tyrosine methyl ester 
• 73210-55-6 3-(3-Amino-5-fluoro-4-hydroxy-phenyl)-2-(2,2,2-trifluoro-acetylamino)-propionic acid methyl ester 
• 5106-00-3 N-(trifluoroacetyl)-3-nitro-L-tyrosine methyl ester 
• 73210-54-5 3-(3-Fluoro-4-hydroxy-5-nitro-phenyl)-2-(2,2,2-trifluoro-acetylamino)-propionic acid methyl ester 
• 1604-54-2 N-(trifluoroacetyl)-L-tyrosine methyl ester 
• 28177-48-2 2,6-difluorophenol 
• 127-17-3 2-oxo-propionic acid 
• 113-24-6 sodium pyruvate 
• 631-61-8 ammonium acetate 
• 60-24-2 2-hydroxyethanethiol 

Downstream Products

• 273221-86-6 N-(9-fluorenylmethoxycarbonyl)-L-3,5-difluorotyrosine 
• 197972-08-0 (S)-4-{(S)-2-[(S)-2-((S)-2-Amino-4-carboxy-butyrylamino)-3-carboxy-propionylamino]-3-carbamoyl-propionylamino}-4-[(S)-1-[(1S,2R)-1-((S)-1-carboxy-ethylcarbamoyl)-2-hydroxy-propylcarbamoyl]-2-(3,5-difluoro-4-hydroxy-phenyl)-ethylcarbamoyl]-butyric acid 
• 1437783-64-6 o-phospho-3,5-difluorotyrosine 
• 1213198-51-6 (S)-2-((tert-butoxycarbonyl)amino)-3-(3,5-difluoro-4-hydroxyphenyl)propanoic acid 

Relevant articles and documents

Formal reduction potential of 3,5-difluorotyrosine in a structured protein: Insight into multistep radical transfer

The reversible Y-O?/Y-OH redox properties of the α3Y model protein allow access to the electrochemical and thermodynamic properties of 3,5-difluorotyrosine. The unnatural amino acid has been incorporated at position 32, the dedicated

Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping

Transient tyrosine and tryptophan radicals play key roles in the electron transfer (ET) reactions of photosystem (PS) II, ribonucleotide reductase (RNR), photolyase, and many other proteins. However, Tyr and Trp are not functionally interchangeable, and t

Defining the Role of Tyrosine and Rational Tuning of Oxidase Activity by Genetic Incorporation of Unnatural Tyrosine Analogs

While a conserved tyrosine (Tyr) is found in oxidases, the roles of phenol ring pKa and reduction potential in O2 reduction have not been defined despite many years of research on numerous oxidases and their models. These issues represent major challenges in our understanding of O2 reduction mechanism in bioenergetics. Through genetic incorporation of unnatural amino acid analogs of Tyr, with progressively decreasing pKa of the phenol ring and increasing reduction potential, in the active site of a functional model of oxidase in myoglobin, a linear dependence of both the O2 reduction activity and the fraction of H2O formation with the pKa of the phenol ring has been established. By using these unnatural amino acids as spectroscopic probe, we have provided conclusive evidence for the location of a Tyr radical generated during reaction with H2O2, by the distinctive hyperfine splitting patterns of the halogenated tyrosines and one of its deuterated derivatives incorporated at the 33 position of the protein. These results demonstrate for the first time that enhancing the proton donation ability of the Tyr enhances the oxidase activity, allowing the Tyr analogs to augment enzymatic activity beyond that of natural Tyr.