403-90-7 Usage
Description
3-FLUORO-DL-TYROSINE is a halogenated derivative of the amino acid tyrosine, characterized by the presence of a fluorine atom at the third position. It is a white solid and is utilized in various applications, particularly in the study of protein properties and the biosynthesis of specific proteins.
Uses
Used in Research and Development:
3-FLUORO-DL-TYROSINE is used as a research compound for studying the effects of halogenated tyrosines on the properties of proteins. It is particularly useful in understanding how the presence of a fluorine atom influences the structure, function, and stability of proteins.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 3-FLUORO-DL-TYROSINE is used as a building block in the biosynthesis of proteins such as β-galactosidases (Escherichia coli), bacteriorhodopsin, and intestinal microvillar enzymes, including aminopeptidase N. These proteins have significant roles in various biological processes and are potential targets for therapeutic intervention.
Used in Biochemical Studies:
3-FLUORO-DL-TYROSINE is employed as a biochemical tool to investigate the role of tyrosine in protein structure and function. By substituting tyrosine with its halogenated counterpart, researchers can gain insights into the importance of specific amino acid residues in protein folding, stability, and interactions with other molecules.
Used in Drug Design and Development:
The unique properties of 3-FLUORO-DL-TYROSINE make it a valuable compound in the field of drug design and development. Its incorporation into protein structures can potentially lead to the development of novel therapeutic agents with improved pharmacological properties, such as enhanced selectivity, potency, and reduced side effects.
Biochem/physiol Actions
M-Fluorotyrosine (m-Fluoro-DL-tyrosine) may be substituted for tyrosine in the biosynthesis of proteins such as β-galactosidases (Escherichia coli), bacteriorhodopsin and intestinal microvillar enzymes, eg. aminopeptidase N, to study the effect of halogenated tryosines on the proteins properties.
Check Digit Verification of cas no
The CAS Registry Mumber 403-90-7 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,0 and 3 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 403-90:
(5*4)+(4*0)+(3*3)+(2*9)+(1*0)=47
47 % 10 = 7
So 403-90-7 is a valid CAS Registry Number.
InChI:InChI=1/C9H10FNO3/c10-6-3-5(1-2-8(6)12)4-7(11)9(13)14/h1-3,7,12H,4,11H2,(H,13,14)/t7-/m1/s1
403-90-7Relevant articles and documents
Syntheses of [18F]5-fluoro-3-nitro-L-tyrosine
Vasdev, Neil,Chirakal, Raman,Ashique, Rezwan,Schrobilgen, Gary J.,Gulenchyn, Karen
, p. 9 - 14 (2003)
The detection of 3-nitro-L-tyrosine has been used as a biomarker of "reactive nitrogen species" in biological matrices and has been an ongoing challenge in analytical chemistry. In this work, fluorine-18 labelled 5-fluoro-3-nitro-L-tyrosine (FNT) was synthesized as a potential radiotracer to probe the biological fate of 3-nitro-L-tyrosine. The synthesis of [18F]FNT was carried out by reaction of [18F]3-fluoro-L-tyrosine with NaNO3 in TFA solvent for 5min at 4 °C. The radiochemical yield (RCY) of [18F]FNT was 96±2% and [18F]3-fluoro-l-tyrosine, was 29±1%, relative to [18F]3-fluoro-l-tyrosine and [18F]F2, respectively. The syntheses of [18F]FNT were also accomplished by direct fluorination of 3-nitro-L-tyrosine with [18F]F 2 and by nitration of L-tyrosine with NaNO3, followed by fluorination, in TFA (4 °C) or anhydrous HF (-65 °C) solvent. The latter two synthetic routes produced [18F]FNT in 13.5±1.5% RCY, within 1h. Products were characterized by use of 1H, 13C and 19F NMR spectroscopy and mass spectrometry.
Biocascade Synthesis of L-Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol-Lyase and L-Lactate Oxidase
Jiang, Yiqi,Ju, Shuyun,Li, Guosi,Lian, Jiazhang,Lin, Jianping,Wu, Mianbin,Xue, Hailong,Yang, Lirong
supporting information, (2020/02/25)
A one-pot biocascade of two enzymatic steps catalyzed by an l-lactate oxidase and a tyrosine phenol-lyase has been successfully developed in the present study. The reaction provides an efficient method for the synthesis of l-tyrosine derivatives, which exhibits readily available starting materials and excellent yields. In the first step, an in situ generation of pyruvate from readily available bio-based l-lactate catalyzed by a highly active l-lactate oxidase from Aerococcus viridans (AvLOX) was developed (using oxygen as oxidant and catalase as hydrogen peroxide removing reagent). Pyruvate thus produced underwent C–C coupling with phenol derivatives as acceptor substrate using specially designed thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii (TTPL). Overall, this cascade avoids the high cost and easy decomposition of pyruvate and offered an efficient and environmentally friendly procedure for l-tyrosine derivatives synthesis.
