138514-97-3

Basic information

• Product Name: 7-FLUORO-L-TRYPTOPHAN
• Synonyms: 7-FLUORO-L-TRYPTOPHAN;L-Tryptophan, 7-fluoro-
• CAS NO: 138514-97-3
• Molecular Formula: C₁₁H₁₁FN₂O₂
• Molecular Weight: 222.22
• Mol File: 138514-97-3.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 7-FLUORO-L-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: 7-FLUORO-L-TRYPTOPHAN(138514-97-3)
• EPA Substance Registry System: 7-FLUORO-L-TRYPTOPHAN(138514-97-3)

Safety Data

• Hazardous Substances Data: 138514-97-3(Hazardous Substances Data)

Usage

General Description

7-Fluoro-L-tryptophan is a more advanced and specialized version of the essential amino acid tryptophan. Its fluorination alters the natural chemical structure of tryptophan, making it somewhat unique. This chemical is often used in scientific research, including biochemistry, immunology, and neuroscience to study protein-protein interactions, protein structure and dynamics, and biological processes. The addition of the fluorine atom to the tryptophan structure can cause changes in the chemical behavior and properties of the resulting compound, which can be advantageous in certain research contexts. That said, as a lab-grade chemical, it is not intended for food, drug, or household use.

Upstream product

• 387-44-0 7-fluoro-1H-indole 
• 56-45-1 L-serin 

Downstream Products

• 1956434-65-3 Fmoc-D-7F-Trp 

Relevant articles and documents

Dimethylallyltryptophan synthase. An enzyme-catalyzed electrophilic aromatic substitution

Dimethylallyltryptophan (DMAT) synthase catalyzes the alkylation of L-tryptophan at C(4) by dimethylallyl diphosphate (DMAPP) in the first pathway-specific step in the biosynthesis of ergot alkaloids. The mechanism of the reaction was studied with analogs of both substrates. Five 7-substituted derivatives of N-acetyltryptophan (2, Z = OCH3, CH3, F, CF3, and NO2) were synthesized. The L enantiomers of the free amino acids were obtained by selective hydrolysis of the racemate using aminoacylase from Aspergillus. In addition, the E and Z fluoromethyl and difluoromethyl analogs of DMAPP (1, Y = CH3, CH2F, CHF2) were prepared. Rates of the enzyme-catalyzed reactions were measured for the dimethylallyl derivatives with L-tryptophan and for the L-tryptophan derivatives with DMAPP. In addition, the relative reactivities of the methanesulfonate derivatives of the DMAPP analogs were determined for solvolysis in aqueous acetone. A Hammett plot for the tryptophan analogs gave a good linear correlation with p = -2.0. In addition, a Hammett plot of the logarithms of the relative rates of solvolysis and enzyme-catalyzed alkylation gave a positive linear correlation. These results indicate that the prenyl-transfer reaction catalyzed by DMAT synthase is an electrophilic aromatic substitution and is mechanistically similar to the electrophilic alkylation catalyzed by farnesyl diphosphate synthase.