754971-91-0

Basic information

• Product Name: L-2,5-Dichlorophenylalanine
• Synonyms: L-2,5-Dichlorophenylalanine;H-Phe(2,5-DiCl)-OH;(S)-2-AMino-3-(2,5-dichlorophenyl)propanoic acid;L-Phenylalanine,2,5-dichloro-
• CAS NO: 754971-91-0
• Molecular Formula: C9H9Cl2NO2
• Molecular Weight: 234.07926
• Mol File: 754971-91-0.mol

Chemical Properties

• Boiling Point: 365.7±42.0 °C(Predicted)
• Appearance: /
• Density: 1.450±0.06 g/cm3(Predicted)
• Storage Temp.: Keep in dark place,Inert atmosphere,Room temperature
• PKA: 2.12±0.15(Predicted)
• CAS DataBase Reference: L-2,5-Dichlorophenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: L-2,5-Dichlorophenylalanine(754971-91-0)
• EPA Substance Registry System: L-2,5-Dichlorophenylalanine(754971-91-0)

Safety Data

• Hazardous Substances Data: 754971-91-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Synthesis:
L-2,5-Dichlorophenylalanine is utilized as a key intermediate in the synthesis of various pharmaceuticals, contributing to the development of novel therapeutic agents.
Used in Medicinal Chemistry Research:
As a research tool, L-2,5-Dichlorophenylalanine aids in the exploration of its potential as a drug target for a range of diseases, facilitating the advancement of medical treatments.
Used in Material Science:
L-2,5-Dichlorophenylalanine is employed in the development of new materials, leveraging its unique properties to enhance material performance and functionality.
Used in Chemical Process Development:
L-2,5-Dichlorophenylalanine serves as a building block in the creation of innovative chemical processes, potentially improving efficiency and expanding the scope of chemical synthesis.

Relevant articles and documents

METABOLISM OF D,L-CHLORO-PHENYLALANINES BY PHENYLALANINE AMINOTRANSFERASE ISOZYMES PURIFIED FROM BUSHBEAN SHOOTS

Key Word Index - Phaseolus vulgaris; Leguminosae; bushbean; metabolism; phenylalanine decarboxylase; phenylalanine aminotransferase; purification; substituted amino acids; D,L-chloro-phenylalanines.A series of mono-, di- and trichloro-D,L-phenylalanines was tested as substrates for both phenylalanine aminotransferase and phenylalanine decarboxylase partially purified from bushbean (Phaseolus vulgaris L.) seedling extracts by ammonium sulphate fractionation and Sephacryl S-300 gel filtration.While most of the D,L-chlorophenylalanines were transaminated at rates of 35-100percent of that observed with D,L-phenylalanine, no chloro-phenylalanine decarboxylase activity was observed.A transamination reaction is therefore likely to be the initial step in the conversion of chloro-phenylalanines to their corresponding chloro-phenylacetic acids via a reaction pathway similar to the known route for the metabolism of L-phenylalanine to phenylacetic acid.The highest specific activity of phenylalanine aminotransferase was found in both root and shoot tissues of bushbean at the 10-day stage of seedling growth.Partially purified extracts of these tissues were able to transaminate most of the mono- and dichloro-phenylalanines at ca 20-40percent of the rate observed with D,L-phenylalanine, while the trichloro-phenylalanines (assayed at lower concentrations due to solubility) were transaminated at rates equal to those observed with D,L-phenylalanine.The 4-chloro derivative was the best substrate tested showing rates of transamination that were 25percent higher than those observed with D,L-phenylalanine.Further purification of shoot fractions by DEAE-Sephacel chromatography resolved the phenylalanine aminotransferase activity into two peaks (enzymes I and II) which on further purification, were found to behave differently during hydrophobic chromatography and PAGE.These results indicated the presence of two isozymic forms of phenylalanine aminotransferase in bushbean shoots and both were found to catalyse transamination of the monochloro-phenylalanines examined in this study.