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
• Article Data: 1

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

General Description

L-2,5-Dichlorophenylalanine is a chemical compound with the molecular formula C9H9Cl2NO2. It is an amino acid derivative that contains two chlorine atoms on the phenyl ring. L-2,5-Dichlorophenylalanine is used as a research tool and a building block for the synthesis of various pharmaceuticals and organic compounds. L-2,5-Dichlorophenylalanine has been studied for its potential applications in the field of medicinal chemistry, including its role as a potential drug target for various diseases. Additionally, it has been investigated for its potential use in the development of new materials and chemical processes. Overall, L-2,5-Dichlorophenylalanine exhibits promising properties and has potential applications in various scientific and industrial fields.

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.