1241684-03-6

Basic information

• Product Name: 2,6-Dichloro-D-Phenylalanine
• Synonyms: 2,6-Dichloro-D-Phenylalanine;H-D-Phe(2,6-Cl2)-OH;(R)-2-AMino-3-(2,6-dichlorophenyl)propanoic acid
• CAS NO: 1241684-03-6
• Molecular Formula: C9H9Cl2NO2
• Molecular Weight: 234.07926
• Mol File: 1241684-03-6.mol

Chemical Properties

• Boiling Point: 368.1±42.0 °C(Predicted)
• Appearance: /
• Density: 1.450±0.06 g/cm3(Predicted)
• PKA: 2.12±0.10(Predicted)
• CAS DataBase Reference: 2,6-Dichloro-D-Phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 2,6-Dichloro-D-Phenylalanine(1241684-03-6)
• EPA Substance Registry System: 2,6-Dichloro-D-Phenylalanine(1241684-03-6)

Safety Data

• Hazardous Substances Data: 1241684-03-6(Hazardous Substances Data)

Usage

Uses

Used in Scientific and Biochemical Research:
2,6-Dichloro-D-Phenylalanine is used as a research compound for its unique chemical properties, allowing scientists to explore its interactions with various biological systems and understand its potential effects on different organisms.
Used in Herbicide Formulations:
In the agricultural industry, 2,6-Dichloro-D-Phenylalanine is used as an active ingredient in herbicides, specifically for its ability to control the growth of weeds. Its application in this field is crucial for maintaining crop yields and ensuring the efficient use of agricultural land.
Used in Plant Physiology Studies:
2,6-Dichloro-D-Phenylalanine is employed as a tool in plant physiology research to investigate the effects of this compound on plant growth and development. This helps in understanding the underlying mechanisms of action and potential applications in crop management and protection.

Upstream product

• 5345-89-1 C₉H₆Cl₂O₂ 

Relevant articles and documents

Intensified biocatalytic production of enantiomerically pure halophenylalanines from acrylic acids using ammonium carbamate as the ammonia source

An intensified, industrially-relevant strategy for the production of enantiopure halophenylalanines has been developed using the novel combination of a cyanobacterial phenylalanine ammonia lyase (PAL) and ammonium carbamate reaction buffer. The process boasts STYs up to >200 g L-1 d-1, ees ≥ 98% and simplified catalyst/reaction buffer preparation and work up.

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.