5472-67-3

Usage

Uses

Used in Pharmaceutical and Agrochemical Industries:
3,4-Dichloro-DL-phenylalanine is used as a building block for the synthesis of various pharmaceuticals and agrochemicals, due to its ability to modulate bioactive compounds and its potential for developing new drugs.
Used in Medicinal Chemistry and Drug Discovery:
3,4-Dichloro-DL-phenylalanine is utilized as a key component in the discovery and development of new drugs, given its capacity to influence the properties and effectiveness of bioactive compounds.
Used in Asymmetric Synthesis:
3,4-Dichloro-DL-phenylalanine is employed as a chiral building block in asymmetric synthesis, which is important for the production of a wide range of chemical products with specific stereochemistry.
Used in the Development of New Materials and Technologies:
3,4-Dichloro-DL-phenylalanine is studied for its potential as a precursor in the synthesis of new materials and as a component in the advancement of new technologies, highlighting its versatility and importance in various scientific and industrial applications.

Upstream product

• 114872-55-8 acetylamino-(3,4-dichloro-benzyl)-malonic acid diethyl ester 
• 669775-24-0 N-benzoyl-(3',4'-dichloro)phenylalanine 
• 18880-04-1 3,4-dichlorobenzyl bromide 
• 59315-14-9 (3,4-dichloro-benzyl)-malonic acid diethyl ester 
• 669775-20-6 methyl (N-benzoyl)-3',4'-dichlorophenylalaninate 
• 146821-48-9 (3,4-dichloro-benzyl)-malonic acid 

Downstream Products

• 185321-62-4 2-tert-butyloxycarbonylamino-3-(3,4-dichlorophenyl)propionic acid 
• 376595-03-8 Fmoc-3,4-dichlorophenylalanine 
• 185321-65-7 3-amino-4-(3,4-dichlorophenyl)butyric acid 2-trimethylsilanyl ethyl ester 
• 185321-63-5 [3-diazo-1-(3,4-dichlorobenzyl)-2-oxo-propyl]carbamic acid tert-butyl ester 
• 185321-64-6 3-tert-butoxycarbonylamino-4-(3,4-dichlorophenyl)butyric acid 2-trimethylsilanyl ethyl ester 
• 52794-98-6 (R)-2-amino-3-(3,4-dichlorophenyl)propanoic acid 
• 52794-99-7 (S)-2-amino-3-(3,4-dichlorophenyl)propanoic acid 

Relevant academic research and scientific papers

Solid phase reduction of oxazolones using BER-Ni2B-A simple synthesis of N-benzoylphenylalanines

Borohydride exchange resin (BER)-Ni2B is successfully used as a reagent for the solid phase reduction of the C-4 exocyclic double bond of oxazolones to give the N-benzoylphenylalanines and hence the corresponding amino acids.

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.