80126-51-8

Basic information

• Product Name: L-3-Chlorophenylalanine
• Synonyms: L-Phe(3-Cl)-OH;3-(3-Chlorophenyl)-L-alanine;3-CHLORO-L-PHENYLALANINEHCL 99+%;L-3-Chloro-phe-OH;L-3-Chlorophenylalan;L-Phenylalanine,3-chloro-;L-Phe(3-Cl)-OH ] 3-Chloro-L-Phenylalanine;(S)-2-AMino-3-(3-chlorophenyl)propanoic acid
• CAS NO: 80126-51-8
• Molecular Formula: C₉H₁₀ClNO₂
• Molecular Weight: 199.63
• Product Categories: Phenylalanine [Phe, F];Unusual Amino Acids;a-amino;Amino Acids
• Mol File: 80126-51-8.mol
• Article Data: 10

Chemical Properties

• Melting Point: 215-216 °C(Solv: water (7732-18-5); methanol (67-56-1))
• Boiling Point: 339.5 °C at 760 mmHg
• Flash Point: 159.1 °C
• Appearance: /
• Density: 1.336 g/cm³
• Vapor Pressure: 3.54E-05mmHg at 25°C
• Refractive Index: 1.589
• Storage Temp.: Store at 0°C
• PKA: 2.17±0.10(Predicted)
• CAS DataBase Reference: L-3-Chlorophenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: L-3-Chlorophenylalanine(80126-51-8)
• EPA Substance Registry System: L-3-Chlorophenylalanine(80126-51-8)

Safety Data

• Hazard Codes: Xi
• Hazardous Substances Data: 80126-51-8(Hazardous Substances Data)

Usage

InChI:InChI=1/C9H10ClNO2/c10-7-3-1-2-6(4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)/t8-/m1/s1

Upstream product

• 1866-38-2 m-Chlorocinnamic acid 
• 1956-15-6 3-chlorophenylalanine 
• 587-04-2 m-Chlorobenzaldehyde 
• 1866-38-2 3-chlorocinnamic acid 
• 766-80-3 1-bromomethyl-3-chlorobenzene 
• 123052-80-2 (2S,5S)-2-tert-Butyl-5-(3-chloro-benzyl)-3-methyl-4-oxo-imidazolidine-1-carboxylic acid tert-butyl ester 

Downstream Products

• 1169765-66-5 Z-L-Phe(3Cl) 
• 1956-15-6 3-chlorophenylalanine 
• 132210-39-0 (rac)-2-benzamido-3-(3-chlorophenyl)propanoic acid 
• 80126-52-9 (R)-2-amino-3-(3-chlorophenyl)propanoic acid 
• 457654-55-6 D,L-3-chlorophenylalanine Ethyl Ester Hydrochloride 

Relevant articles and documents

A novel phenylalanine ammonia-lyase from Pseudozyma antarctica for stereoselective biotransformations of unnatural amino acids

A novel phenylalanine ammonia-lyase of the psychrophilic yeast Pseudozyma antarctica (PzaPAL) was identified by screening microbial genomes against known PAL sequences. PzaPAL has a significantly different substrate binding pocket with an extended loop (26 aa long) connected to the aromatic ring binding region of the active site as compared to the known PALs from eukaryotes. The general properties of recombinant PzaPAL expressed in E. coli were characterized including kinetic features of this novel PAL with L-phenylalanine (S)-1a and further racemic substituted phenylalanines rac-1b-g,k. In most cases, PzaPAL revealed significantly higher turnover numbers than the PAL from Petroselinum crispum (PcPAL). Finally, the biocatalytic performance of PzaPAL and PcPAL was compared in the kinetic resolutions of racemic phenylalanine derivatives (rac-1a-s) by enzymatic ammonia elimination and also in the enantiotope selective ammonia addition reactions to cinnamic acid derivatives (2a-s). The enantiotope selectivity of PzaPAL with o-, m-, p-fluoro-, o-, p-chloro- and o-, m-bromo-substituted cinnamic acids proved to be higher than that of PcPAL.

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.

Synthesis of D- and L-Phenylalanine Derivatives by Phenylalanine Ammonia Lyases: A Multienzymatic Cascade Process

The synthesis of substituted D-phenylalanines in high yield and excellent optical purity, starting from inexpensive cinnamic acids, has been achieved with a novel one-pot approach by coupling phenylalanine ammonia lyase (PAL) amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction). A simple high-throughput solid-phase screening method has also been developed to identify PALs with higher rates of formation of non-natural D-phenylalanines. The best variants were exploited in the chemoenzymatic cascade, thus increasing the yield and ee value of the D-configured product. Furthermore, the system was extended to the preparation of those L-phenylalanines which are obtained with a low ee value using PAL amination.