103616-89-3

Basic information

• Product Name: 2-Chloro-L-phenylalanine
• Synonyms: 2-CHLORO-PHE-OH HCL;2-Chloro-L-Phenylalanine HCl;(S)-2-amino-3-(2-chlorophenyl)propanoic acid;2-Chloro-L-phenylalaninehydrocloride;(2R)-2-amino-3-(2-chlorophenyl)propanoic acid;2-CHLORO-L-PHENYLALANINE HYDROCHLORIDE;L-H-Phe(2-Cl)-OH;3-(2-Chlorophenyl)-L-alanine
• CAS NO: 103616-89-3
• Molecular Formula: C₉H₁₀ClNO₂
• Molecular Weight: 199.63
• Product Categories: Amino Acids;Phenylalanine [Phe, F];Unusual Amino Acids;Amino hydrochloride;Peptide;A - HPeptide Synthesis;Amino Acid Derivatives;Amino Acids;Modified Amino Acids;Phenylalanine;a-amino
• Mol File: 103616-89-3.mol
• Article Data: 15

Chemical Properties

• Melting Point: 233-235°C
• Boiling Point: 339.5 °C at 760 mmHg
• Flash Point: 159.1 °C
• Appearance: /
• Density: 1.336 g/cm³
• Storage Temp.: −20°C
• Solubility: DMSO (Slightly), Water (Slightly)
• PKA: 2.16±0.10(Predicted)
• Water Solubility: Insoluble in water.
• CAS DataBase Reference: 2-Chloro-L-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Chloro-L-phenylalanine(103616-89-3)
• EPA Substance Registry System: 2-Chloro-L-phenylalanine(103616-89-3)

Safety Data

• Hazard Codes: Xi
• Safety Statements: 24/25
• WGK Germany: 3
• Hazardous Substances Data: 103616-89-3(Hazardous Substances Data)

Usage

Uses

The largest gain in affinity of all tested unnatural amino acids was observed for 2-chloro-L-phenylalanine.

InChI:InChI=1/C9H10ClNO2.ClH/c10-7-4-2-1-3-6(7)5-8(11)9(12)13;/h1-4,8H,5,11H2,(H,12,13);1H/t8-;/m0./s1

Upstream product

• 14091-11-3 rac-2-chlorophenylalanine 
• 704-96-1 trans-2-chlorocinnamic acid 
• 68208-20-8 3-amino-3-(2-chloro-phenyl)-propionic acid 
• 3752-25-8 o-chlorocinnamic acid 
• 611-17-6 1-bromomethyl-2-chlorobenzene 
• 855650-84-9 acetylamino-(2-chloro-benzyl)-malonic acid 
• 6955-12-0 (+/-)-N-acetyl-3-(2-chlorophenyl)alanine 
• 5440-50-6 N-acetyl-3-(2-chlorophenyl)-2-ethoxycarbonyl alanine ethyl ester 
• 103522-34-5 (S)-N-acetyl-o-chlorophenylalanine 
• 89-98-5 2-chloro-benzaldehyde 

Downstream Products

• 14091-11-3 rac-2-chlorophenylalanine 
• 80126-50-7 (R)-2'-chlorophenylalanine 
• 114873-02-8 N^α-[(tert-butoxy)carbonyl]-2-(chloro)-L-phenylalanine 
• 944470-58-0 (S)-tert-butyl 1-(2-chlorophenyl)-3-hydroxypropan-2-ylcarbamate 

Relevant articles and documents

Resolution of non-protein amino acids via microbial protease-catalyzed ester hydrolysis: Marked enhancement of enantioselectivity by the use of esters with longer alkyl chains and at low temperature

In the microbial protease-catalyzed hydrolysis of amino acid esters with the free α-amino group, the enantioselectivity can be enhanced greatly by employing esters with longer alkyl chains such as the isobutyl ester instead of the conventional methyl ester and by conducting the reaction at low temperature.

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.

Kinetic Resolution of Aromatic β-Amino Acids Using a Combination of Phenylalanine Ammonia Lyase and Aminomutase Biocatalysts

An enzymatic strategy for the preparation of (R)-β-arylalanines employing phenylalanine aminomutase and ammonia lyase (PAM and PAL) enzymes has been demonstrated. Candidate PAMs with the desired (S)-selectivity from Streptomyces maritimus (EncP) and Bacillus sp. (PabH) were identified via sequence analysis using a well-studied template sequence. The newly discovered PabH could be linked to the first ever proposed biosynthesis of pyloricidin-like secondary metabolites and was shown to display better β-lyase activity in many cases. In spite of this, a method combining the higher conversion of EncP with a strict α-lyase from Anabaena variabilis (AvPAL) was found to be more amenable, allowing kinetic resolution of five racemic substrates and a preparative-scale reaction with >98% (R) enantiomeric excess. This work represents an improved and enantiocomplementary method to existing biocatalytic strategies, allowing simple product separation and modular telescopic combination with a preceding chemical step using an achiral aldehyde as starting material. (Figure presented.).

Telescopic one-pot condensation-hydroamination strategy for the synthesis of optically pure L-phenylalanines from benzaldehydes

A chemo-enzymatic telescopic approach was designed for the synthesis of L-arylalanines in high yield and optical purity, starting from commercially available and inexpensive substituted benzaldehydes. The method exploits a chemical Knoevenagel–Doebner condensation (optimised to give complete conversions in a short reaction time, employing microwave irradiation) and a biocatalytic phenylalanine ammonia lyase mediated hydroamination (for the stereoselective addition of ammonia). The two reactions can be run sequentially in one pot, bringing together the advantages of chemical and biological catalysis. The preparative applicability was demonstrated with the synthesis of five L-dihalophenylalanines (71–84% yield, 98–99% ee) of relevance as molecular probes, for medicinal chemistry and for the synthesis of pharmaceutical ingredients.