14091-11-3

Basic information

• Product Name: 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID
• Synonyms: DL-O-CHLOROPHENYLALANINE;2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID;2-CHLORO-DL-PHENYLALANINE;2-chloro-3-phenyl-DL-alanine;2-Chloro-Dl-Phenylalanine,>99%;2-CHLOROPHENYLALANINE;DL-Phe(2-Cl)-OH;H-DL-Phe(2-Cl)-OH
• CAS NO: 14091-11-3
• Molecular Formula: C₉H₁₀ClNO₂
• Molecular Weight: 199.63
• EINECS: 237-939-2
• Mol File: 14091-11-3.mol
• Article Data: 6

Chemical Properties

• Melting Point: 216-219 °C
• Boiling Point: 339.532 °C at 760 mmHg
• Flash Point: 159.143 °C
• Appearance: White lens powder
• Density: 1.336 g/cm³
• Refractive Index: 1.593
• Storage Temp.: Store at 0-5°C
• Solubility: Aqueous Acid (Slightly)
• PKA: pK1: 2.23(+1);pK2: 8.94(0) (25°C)
• CAS DataBase Reference: 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID(14091-11-3)
• EPA Substance Registry System: 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID(14091-11-3)

Safety Data

• Hazardous Substances Data: 14091-11-3(Hazardous Substances Data)

Usage

Uses

2-Chloro-DL-phenylalanine is used in the synthesis of 2-benzylpyrroles and 2-benzoylpyrroles with insecticidal and acaricidal activity.

InChI:InChI=1/C9H10ClNO2/c10-9(11,8(12)13)6-7-4-2-1-3-5-7/h1-5H,6,11H2,(H,12,13)/t9-/m0/s1

Upstream product

• 74164-07-1 N-benzoyl-2-chloro-phenylalanine 
• 5440-50-6 N-acetyl-3-(2-chlorophenyl)-2-ethoxycarbonyl alanine ethyl ester 
• 145243-37-4 2-(Benzhydrylidene-amino)-3-(2-chloro-phenyl)-propionic acid methyl ester 
• 103616-89-3 (2S)-2-amino-3-(2-chlorophenyl)propanoic acid 
• 704-96-1 trans-2-chlorocinnamic acid 
• 3752-25-8 o-chlorocinnamic acid 
• 77738-21-7 diethyl 2-(2-chlorobenzyl)malonate 
• 611-17-6 1-bromomethyl-2-chlorobenzene 
• 611-19-8 1-chloro-2-(chloromethyl)benzene 

Downstream Products

• 13078-80-3 2-(2-chlorophenyl)ethanamine 
• 704-96-1 trans-2-chlorocinnamic acid 
• 80126-50-7 (R)-2'-chlorophenylalanine 
• 103616-89-3 (2S)-2-amino-3-(2-chlorophenyl)propanoic acid 
• 90725-44-3 2-bromo-3-(2-chlorophenyl)propanoic acid 
• 1273308-52-3 C₂₁H₁₆Cl₂FNO₃S 
• 1273308-49-8 C₂₉H₂₂Cl₂FNO₅S 
• 1273308-46-5 C₉H₇Cl₂FO 
• 1273308-43-2 C₉H₈ClFO₂ 
• 1273308-38-5 2-(4-Chlorophenyl)-4-[3-(2-chlorophenyl)-2-fluoropropanoylamino]thiophene-3-carboxylic acid 
• 169676-25-9 Z-DL-Phe(2Cl)-OCH₂CF₃ 
• 141971-12-2 Z-DL-Phe(2Cl)OMe 
• 133373-31-6 rac-3-(2-chlorophenyl)-2-hydroxypropionic acid 
• 198560-41-7 3-(2-chloro-phenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid 

Relevant articles and documents

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Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway

Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.

Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis

The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous -amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.