737751-95-0

Basic information

• Product Name: (R)-3-Amino-3-(2-bromo-phenyl)-propionic acid
• Synonyms: H-D-b-Phe(2-Br)-OH;(3R)-3-aMino-3-(2-broMophenyl)propanoic acid;D-3-Amino-3-(2-bromo)propanoic acid
• CAS NO: 737751-95-0
• Molecular Formula: C9H10BrNO2
• Molecular Weight: 244.09
• Mol File: 737751-95-0.mol
• Article Data: 7

Chemical Properties

• Melting Point: 232℃
• Boiling Point: 366.8±32.0 °C(Predicted)
• Appearance: /
• Density: 1.585±0.06 g/cm3(Predicted)
• Storage Temp.: Keep in dark place,Inert atmosphere,Room temperature
• PKA: 3.62±0.10(Predicted)
• Sensitive: Air Sensitive
• CAS DataBase Reference: (R)-3-Amino-3-(2-bromo-phenyl)-propionic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-3-Amino-3-(2-bromo-phenyl)-propionic acid(737751-95-0)
• EPA Substance Registry System: (R)-3-Amino-3-(2-bromo-phenyl)-propionic acid(737751-95-0)

Safety Data

• Hazardous Substances Data: 737751-95-0(Hazardous Substances Data)

Usage

General Description

(R)-3-Amino-3-(2-bromo-phenyl)-propionic acid is a chemical compound with the molecular formula C9H10BrNO2. It is an amino acid derivative and contains a bromophenyl group. (R)-3-Amino-3-(2-bromo-phenyl)-propionic acid is a chiral molecule, meaning it has a non-superimposable mirror image. It may have potential applications in medicinal chemistry, as well as in the development of pharmaceutical drugs and other biologically active compounds. Its specific properties and potential uses would depend on further research and analysis of its chemical and biological activity.

Upstream product

• 141-82-2 malonic acid 
• 6630-33-7 ortho-bromobenzaldehyde 
• 7345-79-1 2-bromocinnamic acid 
• 117391-48-7 3-amino-3-(2-bromo-phenyl)-propionic acid 

Downstream Products

• 1213854-52-4 C₁₀H₁₂BrNO₂ 

Relevant articles and documents

The bacterial ammonia lyase EncP: A tunable biocatalyst for the synthesis of unnatural amino acids

Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylates, yielding high value amino acids as products. Recent examples include the use of phenylalanine ammonia lyases (PALs), either alone or as a gateway to deracemization cascades (giving (S)- or (R)-α-phenylalanine derivatives, respectively), and also eukaryotic phenylalanine aminomutases (PAMs) for the synthesis of the (R)-β-products. Herein, we present the investigation of another family member, EncP from Streptomyces maritimus, thereby expanding the biocatalytic toolbox and enabling the production of the missing (S)-β-isomer. EncP was found to convert a range of arylacrylates to a mixture of (S)-α- and (S)-β-arylalanines, with regioselectivity correlating to the strength of electron-withdrawing/-donating groups on the ring of each substrate. The low regioselectivity of the wild-type enzyme was addressed via structure-based rational design to generate three variants with altered preference for either α- or β-products. By examining various biocatalyst/substrate combinations, it was demonstrated that the amination pattern of the reaction could be tuned to achieve selectivities between 99:1 and 1:99 for β:α-product ratios as desired.

Carica papaya lipase catalysed resolution of β-amino esters for the highly enantioselective synthesis of (S)-dapoxetine

An efficient synthesis of the (S)-3-amino-3-phenylpropanoic acid enantiomer has been achieved by Carica papaya lipase (CPL) catalysed enantioselective alcoholysis of the corresponding racemic N-protected 2,2,2-trifluoroethyl esters in an organic solvent. A high enantioselectivity (E > 200) was achieved by two strategies that involved engineering of the substrates and optimization of the reaction conditions. Based on the resolution of a series of amino acids, it was found that the structure of the substrate has a profound effect on the CPL-catalysed resolution. The enantioselectivity and reaction rate were significantly enhanced by switching the conventional methyl ester to an activated trifluoroethyl ester. When considering steric effects, the substituted phenyl and amino groups should not both be large for the CPL-catalysed resolution. The mechanism of the CPL-catalysed enantioselective alcoholoysis of the amino acids is discussed to delineate the substrate requirements for CPL-catalysed resolution. Finally, the reaction was scaled up, and the products were separated and obtained in good yields (≥ 80 %). The (S)-3-amino-3- phenylpropanoic acid obtained was used as a key chiral intermediate in the synthesis of (S)-dapoxetine with very high enantiomeric excess (> 99 %). A carica papaya lipase catalysed resolution of N-protected β-phenylalanine esters has been developed. High enantioselectivity was achieved by two strategies that involved engineering of the substrates and optimization of the reaction conditions. After 50 % conversion, the products were separated and used as key chiral intermediates for the synthesis of (S)-dapoxetine with > 99 % ee. Copyright

Phenylalanine aminomutase-catalyzed addition of ammonia to substituted cinnamic acids: A route to enantiopure α- and β-amino acids

(Chemical Equation Presented) An approach is described for the synthesis of aromatic α- and β-amino acids that uses phenylalanine aminomutase to catalyze a highly enantioselective addition of ammonia to substituted cinnamic acids. The reaction has a broad scope and yields substituted α- and β-phenylalanines with excellent enantiomeric excess. The regioselectivity of the conversion is determined by substituents present at the aromatic ring. A box model for the enzyme active site is proposed, derived from the influence of the hydrophobicity of substituents on the enzyme affinity toward various substrates.