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Usage

Uses

Used in Pharmaceutical Synthesis:
(2R,3R)-3-AMINO-3-(4-FLUORO-PHENYL)-2-HYDROXY-PROPIONIC ACID is used as a key intermediate in the synthesis of various pharmaceuticals and organic compounds. Its chiral nature and functional groups contribute to the development of new drugs and medications with specific therapeutic properties.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, (2R,3R)-3-AMINO-3-(4-FLUORO-PHENYL)-2-HYDROXY-PROPIONIC ACID is employed as a building block for the creation of novel drug candidates. The presence of the fluorine atom in the phenyl ring allows for enhanced biological activity and selectivity, making it a valuable component in the design of targeted therapeutic agents.
Used in Drug Development:
(2R,3R)-3-AMINO-3-(4-FLUORO-PHENYL)-2-HYDROXY-PROPIONIC ACID is utilized in drug development as a precursor for the production of various medications. Its unique structure and functional groups enable the creation of drugs with improved pharmacokinetic and pharmacodynamic profiles, leading to more effective treatments for a range of medical conditions.
Used in Biochemical Research:
In biochemical research, (2R,3R)-3-AMINO-3-(4-FLUORO-PHENYL)-2-HYDROXY-PROPIONIC ACID serves as a valuable tool for studying enzyme mechanisms, protein interactions, and other biological processes. Its chiral nature and functional groups allow researchers to probe the selectivity and specificity of biological systems, contributing to a deeper understanding of molecular recognition and function.

Upstream product

• 459-32-5 (E)-4-fluorocinnamic acid 

Relevant academic research and scientific papers

Exploring the scope of an α/β-aminomutase for the amination of cinnamate epoxides to arylserines and arylisoserines

Biocatalytic process-development continues to advance toward discovering alternative transformation reactions to synthesize fine chemicals. Here, a 5-methylidene-3,5-dihydro-4H-imidazol-4-one (MIO)-dependent phenylalanine aminomutase from Taxus canadensis (TcPAM) was repurposed to irreversibly biocatalyze an intermolecular amine transfer reaction that converted ring-substituted trans-cinnamate epoxide racemates to their corresponding arylserines. From among 12 substrates, the aminomutase ring-opened 3′-Cl-cinnamate epoxide to 3′-Cl-phenylserine 140 times faster than it opened the 4′-Cl-isomer, which was turned over slowest among all epoxides tested. GC/MS analysis of chiral auxiliary derivatives of the biocatalyzed phenylserine analogues showed that the TcPAM-transamination reaction opened the epoxides enantio- A nd diastereoselectively. Each product mixture contained (2S)+(2R)-anti (erythro) and (2S)+(2R)-syn (threo) pairs with the anti-isomers predominating (-90:10 dr). Integrating the vicinal proton signals in the 1H NMR spectrum of the enzyme-catalyzed phenylserines and calculating the chemical shift difference (?"?) between the anti and syn proton signals confirmed the diastereomeric ratios and relative stereochemistries. Application of a (2S)-threonine aldolase from E. coli further established the absolute stereochemistry of the chiral derivatives of the diastereomeric enzymatically derived products. The 2R:2S ratio for the biocatalyzed anti-isomers was highest (88:12) for 3′-NO2-phenylserine and lowest (66:34) for 4′-F-phenylserine. This showed that the stereospecificity of TcPAM is in part directed by the substituent-type on the cinnamate epoxide analogue. The catalyst also converted each cinnamate epoxide analogue to its corresponding isoserine, highlighting a biocatalytic route to arylisoserines, which play a key role in building the pharmacophore seen in anticancer and protease inhibitor drugs.