458528-69-3

Usage

Uses

Used in Pharmaceutical Synthesis:
(S)-3-(2-bromophenyl)-2-hydroxypropionic acid is used as a key intermediate in the synthesis of various pharmaceuticals and biologically active molecules. Its unique structure and pharmacological properties contribute to the development of new drugs with potential therapeutic applications.
Used in Organic Synthesis:
In the field of organic chemistry, (S)-3-(2-bromophenyl)-2-hydroxypropionic acid serves as a versatile building block. Its bromine substituent on the phenyl ring allows for a range of organic reactions, facilitating the creation of diverse chemical compounds with specific functionalities.
Used in Anticancer Applications:
(S)-3-(2-bromophenyl)-2-hydroxypropionic acid is utilized as a potential anticancer agent. Its pharmacological properties, such as anti-inflammatory and neuroprotective activities, make it a promising candidate for the development of novel cancer treatments.
Used in Drug Development:
(S)-3-(2-bromophenyl)-2-hydroxypropionic acid's potential pharmacological properties, including its anti-inflammatory, anti-cancer, and neuroprotective activities, make (S)-3-(2-bromophenyl)-2-hydroxypropionic acid an important target for drug development. Researchers are exploring its potential in creating new therapeutic agents for various medical conditions.
Used in Organic Reactions:
(S)-3-(2-bromophenyl)-2-hydroxypropionic acid is employed as a valuable reactant in various organic reactions due to its bromine substituent on the phenyl ring. This feature enables the synthesis of a wide array of chemical compounds with specific properties and applications.

Upstream product

• 458528-59-1 (2-bromophenyl)acetaldehyde cyanohydrin 
• 18698-97-0 ortho-bromophenylacetic acid 
• 42538-40-9 (S)-2-amino-3-(2-bromophenyl)propanoic acid 

Downstream Products

• 917247-85-9 rac-3-(2-bromophenyl)-2-hydroxypropionic acid 

Relevant academic research and scientific papers

Nitrilases, nucleic acids encoding them and methods for making and using them

The invention relates to nitrilases and to nucleic acids encoding the nitrilases. In addition methods of designing new nitrilases and method of use thereof are also provided. The nitrilases have increased activity and stability at increased pH and temperature.

Biocatalytic racemization of (hetero)aryl-aliphatic α- hydroxycarboxylic acids by Lactobacillus spp. proceeds via an oxidation-reduction sequence

The biocatalytic racemization of a range of (hetero)aryl- and (di)aryl-aliphatic α-hydroxycarboxylic acids has been achieved by using whole resting cells of Lactobacillus spp. The essentially mild (physiological) reaction conditions ensure the suppression of undesired side reactions, such as elimination, decomposition or condensation. Cofactor/inhibitor studies using a cell-free extract of Lactobacillus paracasei DSM 20207 reveal that the addition of redox cofactors (NAD+/NADH) leads to a distinct increase in the racemization rate, while strong inhibition is observed in the presence of Thio-NAD+, which suggests that the racemization proceeds by an oxidation-reduction sequence rather than involvement of a "racemase" enzyme. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.

An enzyme library approach to biocatalysis: Development of nitrilases for enantioselective production of carboxylic acid derivatives

The discovery, from Nature, of a large and diverse set of nitrilases is reported. The utility of this nitrilase library for identifying enzymes that catalyze efficient production of valuable hydroxy carboxylic acid derivatives is demonstrated. Unprecedented enantioselectivity and substrate scope are highlighted for three newly discovered and distinct nitrilases. For example, a wide array of (R)-mandelic acid derivatives and analogues were produced with high rates, yields, and enantiomeric excesses (95-99% ee). We also have found nitrilases that provide direct access to (S)-phenyllactic acid and other aryllactic acid derivatives, again with high yields and enantioselectivities. Finally, different nitrilases have been discovered that catalyze enantiotopic hydrolysis of 3-hydroxyglutaronitrile to afford either enantiomer of 4-cyano-3-hydroxybutyric acid with high enantiomeric excesses (>95% ee). The first enzymes are reported that effect this transformation to furnish the (R)-4-cyano-3-hydroxybutyric acid which is a precursor to the blockbuster drug Lipitor. Copyright