176021-33-3

Basic information

• Product Name: (S)-2-(4-chlorophenylthio)propanoic acid
• Synonyms: (S)-2-(4-chlorophenylthio)propanoic acid
• CAS NO: 176021-33-3
• Molecular Weight: 216.688
• Mol File: 176021-33-3.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: (S)-2-(4-chlorophenylthio)propanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-(4-chlorophenylthio)propanoic acid(176021-33-3)
• EPA Substance Registry System: (S)-2-(4-chlorophenylthio)propanoic acid(176021-33-3)

Safety Data

• Hazardous Substances Data: 176021-33-3(Hazardous Substances Data)

Upstream product

• 106-54-7 p-Chlorothiophenol 
• 18527-14-5 2-((4-chlorophenyl)thio)propanenitrile 
• 18527-12-3 2-<(4-chlorophenyl)thio>propionic acid 
• 103247-65-0 2-<(4-Chlorphenyl)thio>-propansaeuremethylester 
• 18518-85-9 ethyl 2-((4-chlorophenyl)thio)propanoate 

Relevant articles and documents

Enantioselective Synthesis of α-Thiocarboxylic Acids by Nitrilase Biocatalysed Dynamic Kinetic Resolution of α-Thionitriles

The enantioselective synthesis of α-thiocarboxylic acids by biocatalytic dynamic kinetic resolution (DKR) of nitrile precursors exploiting nitrilase enzymes is described. A panel of 35 nitrilase biocatalysts were screened and enzymes Nit27 and Nit34 were found to catalyse the DKR of racemic α-thionitriles under mild conditions, affording the corresponding carboxylic acids with high conversions and good-to-excellent ee. The ammonia produced in situ during the biocatalytic transformation favours the racemization of the nitrile enantiomers and, in turn, the DKR without the need of any external additive base.

Enantioselective hydrolysis of some 2-aryloxyalkanoic acid methyl esters and isosteric analogues using a penicillin G acylase-based HPLC monolithic silica column

A technique based on liquid chromatography has been developed to facilitate studies of enantioselectivity in penicillin G acylase (PGA)-catalyzed hydrolysis of some 2-aryloxyalkanoic acid methyl esters and isosteric analogues. PGA was covalently immobilized on an aminopropyl monolithic silica support to create an immobilized HPLC-enzyme reactor. Two sets of experimental data were drawn to calculate the enantioselectivity (E) of the kinetically controlled enantiomer-differentiating reaction, the degree of substrate conversion and the enantiomeric excess of the product. The developed enzymatic reactor was coupled through a switching valve to an achiral analytical column for separation and quantitation of the hydrolysis products. The enantiomeric excess was determined off-line on a PGA-chiral stationary phase. In this way, highly precise E values were determined. A computational study related to the hydrolysis of the considered racemic esters was also carried out in order to unambiguously clarify both the substrate specificity and the enantioselectivity displayed by PGA.