289639-45-8

Upstream product

• 6287-38-3 3,4-dichlorobenzaldehyde 
• 103860-25-9 3-(3,4-dichlorophenyl)-glutaric acid 
• 64-17-5 ethanol 
• 103982-67-8 3-(3,4-dichlorophenyl)-glutaric acid anhydride 

Relevant academic research and scientific papers

Studies on enzymatic synthesis of chiral non-racemic 3-arylglutaric acid monoesters

The enantioselective enzymatic desymmetrization (EED) of various 3-arylglutaric anhydrides 1 with alcohols in organic media has been studied. The effect of the solvent on the stereochemical outcome of the reaction was investigated in detail. The amount of biocatalyst was optimized, and the possibility of its re-use was tested. The first example of the EED of 3-substituted glutaric anhydrides with esters as nucleophiles is reported.

Enzymatic desymmetrization of 3-arylglutaric acid anhydrides

Optically active (R)- and (S)-3-arylglutaric acid monoesters 3 were synthesized in quantitative yields and good stereoselectivities by lipase-catalyzed desymmetrization of the corresponding 3-arylglutaric anhydrides 2 with alcohols. It was observed that the stereochemical outcome of the reaction was influenced by the substituents present on the aromatic ring. The influence of the enzyme, alcohol, and solvent was systematically examined. Absolute configurations of the monoesters 3 were assigned by chemical correlation to corresponding lactones 4.

Enzymatic Hydrolysis of a Prochiral 3-Substituted Glutarate Ester, an Intermediate in the Synthesis of an NK1/NK2 Dual Antagonist

An enzymatic process for desymmetrization of the prochiral diethyl 3-[3′,4′-dichlorophenyl]-glutarate, 1, an intermediate in the synthesis of a series of neurokinin (NK) receptor antagonists, has been developed and scaled up. The transformation catalyzed by Candida antarctica lipase B in either the free or the immobilized form was carried out at 100 g/L of substrate and proceeded with an average conversion of 97%. In the pilot plant, the process produced 200 kg of 2 in 3 batches with ee >99% and an average isolated yield of 80%. The immobilized enzyme preparation was particularly effective, achieving over 70,000 enzyme turnovers per batch.