83234-64-4

Upstream product

• 56-41-7 L-alanin 
• 576-22-7 2-Bromo-m-xylene 
• 57646-33-0 methyl (2R)-2-[(2,6-dimethylphenyl)amino]propanoate 
• 67617-63-4 (S)-methyl 2-(2,6-dimethylphenylamino)propanoate 
• 67617-64-5 N-(2,6-dimethylphenyl)alanine 
• 52888-49-0 methyl N-(2,6-dimethylphenyl)alaninate 
• 67617-65-6 2-methoxyethyl N-(2,6-dimethylphenyl)alaninate 
• 67617-67-8 allyl N-(2,6-dimethylphenyl)alaninate 
• 712327-18-9 2-ethoxyethyl N-(2,6-dimethylphenyl)alaninate 

Downstream Products

• 51858-22-1 3-(2,6-dimethyl-phenyl)-4-methyl-sydnone 
• 91181-38-3 N-(2,6-dimethyl-phenyl)-N-nitroso-DL-alanine 

Relevant academic research and scientific papers

A Novel esterase from Pseudochrobactrum asaccharolyticum WZZ003: Enzymatic properties toward model substrate and catalytic performance in chiral fungicide intermediate synthesis

Only a few esterases have been used for the synthesis of optically pure fungicide. For example, (R)-metalaxyl synthesized using esterase-involved bioreaction displays fungicide activity, whereas (S)-enantiomer is redundant. However, the biosynthesis of (R

Enzyme-catalyzed preparation of methyl (R)-N-(2,6-dimethylphenyl)alaninate: A key intermediate for (R)-metalaxyl

A biocatalytic approach for the production of (R)-metalaxyl, mefenoxam, has been developed. A practical synthesis of methyl (R)-N-(2,6-dimethylphenyl) alaninate, a key intermediate for (R)-metalaxyl, has been developed by the use of lipase-catalyzed hydrolytic kinetic resolution and chemical racemization of the remaining ester. At high concentrations in aqueous media (300 g/L) lipases were stable and gave moderate to good conversions and excellent enantioselectivities (>98% ee). A simple extraction procedure was used to separate the acid product from the remaining ester and the acid was esterified with methanol to give methyl (R)-N-(2,6-dimethylphenyl)alaninate without any reduction in enantiomeric excess (>98% ee). Subsequent chemical coupling with methoxyacetyl chloride provided enantiomerically pure (R)-metalaxyl (>98% ee) without racemization.

Accelerating effect induced by the structure of α-amino acid in the copper-catalyzed coupling reaction of aryl halides with α-amino acids. Synthesis of benzolactam-V8

The coupling of optically pure α-amino acids with aryl halides produces enantiopure N-aryl-α-amino acids with retention of configuration under the catalysis of CuI. This reaction can complete at much lower temperature than typical Ullmann condensation even for electron-rich aryl halides, which indicates that an accelerating effect induced by the structure of the α- amino acid exists in this reaction. α-Amino acids with larger hydrophobic groups give higher coupling yields, while those with smaller hydrophobic groups only deliver lower yields and no coupling products were detected for those with hydrophilic groups. No racemization was observed in most cases of this coupling reaction. After some controlled experiments, a possible mechanism including the π-complex and the intramolecular substitution reaction is proposed. Based on this catalyzed reaction, a facile and stereoselective synthesis of benzolactam-V8, a new PKC activator, is achieved.