2752-32-1

Basic information

• Product Name: L-Aspartic acid, N-(phenylacetyl)-
• Synonyms: N-Phenylacetyl-L-asparaginsaeure;N-benzylcarbonyl aspartic acid
• CAS NO: 2752-32-1
• Molecular Formula: C12H13NO5
• Molecular Weight: 251.239
• Mol File: 2752-32-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: L-Aspartic acid, N-(phenylacetyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Aspartic acid, N-(phenylacetyl)-(2752-32-1)
• EPA Substance Registry System: L-Aspartic acid, N-(phenylacetyl)-(2752-32-1)

Safety Data

• Hazardous Substances Data: 2752-32-1(Hazardous Substances Data)

Upstream product

• 617-45-8 aspartic Acid 
• 101-41-7 benzeneacetic acid methyl ester 
• 101623-22-7 N-phenacetyl-α-L-aspartyl-L-phenylalanine methyl ester 
• 75596-69-9 (S)-dimethyl 2-(phenylacetamido)succinate 

Downstream Products

• 115929-98-1 Ac(Ph)-Asp-Phe-OMe*H-Phe-OMe 

Relevant articles and documents

Preparation of D-amino acids by enzymatic kinetic resolution using a mutant of penicillin-G acylase from E. coli

We have demonstrated for the first time that d-glutamine (d-Gln) and d-glutamic acid (d-Glu) can be efficiently obtained in high ee (97% and 90%, respectively) by enzymatic kinetic resolution of d,l-Gln and d,l-Glu. This was achieved by enantioselective conversion of the l-enantiomers to their N-phenylacetyl derivatives in aqueous solution, using a mutant of penicillin-G acylase (PGA) from E. coli and phenylacetic acid methylester as the acyl donor. Kinetic modeling studies suggest that the high ee values obtained are both due to a strong enantiopreference for the l-amino acid in the deacylation step of the covalent enzyme intermediate, as well as to completeness of conversion that is transiently obtained as a result of the distinct preference of the mutant PGA for phenylacetic acid methylester over the N-phenylacetyl-l-amino acid product. For the other amino acids tested (Asn, Asp, and Ser), the highest ee values that were obtained for the remaining d-enantiomer are moderate (50-80%) because of lower enantioselectivity in the enzyme deacylation step and due to less complete conversion of the l-amino acid caused by competition for the active site between the acyl donor and the N-phenylacetyl-l-amino acid that is produced. The results demonstrate that the mutated PGA has great potential for the production of optically active D-amino acids by kinetic resolution.

N-benzoylaspartate and N-phenylacetylaspartate from pea seeds

-