54582-05-7

Basic information

• Product Name: DL-Phenylalanine, N-(phenylacetyl)-
• CAS NO: 54582-05-7
• Molecular Formula: C17H17NO3
• Molecular Weight: 283.327
• Mol File: 54582-05-7.mol
• Article Data: 8

Chemical Properties

• CAS DataBase Reference: DL-Phenylalanine, N-(phenylacetyl)-(CAS DataBase Reference)
• NIST Chemistry Reference: DL-Phenylalanine, N-(phenylacetyl)-(54582-05-7)
• EPA Substance Registry System: DL-Phenylalanine, N-(phenylacetyl)-(54582-05-7)

Safety Data

• Hazardous Substances Data: 54582-05-7(Hazardous Substances Data)

Upstream product

• 103-82-2 phenylacetic acid 
• 1155-48-2 2-benzoylaminocinnamic acid 
• 156-06-9 2-oxo-3-(phenyl)propionic acid 
• 103-80-0 phenylacetyl chloride 
• 16367-71-8 t-butyl (RS)-phenylalaninate 
• 738-75-0 (S)-3-phenyl-2-phenylacetylamino-propionic acid 
• 150-30-1 Phenylalanine 
• 119582-12-6 α-(2-phenyl-acetylamino)-cinnamic acid 
• 816-66-0 4-methyl-2-oxopentanoic acid 
• 83556-31-4 Phac-DL-Phe-NH₂ 

Downstream Products

• 811461-80-0 N-phenyloxoacetyl-phenylalanine 
• 63-91-2 L-phenylalanine 
• 104513-36-2 1-(N-Phenylacetylamino)-2-phenylethylphosphonic acid 
• 36992-14-0 L-Phenylalanine phosphonate 
• 81838-43-9 N²-<(S)-N²-(phenylacetyl)phenylalanyl>-L-phenylalanine dimethylamide 
• 81837-87-8 N²-<(R)-N²-(phenylacetyl)phenylalanyl>-L-phenylalanine dimethylamide 
• 54076-39-0 (R)-N²-benzoylphenylalanine 
• 738-75-0 (S)-3-phenyl-2-phenylacetylamino-propionic acid 
• 103-82-2 phenylacetic acid 
• 150-30-1 Phenylalanine 
• 81838-42-8 2,4-dibenzyl-4H-oxazol-5-one 
• 110359-25-6 N-phenylacetyl-DL-phenylalanine ethyl ester 

Relevant articles and documents

Penicillin G acylase-mediated kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters

Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reacti

Resolution of α/β-amino acids by enantioselective penicillin G acylase from Achromobacter sp.

Penicillin G acylases (PGAs) are enantioselective enzymes catalyzing a hydrolysis of stable amide bond in a broad spectrum of substrates. Among them, derivatives of α- and β-amino acids represent a class of compounds with high application potential. PGAEc from Escherichia coli and PGAA from Achromobacter sp. CCM 4824 were used to catalyze enantioselective hydrolyses of seven selected N-phenylacetylated α/β-amino acid racemates. The PGAA showed higher stereoselectivity for enantiomers of N-PhAc-β-homoleucine, N-PhAc-α-tert-leucine and N-PhAc-β-leucine. To study the mechanism of enantiodiscrimination on molecular level, we have constructed a homology model of PGAA that was used in molecular docking experiments with the same substrates. In-silico experiments successfully reproduced the data from experimental enzymatic resolutions confirming validity of employed modeling protocol. We employed this protocol to evaluate enantiopreference of PGAA towards seven new substrates with application potential. For five of them, high enantioselectivity of PGAA was predicted.

Rhodium-catalysed racemisation of N-acyl α-amino acids

The first transition metal-catalysed racemisation of N-acyl α-amino acids, which is of importance for kinetic resolution processes, is described. Enantiomerically pure N-acyl α-amino acids were efficiently racemised under mild conditions using various rhodium complexes as catalysts, e.g. [Rh(cod)Cl]2, in the presence of phosphines. (C) 2000 Elsevier Science Ltd.