1627096-62-1

Basic information

• Product Name: [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one
• Synonyms: [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one
• CAS NO: 1627096-62-1
• Molecular Weight: 233.188
• Mol File: 1627096-62-1.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one(CAS DataBase Reference)
• NIST Chemistry Reference: [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one(1627096-62-1)
• EPA Substance Registry System: [4-²H]-4(4-nitrobenzylidene)-2-methyloxazol-5(4H)-one(1627096-62-1)

Safety Data

• Hazardous Substances Data: 1627096-62-1(Hazardous Substances Data)

Upstream product

• 122-04-3 4-nitro-benzoyl chloride 
• 94781-50-7 α-deuterio-4-nitro-benzaldehyde 
• 543-24-8 N-acetylglycine 

Downstream Products

• 882-06-4 4-nitro-trans-cinnamic acid 
• 949-99-5 4-nitro-3-phenyl-L-alanine 
• 56613-61-7 (R)-4-nitro-phenylalanine 
• 1991-83-9 4-nitrophenylalanine 
• 1627105-54-7 trans-3[²H]-3(4-nitrophenyl)acrylic acid 
• 1627105-63-8 C₉H₉⁽²⁾HN₂O₄ 
• 1627107-35-0 C₉H₉⁽²⁾HN₂O₄ 
• 1627101-69-2 (R)-2-amino-3[(R)-²H]-3(4-nitrophenyl)propanoic acid hydrochloride 
• 1627099-40-4 (R)-methyl 2-acetamido-3[2H]-3(4-nitrophenyl)propanoate 
• 1627099-66-4 (S)-methyl 2-acetamido-3-[2H]-3(4-nitrophenyl)propanoate 
• 1627100-30-4 (R)-2-amino-3[(S)-²H]-3(4-nitrophenyl)propanoic acid hydrochloride 
• 1627100-31-5 (S)-2-acetamido-3-[²H]-3(4-nitrophenyl)propanoic acid 
• 1627098-43-4 [4-²H]-methyl 2-acetamido-3(4-nitrophenyl)acrylate 

Relevant articles and documents

Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway

Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.