124126-79-0

Upstream product

• 64-17-5 ethanol 
• 91569-94-7 N-benzoyl-DL-glutamic acid-anhydride 
• 6094-36-6 N-benzoyl-L-glutamic acid 
• 1119-33-1 (S)-2-Amino-pentanedioic acid 5-ethyl ester 
• 98-88-4 benzoyl chloride 
• 42807-47-6 N-benzoyl-L-glutamic acid diethyl ester 

Downstream Products

• 1154049-80-5 6-ethyl 1-methyl N-benzoyl-α,α-dimethyl-DL-β-homoglutamate 
• 1154049-75-8 C₁₆H₂₁NO₅ 
• 1378239-18-9 ethyl 4-benzamido-6-oxohexanoate 
• 1378239-17-8 ethyl 5,5-dimethyl-6-oxo-4-(benzamido)hexanoate 
• 114564-83-9 (2-phenyloxazol-5-yl)-acetic acid ethyl ester 
• 1227164-57-9 (2-phenyloxazol-5-yl)methyl acetate 
• 102466-34-2 N-(N-benzoyl-DL-α-glutamyl)-glycine hexylamide 

Relevant academic research and scientific papers

One-pot conversion of amino acids into 2,5-disubstituted oxazoles: No metals needed

2,5-Disubstituted oxazoles with a variety of alkyl and aryl groups are efficiently formed from N-acylamino acids, by a one-pot radical decarboxylation- oxidation-enolization and iodine-promoted cyclization process. Remarkably, the reaction takes place under mild conditions, and no metal catalysis is needed. The process can be useful for the direct modification of small peptides.

An Approach to Trapping γ-Glutamyl Radical Intermediates Proposed for Vitamin K Dependent Carboxylase: α,β-Methyleneglutamic Acid

The vitamin K dependent carboxylase activates the glutamyl γ-CH of substrate peptides for carboxylation by producing a γ-glutamyl free radical, a γ-glutamyl carbanion, or through a concerted carboxylation.We propose to intercept the putative γ-glutamyl free radical by the intramolecular rearrangement of a substrate containing the α,β-cyclopropane analogue of glutamic acid.The rearrangement of cyclopropylcarbinyl radicals into 2-butenyl radicals is rapid, exothermic, and considered diagnostis of free-radical formation.1-Amino-2-(carboxymethyl)cyclopropane-1-carboxylate, the β-cyclopropane analogue of glutamic acid, was synthesized starting from diethyl α-ketoglutarate.The α-keto ester was first treated with benzonitrile in sulfuric acid, to yield diethyl α,α-dibenzamidoglutarate.The α,α-dibenzamido acid was cleaved to produce the α,β-dehydroamino acid and benzamide on treatment with p-toluenesulfonic acid in hot benzene.Diazomethane addition to the dehydroamino acid resulted in cycloaddition of diazomethane and production of the pyrazoline, which upon irradiation lost N2 to give the protected cyclopropane-containing amino acid analogue.Acid hydrolysis of the N-benzoyl-α,β-methyleneglutamate diethyl ester resulted in the production of the unprotected amino acid, α,β-methyleneglutamic acid, in high yield.A single dehydroamino acid and a single methyleneglutamic acid isomer were produced in this synthesis; both are identified as the Z isomer, the former by NMR using the nuclear Overhauser effect and the latter through X-ray crystallographic analysis of N-benzoyl-α,β-methyleneglutamate diethyl ester.Saponification of a N-protectedmethyleneglutamic acid dialkyl ester using limiting alkali was shown to selectively yield the α-alkyl ester γ-acid.The reaction was used to produce α,β-cyclopropane-containing analogues of the carboxylase substrates N-t-Boc-L-glutamic acid α-benzyl ester and N-benzoyl-L-glutamic acid α-ethyl ester.The cyclpropane-containing analogues were tested and found to be neither substrates for nor inhibitors of the rat liver microsomal vitamin K dependent carboxylase.The inability of the enzyme to recognize these substrate analogues is attributed to the α-alkyl substitution, which apparently abolishes substrate binding.