6931-86-8

Upstream product

• 2768-50-5 dibenzyl L-glutamate 
• 13030-09-6 1-benzyl L-glutamate 
• 7365-91-5 C₃₉H₄₀N₂O₉ 
• 13515-99-6 D-glutamic acid dimethyl ester hydrochloride 
• 86938-17-2 2-(S)-tert-butoxycarbonylaminopentanedioic acid 1-ethyl ester 
• 23150-65-4 L-glutamic dimethyl ester hydrochloride 
• 449171-15-7 Boc-D-Glu-OEt 
• 6893-26-1 D-Glutamic acid 
• 56-86-0 L-glutamic acid 
• 3705-42-8 Cbz-(L)-Glu-OBn 
• 7365-90-4 benzyloxycarbonyl-α-benzyl-γ-L-glutamyl-D-glutamic acid dibenzyl ester 

Relevant academic research and scientific papers

γ-Glutamyl-dipeptides: Easy tools to rapidly probe the stereoelectronic properties of the ionotropic glutamate receptor binding pocket

γ-Glutamyl-dipeptides, built by condensing the distal carboxylate of L-Glu (or D-Glu) onto a series of differently functionalized amino acids, were prepared and used as tools for rapidly probing the stereo-electronic properties of iGluRs, searching for subtype-selective ligands.

Efficient peptide couplings and their use in the synthesis and isolation of a cyclopenta (G) quinazoline trisodium salt

A new method for the synthesis of L-Glutamyl-γ-D-Glutamic acid and its use in the synthesis of (2R)-((4S)-carboxy-4-(4,N-(((6S)-2-(hydroxymethyl)-4-oxo-3,4,7,8-tetrahydro-3H-cyclopenta[g]quinazolin-6-yl)-N-(prop-2-ynyl)amino)benzamido)butanamido)pentanedioic acid, 1 are provided. Also provided is an efficient method for the isolation and purification of the trisodium salt of the abovementioned acid, 2, in a form suitable for long term storage and use in a parenteral dosing form.

Microstructure of poly(γ-glutamic acid) produced by Bacillus subtilis consisting of clusters of D- and L-glutamic acid repeating units

Poly(γ-glutamic acid) (PGA) produced by a strain of Bacillus subtilis was partially hydrolyzed into various oligopeptides so that the dipeptide fraction was isolated by the preparative thin-layer chromatography. HPLC analysis was applied to the detection of each of the four stereoisomers in this fraction using chemically synthesized authentic samples. The fraction consisted of N-γ-D-glutamyl-D-glutamic acid, N-γ-L-glutamyl-L-glutamic acid, N-γ-D-glutamyl-L-glutamic acid, and N-γ-L-glutamyl-D-glutamic acid at a ratio of 5.9:6.0:1.0:1.0. On the basis of this result, a model was proposed for the microstructure of the bacterial PGA, in which D- and L-glutamic acid repeating units are alternately linked in a single chain of the molecule.

Synthesis of γ-Glutamyl Peptides Catalyzed by Transamidase from Bacillus natto

Crude ammonium sulfate fraction of a cell free extract from Bacillus natto contained an enzyme (or enzymes) which catalyzed the transamidation reaction specific for glutamine.Both L- and D-isomers of glutamine were active as substrate.On incubation of L- or D-glutamine with the enzyme preparation, two peptides consisting of glutamic acid and glutamine were formed.The main component of the peptides was readily isolated by ion-exchange chromatography and identified as γ-glutamylglutamine by paper chromatography and by paper electrophoresis using authentic peptides.The optical configuration of the amino acid residues in the dipeptide was determined by digestion of the acid hydrolyzate with L-glutamic acid decarboxylase, and the result showed that the dipeptide obtained from L-glutamine was a L-L isomer, while the dipeptide from D-glutamine was a D-D isomer.