7415-89-6

Upstream product

• 69408-26-0 dibenzyl glutamate 
• 126401-10-3 N-carbobenzyloxy-L-glutamic acid alphabenzyl ester 
• 3705-42-8 Cbz-(L)-Glu-OBn 
• 2791-84-6 D-glutamic acid dibenzyl ester p-toluenesufonate salt 
• 56-86-0 L-glutamic acid 
• 2768-50-5 dibenzyl L-glutamate 
• 13030-09-6 1-benzyl L-glutamate 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 1116-22-9 (R)-2-((S)-4-amino-4-carboxybutanamido)pentanedioic acid 

Relevant academic research and scientific papers

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.