7540-08-1Relevant academic research and scientific papers
Synthesis of γ-Glutamyl Peptides Catalyzed by Transamidase from Bacillus natto
Noda, Kosaku,Igata, Keiko,Horikawa, Yoshiko,Fujii, Hisao
, p. 2419 - 2424 (2007/10/02)
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.
