Enzymatic Synthesis of Glutaselenone and its derivatives with γ-Glutamyltranspeptidase

Abstract

We investigated catalytic activity of γ-glutamyltranspeptidase on selenocysteine-containing peptides, and compaired with that on their cysteine analogues. Activity of the two types of the enzyme, one was from bovine kidney and the other was from E. coli, were assayed with γ-glutamyl-p-nitroanilide or L- and D-glutamine as γ-glutamyl donors and L-Se-benzy-selenocysteinyl-glycinemethylester or L-S-benzyl-cysteinyl-glycine methylester as γ-glutamyl accepters. The results obtained from the investigation of γ-glutamyltransferase activity was applied to the synthesis of glutaselenone derivatives.