Biosynthesis of cyclic oligopeptide.

Abstract

The first demonstration of the biosynthesis of oligopeptide in a cell-free enzyme system was made on glutathione by Johnston and Bloch in 1951. The enzymatic mechanism of glutathione synthesis was studied extensively by Bloch and his collaborators (Snoke and Bloch, 1952; Snoke, Yanari, and Bloch, 1953; Snoke, 1955; Snoke and Bloch, 1955; Mandeles and Bloch, 1955) and the involvement of λ-glutamyl phosphate as an active intermediate was suggested (Strumeyer and Bloch, 1960). Later, using λ-glutamyl-α-aminobutyrate, an intermediary dipeptide of ophthalmic acid synthesis, Nishimura, Dodd, and Meister (1963, 1964) proved that the activated form of the dipeptide was enzyme-bound dipeptidyl phosphate. The biosynthetic mechanism of muramyl pentapeptide of Staphylococcus aureus seems similar to that of glutathione. The peptide formation involves the release of inorganic phosphate from ATP (Ito and Strominger, 1964).