Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide synthetases (NRPS)

A deletion mutant of tyrocidine synthetase 1 (Delta Delta TY1), comprising the adenylation domain of TY1 as an independent functional adenylate-formin g unit, was used to investigate the ability of the adenylation domain in no nribosomal peptide synthetases to catalyse peptide bond formation from the aminoacyl adenylate intermediate. The results demonstrate that only one sub strate amino acid needs to be activated as an aminoacyl adenylate, In view of the potential exploitation of peptide synthetases for enzymatic synthesi s of dipeptides of choice, it is important to note that this does not neces sarily require a dimodular construct or an intermediate acyl transfer step. (C) 2001 Federation of European Biochemical Societies. Published by Elsevi er Science B.V. All rights reserved.