作者: John A. McIntosh , Mohamed S. Donia , Satish K. Nair , Eric W. Schmidt
DOI: 10.1021/JA205458H
关键词:
摘要: The enzymatic basis of ribosomal peptide natural product prenylation has not been reported. Here, we characterize a prenyltransferase, LynF, from the TruF enzyme family. LynF is first characterized representative protein family, which responsible for both reverse- and forward-O-prenylation tyrosine, serine, threonine in cyclic peptides known as cyanobactins. We show that reverse O-prenylates tyrosine macrocyclic peptides. Based upon these results, propose family prenylates mature peptides, leader sequence other recognition elements have excised. This differs common model biosynthesis, required to direct post-translational modifications. In addition, find O-prenylated derivatives undergo facile Claisen rearrangement at ‘physiological’ temperature aqueous buffers, leading forward C-prenylated products. Although rearr...