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Cover Feature: Dissecting the Mechanism of Oligomerization and Macrocyclization Reactions of NRPS‐Independent Siderophore Synthetases (Chem. Eur. J. 60/2018)
Author(s) -
Rütschlin Sina,
Böttcher Thomas
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201804819
Subject(s) - nonribosomal peptide , siderophore , chemistry , stereochemistry , peptide , enzyme , cover (algebra) , combinatorial chemistry , biochemistry , biosynthesis , gene , mechanical engineering , engineering
True lords of the rings are NRPS‐independent siderophore (NIS; NRPS=nonribosomal peptide synthetase) synthetases (depicted as a protein surface representation) that produce macrocyclic hydroxamate siderophores of different ring sizes. Some NIS synthetases either dimerize or trimerize their substrates before macrocyclization. Exploiting the promiscuity of NIS synthetases with artificial substrates allowed for the interrogation of the mechanistic details and the development of a model explaining the differences between trimerizing and dimerizing enzymes. More information can be found in the Full Paper by T. Böttcher and S. Rütschlin on page 16044.