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. 2020 Jun 9;11:1183. doi: 10.3389/fmicb.2020.01183

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Copyright © 2020 Lagedroste, Reiners, Knospe, Smits and Schmitt.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Reaction and structure of common PTMs in lanthipeptides. During a first modification step (PTM 1) a dehydratase catalyzes the dehydration of serine and threonine residues (Dha, Dhb). In a second step (PTM 2.1) a cyclase catalyzes the Michael-type addition of a cysteine residue to a dehydrated amino acid. Within the active center an acid (H-A, e.g., His) protonates the enolate. Finally, the Lan or MeLan rings are formed. In some lanthipeptides an additional Michael-type addition reaction (PTM 2.2) is catalyzed by the cyclase yielding a Lab amino acid. In the scheme the stereochemistry of the chiral center in the final products are exemplary (e.g., DL-Lan; but LL-Lan is also possible). The acronym X_n stands for n-quantity amino acids. The scheme is modified and based on (Repka et al., 2017).