Lantibiotics are ribosomally-synthesized and post-translationally modified antimicrobial peptides that are characterized by the thioether crosslinks lanthionine (Lan) and methyllanthionine (MeLan). Cinnamycin is a nineteen amino acid lantibiotic that contains one Lan and two MeLan crosslinks. Cinnamycin also contains an unusual lysinoalanine (Lal) bridge formed from the e-amino group of lysine 19 and a serine residue at position 6, and an erythro-3-hydroxy-L-aspartic acid resulting from the hydroxylation of L-aspartate at position 15. Recently, we showed that CinX is an a-ketoglutarate/iron(II)-dependent hydroxylase responsible from the hydroxylation of Asp15. CinM catalyzes dehydration of four Ser and Thr residues and subsequent cyclization of Cys residues to form the three (Me)Lan crosslinks. Although CinM dehydrated Ser6, it did not catalyze the formation of Lal. A small protein encoded by cinorf7 is critical for the formation of the crosslink between Lys19 and dehydroalanine 6. Herein, we investigated the tailoring proteins CinX and Cinorf7 in more detail.

Substrate specificity and mutational studies of CinX and Cinorf7 in cinnamycin biosynthesis

243rd National Meeting (2012)

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