KAMATA Kazuaki    Department   Graduate School of Medical Science, Graduate School of Medical Science    Position   Assistant Professor (Fixed Term)
Article types	Original article
Language	English
Peer review	Peer reviewed
Title	Engineering of acyl ligase domain in nonribosomal peptide synthetases to change fatty acid moieties of lipopeptides
Journal	Formal name：communications chemistry Abbreviation：Commun Chem ISSN code：2399-3669
Domestic / Foregin	Foregin
Publisher	Springer Nature
Volume, Issue, Page	8(17),pp.doi.org/10.1038/s42004-024-01379-w
Author and coauthor	AOKI Rina†, KUMAGAWA Eri, KAMATA Kazuaki, AGO Hideo, SAKAI Naoki, HASUNUMA Tomohisa, TAOKA Naoaki, OHTA Yukari, KOBAYASHI Shingo*
Publication date	2025/01/21
Summary	Cyclic lipopeptides (CLPs) produced by the genus Bacillus are amphiphiles composed of hydrophilic amino acid and hydrophobic fatty acid moieties and are biosynthesised by non-ribosomal peptide synthetases (NRPSs). CLPs are produced as a mixture of homologues with different fatty acid moieties, whose length affects CLP activity. Iturin family lipopeptides are a family of CLPs comprising cyclic heptapeptides and β-amino fatty acids and have antimicrobial activity. There is little research on how the length of the fatty acid moiety of iturin family lipopeptides is determined. Here, we demonstrated that the acyl ligase (AL) domain determines the length of the fatty acid moiety in vivo. In addition, enzyme assays revealed how mutations in the substrate-binding pocket of the AL domain affected substrate specificity in vitro. Our findings have implications for the design of fatty acyl moieties for CLP synthesis using NRPS.
DOI	10.1038/s42004-024-01379-w