カマタ　カズアキ   KAMATA Kazuaki   鎌田　和明    所属   医学研究科 医学研究科 (医学部医学科をご参照ください)    職種   特任助教
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	Engineering of acyl ligase domain in nonribosomal peptide synthetases to change fatty acid moieties of lipopeptides
掲載誌名	正式名：communications chemistry 略　 称：Commun Chem ISSNコード：2399-3669
掲載区分	国外
出版社	Springer Nature
巻・号・頁	8(17),pp.doi.org/10.1038/s42004-024-01379-w
著者・共著者	AOKI Rina†, KUMAGAWA Eri, KAMATA Kazuaki, AGO Hideo, SAKAI Naoki, HASUNUMA Tomohisa, TAOKA Naoaki, OHTA Yukari, KOBAYASHI Shingo*
発行年月	2025/01/21
概要	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