ダウンロード数 : ?
ID 38139
ファイル
言語
英語
著者
Ozaki, Taro
Kurokawa, Yukari
林 昌平 東京大学
Oku, Naoya
Asamizu, Shumpei
Igarashi, Yasuhiro
Onaka, Hiroyasu
内容記述(抄録等)
Dehydroalanines in goadsporin are proposed to be formed by GodF and GodG, which show slight homology to the N-terminal glutamylation and C-terminal elimination domains, respectively, of LanB, a class I lanthipeptide dehydratase. Although similar, separated-type LanBs are conserved among thiopeptides and indispensable for their biosynthesis and biological activities, these enzymes had not yet been characterized. Here, we identified goadsporin B, which has unmodified Ser4 and Ser14, from both godF and godG disruptants. The godG disruptant also produced goadsporin C, a glutamylated-Ser4 variant of goadsporin B. These results suggested that dehydroalanines are formed by glutamylation and glutamate elimination. NMR analysis revealed for the first time that the glutamyl group was attached to a serine via an ester bond, by the catalysis of LanB-type enzymes. Our findings provide insights into the function of separated-type LanBs involved in the biosynthesis of goadsporin and thiopeptides.
主題
biosynthesis
dehydroalanine
glutamylation
goadsporin
natural products
RiPPs
掲載誌名
Chembiochem : a European journal of chemical biology
17
3
開始ページ
218
終了ページ
223
ISSN
14394227
発行日
2016-01-08
DOI
NCID
AA11497584
出版者
Wiley-VCH Verlag
資料タイプ
学術雑誌論文
ファイル形式
PDF
関連情報URL(IsVersionOf)
http://onlinelibrary.wiley.com/doi/10.1002/cbic.201500541/abstract
権利関係
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
著者版/出版社版
著者版
業績ID
e30610
部局
他機関