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language
eng
Author
Ozaki, Taro
Kurokawa, Yukari
Hayashi, Shohei The University of Tokyo
Oku, Naoya
Asamizu, Shumpei
Igarashi, Yasuhiro
Onaka, Hiroyasu
Description
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.
Subject
biosynthesis
dehydroalanine
glutamylation
goadsporin
natural products
RiPPs
Journal Title
Chembiochem : a European journal of chemical biology
Volume
17
Issue
3
Start Page
218
End Page
223
ISSN
14394227
Published Date
2016-01-08
DOI
NCID
AA11497584
Publisher
Wiley-VCH Verlag
NII Type
Journal Article
Format
PDF
Resource URL(IsVersionOf)
http://onlinelibrary.wiley.com/doi/10.1002/cbic.201500541/abstract
Rights
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Text Version
著者版
Gyoseki ID
e30610
OAI-PMH Set
Other
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