HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

Heterochiral coupling in non-ribosomal peptide macrolactamization

Files in This Item:
WoS_94265_Wakimoto.pdf1.67 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79676

Title: Heterochiral coupling in non-ribosomal peptide macrolactamization
Authors: Matsuda, Kenichi Browse this author →KAKEN DB
Zhai, Rui Browse this author
Mori, Takahiro Browse this author
Kobayashi, Masakazu Browse this author
Sano, Ayae Browse this author
Abe, Ikuro Browse this author
Wakimoto, Toshiyuki Browse this author →KAKEN DB
Issue Date: 4-May-2020
Publisher: Nature Publishing Group
Journal Title: Nature Catalysis
Volume: 3
Start Page: 507
End Page: 515
Publisher DOI: 10.1038/s41929-020-0456-7
Abstract: Heterochiral coupling is favoured in abiotic peptide bond formation, whereas biotic peptide bond formation is dominated by homochiral coupling. Here, we report that heterochiral coupling is a rather general paradigm in the head-to-tail macrolactamization of non-ribosomal peptide biosynthesis. The canonical cis-acting offloading cyclases, such as type I thioesterase (TE) and terminal condensation-like domains, catalyse head-to-tail macrolactamization between N- and C-terminal residues with d- and l-configurations, respectively. In contrast, the penicillin-binding protein-type TEs, a recently identified family of trans-acting cyclases, couple heterochiral residues with complementary stereoselectivity to the canonical one. Thus, a suite of cis- and trans-TE non-ribosomal peptide synthetases could overcome the stereochemical constraints present in heterochiral head-to-tail macrolactam formation in bacterial non-ribosomal peptide biosynthesis. Furthermore, we provide the structural rationale for the C-terminal stereoselectivity of non-canonical offloading cyclases. Penicillin-binding protein-type TEs with broad substrate specificity are potentially applicable as biocatalysts and genetic tools for synthetic biology.
Type: article (author version)
URI: http://hdl.handle.net/2115/79676
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 脇本 敏幸

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University