Issue 5, 2019
From the journal:

Organic & Biomolecular Chemistry

SurE is a trans-acting thioesterase cyclizing two distinct non-ribosomal peptides†

Kenichi Matsuda,a   Masakazu Kobayashi,a   Takefumi Kuranaga,a   Kentaro Takada,b   Haruo Ikeda,c   Shigeki Matsunaga ORCID logo b  and  Toshiyuki Wakimoto ORCID logo *a  

* Corresponding authors

a Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido 060-0812, Japan
E-mail: wakimoto@pharm.hokudai.ac.jp

b Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan

c Kitasato Institute for Life Sciences, Kitasato University, Sagamihara, 252-0373 Kanagawa, Japan

Abstract

SurE is a new, stand-alone thioesterase (TE) offloading the non-ribosomal peptide (NRP) assembly line found in surugamide biosynthesis. It is homologous to penicillin binding protein (PBP) and capable of cyclizing two structurally unrelated substrates derived from two different NRP assembly lines, highlighting the broad substrate tolerance of the SurE offloading cyclase.

Graphical abstract: SurE is a trans-acting thioesterase cyclizing two distinct non-ribosomal peptides

  • This article is part of the themed collection: Biosynthesis
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Article information

DOI
https://doi.org/10.1039/C8OB02867B
Article type
Communication
Submitted
16 Nov. 2018
Accepted
04 Janv. 2019
First published
05 Janv. 2019

Org. Biomol. Chem., 2019,17, 1058-1061

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SurE is a trans-acting thioesterase cyclizing two distinct non-ribosomal peptides

K. Matsuda, M. Kobayashi, T. Kuranaga, K. Takada, H. Ikeda, S. Matsunaga and T. Wakimoto, Org. Biomol. Chem., 2019, 17, 1058 DOI: 10.1039/C8OB02867B

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