Fazal, A, Wheeler, J, Webb, ME orcid.org/0000-0003-3574-4686 et al. (1 more author) (2022) The N-terminal substrate specificity of the SurE peptide cyclase. Organic and Biomolecular Chemistry, 20 (36). pp. 7232-7235. ISSN 1477-0520
Abstract
SurE is a standalone peptide cyclase essential for the production of surugamide antibiotics. Although SurE catalyses the cyclisation of varied nonribosomal peptides in vivo, its substrate specificity is poorly understood. To address this issue, an on-resin SurE cyclisation assay was developed and in combination with SNAC thioesters and kinetic measurements was used to define the chemical space of the N-terminal substrate residue.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © The Royal Society of Chemistry 2022. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Molecular Microbiology (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/T008075/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 02 Sep 2022 15:20 |
Last Modified: | 01 Feb 2023 01:55 |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/D2OB01061E |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:190519 |