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The N-terminal substrate specificity of the SurE peptide cyclase
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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9491159/ https://www.ncbi.nlm.nih.gov/pubmed/36062889 http://dx.doi.org/10.1039/d2ob01061e |
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author | Fazal, Asif Wheeler, Jake Webb, Michael E. Seipke, Ryan F. |
author_facet | Fazal, Asif Wheeler, Jake Webb, Michael E. Seipke, Ryan F. |
author_sort | Fazal, Asif |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9491159 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-94911592022-10-31 The N-terminal substrate specificity of the SurE peptide cyclase Fazal, Asif Wheeler, Jake Webb, Michael E. Seipke, Ryan F. Org Biomol Chem Chemistry 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. The Royal Society of Chemistry 2022-09-05 /pmc/articles/PMC9491159/ /pubmed/36062889 http://dx.doi.org/10.1039/d2ob01061e Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Fazal, Asif Wheeler, Jake Webb, Michael E. Seipke, Ryan F. The N-terminal substrate specificity of the SurE peptide cyclase |
title | The N-terminal substrate specificity of the SurE peptide cyclase |
title_full | The N-terminal substrate specificity of the SurE peptide cyclase |
title_fullStr | The N-terminal substrate specificity of the SurE peptide cyclase |
title_full_unstemmed | The N-terminal substrate specificity of the SurE peptide cyclase |
title_short | The N-terminal substrate specificity of the SurE peptide cyclase |
title_sort | n-terminal substrate specificity of the sure peptide cyclase |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9491159/ https://www.ncbi.nlm.nih.gov/pubmed/36062889 http://dx.doi.org/10.1039/d2ob01061e |
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