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Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway
Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-d-Arg-containing autumnalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine a...
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/PMC9609003/ https://www.ncbi.nlm.nih.gov/pubmed/36193595 http://dx.doi.org/10.1039/d2cc01799g |
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author | Clemente, Claudia Johnson, Nicholas Ouyang, Xiaodan Popin, Rafael V. Dall'Angelo, Sergio Wahlsten, Matti Jokela, Jouni Colombano, Alessandro Nardone, Brunello Fewer, David P. Houssen, Wael E. |
author_facet | Clemente, Claudia Johnson, Nicholas Ouyang, Xiaodan Popin, Rafael V. Dall'Angelo, Sergio Wahlsten, Matti Jokela, Jouni Colombano, Alessandro Nardone, Brunello Fewer, David P. Houssen, Wael E. |
author_sort | Clemente, Claudia |
collection | PubMed |
description | Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-d-Arg-containing autumnalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications. |
format | Online Article Text |
id | pubmed-9609003 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-96090032022-11-07 Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway Clemente, Claudia Johnson, Nicholas Ouyang, Xiaodan Popin, Rafael V. Dall'Angelo, Sergio Wahlsten, Matti Jokela, Jouni Colombano, Alessandro Nardone, Brunello Fewer, David P. Houssen, Wael E. Chem Commun (Camb) Chemistry Cyanobactins are linear and cyclic post-translationally modified peptides. Here we show that the prenyl-d-Arg-containing autumnalamide A is a member of the cyanobactin family. Biochemical assays demonstrate that the AutF prenyltransferase targets the guanidinium moiety in arginine and homoarginine and is a useful tool for biotechnological applications. The Royal Society of Chemistry 2022-09-28 /pmc/articles/PMC9609003/ /pubmed/36193595 http://dx.doi.org/10.1039/d2cc01799g Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Clemente, Claudia Johnson, Nicholas Ouyang, Xiaodan Popin, Rafael V. Dall'Angelo, Sergio Wahlsten, Matti Jokela, Jouni Colombano, Alessandro Nardone, Brunello Fewer, David P. Houssen, Wael E. Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title | Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title_full | Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title_fullStr | Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title_full_unstemmed | Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title_short | Biochemical characterization of a cyanobactin arginine-N-prenylase from the autumnalamide biosynthetic pathway |
title_sort | biochemical characterization of a cyanobactin arginine-n-prenylase from the autumnalamide biosynthetic pathway |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9609003/ https://www.ncbi.nlm.nih.gov/pubmed/36193595 http://dx.doi.org/10.1039/d2cc01799g |
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