An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase

Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in...

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Detalles Bibliográficos
Autores principales: Thibodeaux, Gabrielle N., van der Donk, Wilfred A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2012
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3475617/
https://www.ncbi.nlm.nih.gov/pubmed/23001385
http://dx.doi.org/10.1039/c2cc34138g
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author Thibodeaux, Gabrielle N.
van der Donk, Wilfred A.
author_facet Thibodeaux, Gabrielle N.
van der Donk, Wilfred A.
author_sort Thibodeaux, Gabrielle N.
collection PubMed
description Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo.
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spelling pubmed-34756172013-07-18 An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase Thibodeaux, Gabrielle N. van der Donk, Wilfred A. Chem Commun (Camb) Chemistry Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo. Royal Society of Chemistry 2012-11-07 2012-09-21 /pmc/articles/PMC3475617/ /pubmed/23001385 http://dx.doi.org/10.1039/c2cc34138g Text en This journal is © The Royal Society of Chemistry 2012 http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Thibodeaux, Gabrielle N.
van der Donk, Wilfred A.
An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title_full An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title_fullStr An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title_full_unstemmed An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title_short An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
title_sort engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3475617/
https://www.ncbi.nlm.nih.gov/pubmed/23001385
http://dx.doi.org/10.1039/c2cc34138g
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