Efficient rational modification of non-ribosomal peptides by adenylation domain substitution

Non-ribosomal peptide synthases are multimodular enzymes comprised of adenylation (A), condensation (C) and thiolation domains. Here, the authors show that non-ribosomal peptides can be generated solely by A domain substitutions, providing evidence that the postulated substrate specifying role of C-...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Mark J. Calcott, Jeremy G. Owen, David F. Ackerley
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/48924e1b8e5f493994a0d6dff8b81874
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:48924e1b8e5f493994a0d6dff8b81874
record_format	dspace
spelling	oai:doaj.org-article:48924e1b8e5f493994a0d6dff8b818742021-12-02T18:03:08ZEfficient rational modification of non-ribosomal peptides by adenylation domain substitution10.1038/s41467-020-18365-02041-1723https://doaj.org/article/48924e1b8e5f493994a0d6dff8b818742020-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18365-0https://doaj.org/toc/2041-1723Non-ribosomal peptide synthases are multimodular enzymes comprised of adenylation (A), condensation (C) and thiolation domains. Here, the authors show that non-ribosomal peptides can be generated solely by A domain substitutions, providing evidence that the postulated substrate specifying role of C-domains may be rare in nature.Mark J. CalcottJeremy G. OwenDavid F. AckerleyNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Mark J. Calcott Jeremy G. Owen David F. Ackerley Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
description	Non-ribosomal peptide synthases are multimodular enzymes comprised of adenylation (A), condensation (C) and thiolation domains. Here, the authors show that non-ribosomal peptides can be generated solely by A domain substitutions, providing evidence that the postulated substrate specifying role of C-domains may be rare in nature.
format	article
author	Mark J. Calcott Jeremy G. Owen David F. Ackerley
author_facet	Mark J. Calcott Jeremy G. Owen David F. Ackerley
author_sort	Mark J. Calcott
title	Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
title_short	Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
title_full	Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
title_fullStr	Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
title_full_unstemmed	Efficient rational modification of non-ribosomal peptides by adenylation domain substitution
title_sort	efficient rational modification of non-ribosomal peptides by adenylation domain substitution
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/48924e1b8e5f493994a0d6dff8b81874
work_keys_str_mv	AT markjcalcott efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution AT jeremygowen efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution AT davidfackerley efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution
_version_	1718378803422560256

Efficient rational modification of non-ribosomal peptides by adenylation domain substitution

Ejemplares similares