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-...
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2020-09-01
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Online Access: | https://doi.org/10.1038/s41467-020-18365-0 |
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doaj-48924e1b8e5f493994a0d6dff8b818742021-09-12T11:48:32ZengNature Publishing GroupNature Communications2041-17232020-09-0111111010.1038/s41467-020-18365-0Efficient rational modification of non-ribosomal peptides by adenylation domain substitutionMark J. Calcott0Jeremy G. Owen1David F. Ackerley2School of Biological Sciences, Victoria University of WellingtonSchool of Biological Sciences, Victoria University of WellingtonSchool of Biological Sciences, Victoria University of WellingtonNon-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.https://doi.org/10.1038/s41467-020-18365-0 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mark J. Calcott Jeremy G. Owen David F. Ackerley |
spellingShingle |
Mark J. Calcott Jeremy G. Owen David F. Ackerley Efficient rational modification of non-ribosomal peptides by adenylation domain substitution Nature Communications |
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 Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-09-01 |
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. |
url |
https://doi.org/10.1038/s41467-020-18365-0 |
work_keys_str_mv |
AT markjcalcott efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution AT jeremygowen efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution AT davidfackerley efficientrationalmodificationofnonribosomalpeptidesbyadenylationdomainsubstitution |
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1717755339188731904 |