Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors
Metalloproteinase inhibitors are leads for drug development, but their biosynthetic pathways are often unknown. Here the authors show that the acyl branched warhead of actinonin and matlystatins derives from an ethylmalonyl-CoA-like pathway and the structural diversity of matlystatins is due to the...
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| Language: | English |
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Nature Publishing Group
2017-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-01975-6 |
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doaj-33d55bdb2e15447e910a355a7a9c35662021-05-11T07:20:21ZengNature Publishing GroupNature Communications2041-17232017-12-018111210.1038/s41467-017-01975-6Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitorsFranziska Leipoldt0Javier Santos-Aberturas1Dennis P. Stegmann2Felix Wolf3Andreas Kulik4Rodney Lacret5Désirée Popadić6Daniela Keinhörster7Norbert Kirchner8Paulina Bekiesch9Harald Gross10Andrew W. Truman11Leonard Kaysser12Pharmaceutical Biology, Eberhard Karls University TübingenDepartment of Molecular Microbiology, John Innes Centre, Colney LanePharmaceutical Biology, Eberhard Karls University TübingenPharmaceutical Biology, Eberhard Karls University TübingenInterfaculty Institute of Microbiology and Infection Medicine, Microbiology/Biotechnology, Eberhard Karls University TübingenDepartment of Molecular Microbiology, John Innes Centre, Colney LaneDepartment of Molecular Microbiology, John Innes Centre, Colney LanePharmaceutical Biology, Eberhard Karls University TübingenPharmaceutical Biology, Eberhard Karls University TübingenPharmaceutical Biology, Eberhard Karls University TübingenPharmaceutical Biology, Eberhard Karls University TübingenDepartment of Molecular Microbiology, John Innes Centre, Colney LanePharmaceutical Biology, Eberhard Karls University TübingenMetalloproteinase inhibitors are leads for drug development, but their biosynthetic pathways are often unknown. Here the authors show that the acyl branched warhead of actinonin and matlystatins derives from an ethylmalonyl-CoA-like pathway and the structural diversity of matlystatins is due to the activity of a decarboxylase-dehydrogenase enzyme.https://doi.org/10.1038/s41467-017-01975-6 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Franziska Leipoldt Javier Santos-Aberturas Dennis P. Stegmann Felix Wolf Andreas Kulik Rodney Lacret Désirée Popadić Daniela Keinhörster Norbert Kirchner Paulina Bekiesch Harald Gross Andrew W. Truman Leonard Kaysser |
| spellingShingle |
Franziska Leipoldt Javier Santos-Aberturas Dennis P. Stegmann Felix Wolf Andreas Kulik Rodney Lacret Désirée Popadić Daniela Keinhörster Norbert Kirchner Paulina Bekiesch Harald Gross Andrew W. Truman Leonard Kaysser Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors Nature Communications |
| author_facet |
Franziska Leipoldt Javier Santos-Aberturas Dennis P. Stegmann Felix Wolf Andreas Kulik Rodney Lacret Désirée Popadić Daniela Keinhörster Norbert Kirchner Paulina Bekiesch Harald Gross Andrew W. Truman Leonard Kaysser |
| author_sort |
Franziska Leipoldt |
| title |
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| title_short |
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| title_full |
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| title_fullStr |
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| title_full_unstemmed |
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| title_sort |
warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2017-12-01 |
| description |
Metalloproteinase inhibitors are leads for drug development, but their biosynthetic pathways are often unknown. Here the authors show that the acyl branched warhead of actinonin and matlystatins derives from an ethylmalonyl-CoA-like pathway and the structural diversity of matlystatins is due to the activity of a decarboxylase-dehydrogenase enzyme. |
| url |
https://doi.org/10.1038/s41467-017-01975-6 |
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