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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/33d55bdb2e15447e910a355a7a9c3566
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spelling	oai:doaj.org-article:33d55bdb2e15447e910a355a7a9c35662021-12-02T15:38:54ZWarhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors10.1038/s41467-017-01975-62041-1723https://doaj.org/article/33d55bdb2e15447e910a355a7a9c35662017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01975-6https://doaj.org/toc/2041-1723Metalloproteinase 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.Franziska LeipoldtJavier Santos-AberturasDennis P. StegmannFelix WolfAndreas KulikRodney LacretDésirée PopadićDaniela KeinhörsterNorbert KirchnerPaulina BekieschHarald GrossAndrew W. TrumanLeonard KaysserNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2017
url	https://doaj.org/article/33d55bdb2e15447e910a355a7a9c3566
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Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors

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