Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ

The catalytic activity of dioxygenase AsqJ is strictly relying on the methylation of quinolone substrates. Here, the authors apply molecular simulations, X-ray crystallography and in vitro biochemical studies to the engineering of dioxygenase AsqJ with improved catalytic activity for modified non-me...

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Auteurs principaux:	Sophie L. Mader, Alois Bräuer, Michael Groll, Ville R. I. Kaila
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/774a7713e65b4a69a86781a9fc86afcc
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id	oai:doaj.org-article:774a7713e65b4a69a86781a9fc86afcc
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spelling	oai:doaj.org-article:774a7713e65b4a69a86781a9fc86afcc2021-12-02T17:32:16ZCatalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ10.1038/s41467-018-03442-22041-1723https://doaj.org/article/774a7713e65b4a69a86781a9fc86afcc2018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03442-2https://doaj.org/toc/2041-1723The catalytic activity of dioxygenase AsqJ is strictly relying on the methylation of quinolone substrates. Here, the authors apply molecular simulations, X-ray crystallography and in vitro biochemical studies to the engineering of dioxygenase AsqJ with improved catalytic activity for modified non-methylated surrogates.Sophie L. MaderAlois BräuerMichael GrollVille R. I. KailaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sophie L. Mader Alois Bräuer Michael Groll Ville R. I. Kaila Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
description	The catalytic activity of dioxygenase AsqJ is strictly relying on the methylation of quinolone substrates. Here, the authors apply molecular simulations, X-ray crystallography and in vitro biochemical studies to the engineering of dioxygenase AsqJ with improved catalytic activity for modified non-methylated surrogates.
format	article
author	Sophie L. Mader Alois Bräuer Michael Groll Ville R. I. Kaila
author_facet	Sophie L. Mader Alois Bräuer Michael Groll Ville R. I. Kaila
author_sort	Sophie L. Mader
title	Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
title_short	Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
title_full	Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
title_fullStr	Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
title_full_unstemmed	Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ
title_sort	catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase asqj
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/774a7713e65b4a69a86781a9fc86afcc
work_keys_str_mv	AT sophielmader catalyticmechanismandmolecularengineeringofquinolonebiosynthesisindioxygenaseasqj AT aloisbrauer catalyticmechanismandmolecularengineeringofquinolonebiosynthesisindioxygenaseasqj AT michaelgroll catalyticmechanismandmolecularengineeringofquinolonebiosynthesisindioxygenaseasqj AT villerikaila catalyticmechanismandmolecularengineeringofquinolonebiosynthesisindioxygenaseasqj
_version_	1718380376836014080

Catalytic mechanism and molecular engineering of quinolone biosynthesis in dioxygenase AsqJ

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