A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

Catabolizing lignin-derived aromatic compounds requires an aryl-O-demethylation step. Here the authors present the structures of GcoA and GcoB, a cytochrome P450-reductase pair that catalyzes aryl-O-demethylations and show that GcoA displays broad substrate specificity, which is of interest for biot...

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Autores principales:	Sam J. B. Mallinson, Melodie M. Machovina, Rodrigo L. Silveira, Marc Garcia-Borràs, Nathan Gallup, Christopher W. Johnson, Mark D. Allen, Munir S. Skaf, Michael F. Crowley, Ellen L. Neidle, Kendall N. Houk, Gregg T. Beckham, Jennifer L. DuBois, John E. McGeehan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/794b35c1169a406b89565b7b8ae40208
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id	oai:doaj.org-article:794b35c1169a406b89565b7b8ae40208
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spelling	oai:doaj.org-article:794b35c1169a406b89565b7b8ae402082021-12-02T16:56:36ZA promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion10.1038/s41467-018-04878-22041-1723https://doaj.org/article/794b35c1169a406b89565b7b8ae402082018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04878-2https://doaj.org/toc/2041-1723Catabolizing lignin-derived aromatic compounds requires an aryl-O-demethylation step. Here the authors present the structures of GcoA and GcoB, a cytochrome P450-reductase pair that catalyzes aryl-O-demethylations and show that GcoA displays broad substrate specificity, which is of interest for biotechnology applications.Sam J. B. MallinsonMelodie M. MachovinaRodrigo L. SilveiraMarc Garcia-BorràsNathan GallupChristopher W. JohnsonMark D. AllenMunir S. SkafMichael F. CrowleyEllen L. NeidleKendall N. HoukGregg T. BeckhamJennifer L. DuBoisJohn E. McGeehanNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sam J. B. Mallinson Melodie M. Machovina Rodrigo L. Silveira Marc Garcia-Borràs Nathan Gallup Christopher W. Johnson Mark D. Allen Munir S. Skaf Michael F. Crowley Ellen L. Neidle Kendall N. Houk Gregg T. Beckham Jennifer L. DuBois John E. McGeehan A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
description	Catabolizing lignin-derived aromatic compounds requires an aryl-O-demethylation step. Here the authors present the structures of GcoA and GcoB, a cytochrome P450-reductase pair that catalyzes aryl-O-demethylations and show that GcoA displays broad substrate specificity, which is of interest for biotechnology applications.
format	article
author	Sam J. B. Mallinson Melodie M. Machovina Rodrigo L. Silveira Marc Garcia-Borràs Nathan Gallup Christopher W. Johnson Mark D. Allen Munir S. Skaf Michael F. Crowley Ellen L. Neidle Kendall N. Houk Gregg T. Beckham Jennifer L. DuBois John E. McGeehan
author_facet	Sam J. B. Mallinson Melodie M. Machovina Rodrigo L. Silveira Marc Garcia-Borràs Nathan Gallup Christopher W. Johnson Mark D. Allen Munir S. Skaf Michael F. Crowley Ellen L. Neidle Kendall N. Houk Gregg T. Beckham Jennifer L. DuBois John E. McGeehan
author_sort	Sam J. B. Mallinson
title	A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
title_short	A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
title_full	A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
title_fullStr	A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
title_full_unstemmed	A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion
title_sort	promiscuous cytochrome p450 aromatic o-demethylase for lignin bioconversion
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/794b35c1169a406b89565b7b8ae40208
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A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion

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