Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway

The bacterial enzyme PaaZ is involved in the breakdown of environmental pollutants via the aerobic-anaerobic hybrid pathway but its substrate transfer mechanism is not fully understood. Here, the authors present cryoEM structures of free and ligand-bound PaaZ that suggest a mechanism for internal su...

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Autores principales: Nitish Sathyanarayanan, Giuseppe Cannone, Lokesh Gakhar, Nainesh Katagihallimath, Ramanathan Sowdhamini, Subramanian Ramaswamy, Kutti R. Vinothkumar
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/6a6fe31ff0ab4ec58d220d185727fa01
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spelling oai:doaj.org-article:6a6fe31ff0ab4ec58d220d185727fa012021-12-02T15:35:53ZMolecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway10.1038/s41467-019-11931-12041-1723https://doaj.org/article/6a6fe31ff0ab4ec58d220d185727fa012019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11931-1https://doaj.org/toc/2041-1723The bacterial enzyme PaaZ is involved in the breakdown of environmental pollutants via the aerobic-anaerobic hybrid pathway but its substrate transfer mechanism is not fully understood. Here, the authors present cryoEM structures of free and ligand-bound PaaZ that suggest a mechanism for internal substrate channeling.Nitish SathyanarayananGiuseppe CannoneLokesh GakharNainesh KatagihallimathRamanathan SowdhaminiSubramanian RamaswamyKutti R. VinothkumarNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Nitish Sathyanarayanan
Giuseppe Cannone
Lokesh Gakhar
Nainesh Katagihallimath
Ramanathan Sowdhamini
Subramanian Ramaswamy
Kutti R. Vinothkumar
Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
description The bacterial enzyme PaaZ is involved in the breakdown of environmental pollutants via the aerobic-anaerobic hybrid pathway but its substrate transfer mechanism is not fully understood. Here, the authors present cryoEM structures of free and ligand-bound PaaZ that suggest a mechanism for internal substrate channeling.
format article
author Nitish Sathyanarayanan
Giuseppe Cannone
Lokesh Gakhar
Nainesh Katagihallimath
Ramanathan Sowdhamini
Subramanian Ramaswamy
Kutti R. Vinothkumar
author_facet Nitish Sathyanarayanan
Giuseppe Cannone
Lokesh Gakhar
Nainesh Katagihallimath
Ramanathan Sowdhamini
Subramanian Ramaswamy
Kutti R. Vinothkumar
author_sort Nitish Sathyanarayanan
title Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
title_short Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
title_full Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
title_fullStr Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
title_full_unstemmed Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
title_sort molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/6a6fe31ff0ab4ec58d220d185727fa01
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