A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases

Carbapenem-resistant bacteria pose a major health threat by expressing metallo-β-lactamases (MβLs), enzymes able to hydrolyse these life-saving drugs. Here the authors use biophysical and computational methods and show that different MβLs share the same reaction mechanism, suggesting new strategies...

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Autores principales:	María-Natalia Lisa, Antonela R. Palacios, Mahesh Aitha, Mariano M. González, Diego M. Moreno, Michael W. Crowder, Robert A. Bonomo, James Spencer, David L. Tierney, Leticia I. Llarrull, Alejandro J. Vila
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/211e1f98c03048a78682481a30189109
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spelling	oai:doaj.org-article:211e1f98c03048a78682481a301891092021-12-02T17:06:14ZA general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases10.1038/s41467-017-00601-92041-1723https://doaj.org/article/211e1f98c03048a78682481a301891092017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00601-9https://doaj.org/toc/2041-1723Carbapenem-resistant bacteria pose a major health threat by expressing metallo-β-lactamases (MβLs), enzymes able to hydrolyse these life-saving drugs. Here the authors use biophysical and computational methods and show that different MβLs share the same reaction mechanism, suggesting new strategies for drug design.María-Natalia LisaAntonela R. PalaciosMahesh AithaMariano M. GonzálezDiego M. MorenoMichael W. CrowderRobert A. BonomoJames SpencerDavid L. TierneyLeticia I. LlarrullAlejandro J. VilaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q María-Natalia Lisa Antonela R. Palacios Mahesh Aitha Mariano M. González Diego M. Moreno Michael W. Crowder Robert A. Bonomo James Spencer David L. Tierney Leticia I. Llarrull Alejandro J. Vila A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
description	Carbapenem-resistant bacteria pose a major health threat by expressing metallo-β-lactamases (MβLs), enzymes able to hydrolyse these life-saving drugs. Here the authors use biophysical and computational methods and show that different MβLs share the same reaction mechanism, suggesting new strategies for drug design.
format	article
author	María-Natalia Lisa Antonela R. Palacios Mahesh Aitha Mariano M. González Diego M. Moreno Michael W. Crowder Robert A. Bonomo James Spencer David L. Tierney Leticia I. Llarrull Alejandro J. Vila
author_facet	María-Natalia Lisa Antonela R. Palacios Mahesh Aitha Mariano M. González Diego M. Moreno Michael W. Crowder Robert A. Bonomo James Spencer David L. Tierney Leticia I. Llarrull Alejandro J. Vila
author_sort	María-Natalia Lisa
title	A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
title_short	A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
title_full	A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
title_fullStr	A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
title_full_unstemmed	A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
title_sort	general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/211e1f98c03048a78682481a30189109
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A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases

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