De novo active sites for resurrected Precambrian enzymes

The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eli...

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Autores principales:	Valeria A. Risso, Sergio Martinez-Rodriguez, Adela M. Candel, Dennis M. Krüger, David Pantoja-Uceda, Mariano Ortega-Muñoz, Francisco Santoyo-Gonzalez, Eric A. Gaucher, Shina C. L. Kamerlin, Marta Bruix, Jose A. Gavira, Jose M. Sanchez-Ruiz
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7c76aaa815614d3a948e230f4b0670e6
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spelling	oai:doaj.org-article:7c76aaa815614d3a948e230f4b0670e62021-12-02T17:06:16ZDe novo active sites for resurrected Precambrian enzymes10.1038/ncomms161132041-1723https://doaj.org/article/7c76aaa815614d3a948e230f4b0670e62017-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms16113https://doaj.org/toc/2041-1723The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eliminase activity.Valeria A. RissoSergio Martinez-RodriguezAdela M. CandelDennis M. KrügerDavid Pantoja-UcedaMariano Ortega-MuñozFrancisco Santoyo-GonzalezEric A. GaucherShina C. L. KamerlinMarta BruixJose A. GaviraJose M. Sanchez-RuizNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Valeria A. Risso Sergio Martinez-Rodriguez Adela M. Candel Dennis M. Krüger David Pantoja-Uceda Mariano Ortega-Muñoz Francisco Santoyo-Gonzalez Eric A. Gaucher Shina C. L. Kamerlin Marta Bruix Jose A. Gavira Jose M. Sanchez-Ruiz De novo active sites for resurrected Precambrian enzymes
description	The emergence of novel catalytic functions in ancient proteins likely played a role in the evolution of modern enzymes. Here, the authors use protein sequences from Precambrian beta-lactamases and demonstrate that a single hydrophobic-to-ionizable amino acid mutation can lead to substantial Kemp eliminase activity.
format	article
author	Valeria A. Risso Sergio Martinez-Rodriguez Adela M. Candel Dennis M. Krüger David Pantoja-Uceda Mariano Ortega-Muñoz Francisco Santoyo-Gonzalez Eric A. Gaucher Shina C. L. Kamerlin Marta Bruix Jose A. Gavira Jose M. Sanchez-Ruiz
author_facet	Valeria A. Risso Sergio Martinez-Rodriguez Adela M. Candel Dennis M. Krüger David Pantoja-Uceda Mariano Ortega-Muñoz Francisco Santoyo-Gonzalez Eric A. Gaucher Shina C. L. Kamerlin Marta Bruix Jose A. Gavira Jose M. Sanchez-Ruiz
author_sort	Valeria A. Risso
title	De novo active sites for resurrected Precambrian enzymes
title_short	De novo active sites for resurrected Precambrian enzymes
title_full	De novo active sites for resurrected Precambrian enzymes
title_fullStr	De novo active sites for resurrected Precambrian enzymes
title_full_unstemmed	De novo active sites for resurrected Precambrian enzymes
title_sort	de novo active sites for resurrected precambrian enzymes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7c76aaa815614d3a948e230f4b0670e6
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De novo active sites for resurrected Precambrian enzymes

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