An enzymatic activation of formaldehyde for nucleotide methylation

The bacterial thymidylate synthase ThyX catalyzes the reductive methylation of deoxyuridylate (dUMP) into deoxythymidylate (dTMP) and requires both folate and flavin for activity. Here, the authors combine biochemical experiments, spectroscopic measurements and flavin synthesis chemistry to show tha...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Charles Bou-Nader, Frederick W. Stull, Ludovic Pecqueur, Philippe Simon, Vincent Guérineau, Antoine Royant, Marc Fontecave, Murielle Lombard, Bruce A. Palfey, Djemel Hamdane
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9d2804fa1f2e4892889a444777040660
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:9d2804fa1f2e4892889a444777040660
record_format	dspace
spelling	oai:doaj.org-article:9d2804fa1f2e4892889a4447770406602021-12-02T16:23:43ZAn enzymatic activation of formaldehyde for nucleotide methylation10.1038/s41467-021-24756-82041-1723https://doaj.org/article/9d2804fa1f2e4892889a4447770406602021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24756-8https://doaj.org/toc/2041-1723The bacterial thymidylate synthase ThyX catalyzes the reductive methylation of deoxyuridylate (dUMP) into deoxythymidylate (dTMP) and requires both folate and flavin for activity. Here, the authors combine biochemical experiments, spectroscopic measurements and flavin synthesis chemistry to show that formaldehyde (CH2O) can replace the natural methylene donor of ThyX in a CH2O-shunt reaction, yielding a carbinolamine intermediate with the reduced flavin coenzyme, and they present the crystal structure of this intermediate.Charles Bou-NaderFrederick W. StullLudovic PecqueurPhilippe SimonVincent GuérineauAntoine RoyantMarc FontecaveMurielle LombardBruce A. PalfeyDjemel HamdaneNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Charles Bou-Nader Frederick W. Stull Ludovic Pecqueur Philippe Simon Vincent Guérineau Antoine Royant Marc Fontecave Murielle Lombard Bruce A. Palfey Djemel Hamdane An enzymatic activation of formaldehyde for nucleotide methylation
description	The bacterial thymidylate synthase ThyX catalyzes the reductive methylation of deoxyuridylate (dUMP) into deoxythymidylate (dTMP) and requires both folate and flavin for activity. Here, the authors combine biochemical experiments, spectroscopic measurements and flavin synthesis chemistry to show that formaldehyde (CH2O) can replace the natural methylene donor of ThyX in a CH2O-shunt reaction, yielding a carbinolamine intermediate with the reduced flavin coenzyme, and they present the crystal structure of this intermediate.
format	article
author	Charles Bou-Nader Frederick W. Stull Ludovic Pecqueur Philippe Simon Vincent Guérineau Antoine Royant Marc Fontecave Murielle Lombard Bruce A. Palfey Djemel Hamdane
author_facet	Charles Bou-Nader Frederick W. Stull Ludovic Pecqueur Philippe Simon Vincent Guérineau Antoine Royant Marc Fontecave Murielle Lombard Bruce A. Palfey Djemel Hamdane
author_sort	Charles Bou-Nader
title	An enzymatic activation of formaldehyde for nucleotide methylation
title_short	An enzymatic activation of formaldehyde for nucleotide methylation
title_full	An enzymatic activation of formaldehyde for nucleotide methylation
title_fullStr	An enzymatic activation of formaldehyde for nucleotide methylation
title_full_unstemmed	An enzymatic activation of formaldehyde for nucleotide methylation
title_sort	enzymatic activation of formaldehyde for nucleotide methylation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/9d2804fa1f2e4892889a444777040660
work_keys_str_mv	AT charlesbounader anenzymaticactivationofformaldehydefornucleotidemethylation AT frederickwstull anenzymaticactivationofformaldehydefornucleotidemethylation AT ludovicpecqueur anenzymaticactivationofformaldehydefornucleotidemethylation AT philippesimon anenzymaticactivationofformaldehydefornucleotidemethylation AT vincentguerineau anenzymaticactivationofformaldehydefornucleotidemethylation AT antoineroyant anenzymaticactivationofformaldehydefornucleotidemethylation AT marcfontecave anenzymaticactivationofformaldehydefornucleotidemethylation AT muriellelombard anenzymaticactivationofformaldehydefornucleotidemethylation AT bruceapalfey anenzymaticactivationofformaldehydefornucleotidemethylation AT djemelhamdane anenzymaticactivationofformaldehydefornucleotidemethylation AT charlesbounader enzymaticactivationofformaldehydefornucleotidemethylation AT frederickwstull enzymaticactivationofformaldehydefornucleotidemethylation AT ludovicpecqueur enzymaticactivationofformaldehydefornucleotidemethylation AT philippesimon enzymaticactivationofformaldehydefornucleotidemethylation AT vincentguerineau enzymaticactivationofformaldehydefornucleotidemethylation AT antoineroyant enzymaticactivationofformaldehydefornucleotidemethylation AT marcfontecave enzymaticactivationofformaldehydefornucleotidemethylation AT muriellelombard enzymaticactivationofformaldehydefornucleotidemethylation AT bruceapalfey enzymaticactivationofformaldehydefornucleotidemethylation AT djemelhamdane enzymaticactivationofformaldehydefornucleotidemethylation
_version_	1718384125603217408

An enzymatic activation of formaldehyde for nucleotide methylation

Ejemplares similares