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dc.contributor.authorAranda, Juan
dc.contributor.authorRoca, Maite
dc.contributor.authorTuñón, Iñaki
dc.date.accessioned2016-05-11T13:51:45Z
dc.date.available2016-05-11T13:51:45Z
dc.date.issued2012
dc.identifier.citationARANDA, Juan; ROCA, Maite; TUÑÓN, Iñaki. Substrate promiscuity in DNA methyltransferase M. Pvu II. A mechanistic insight. Organic & biomolecular chemistry, 2012, vol. 10, no 28, p. 5395-5400.ca_CA
dc.identifier.issn1477-0520
dc.identifier.issn1477-0539
dc.identifier.urihttp://hdl.handle.net/10234/159556
dc.description.abstractM.PvuII is a DNA methyltransferase from the bacterium Proteus vulgaris that catalyzes methylation of cytosine at the N4 position. This enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position. In this work we use QM/MM methods to investigate the reaction mechanism of this promiscuous activity. We found that N6 methylation in M.PvuII takes place by means of a stepwise mechanism in which deprotonation of the exocyclic amino group is followed by the methyl transfer. Deprotonation involves two residues of the active site, Ser53 and Asp96, while methylation takes place directly from the AdoMet cofactor to the target nitrogen atom. The same reaction mechanism was described for cytosine methylation in the same enzyme, while the reversal timing, that is methylation followed by deprotonation, has been described in M.TaqI, an enzyme that catalyzes the N6-adenine DNA methylation from Thermus aquaticus. These mechanistic findings can be useful to understand the evolutionary paths followed by N-methyltransferases.ca_CA
dc.description.sponsorShipThis work was supported by the Ministerio de Ciencia e Innovación project CTQ2009-14541-C02-02, Generalitat Valenciana projects ACOMP/2011/028, ACOM/2012/243, GV/2012/053 and Universitat de Valencia project UV-INV-AE11-40931. J.A. and M.R. thank Ministerio Ciencia e Innovación for a doctoral grant and a ‘Juan de la Cierva’ contract, respectively. The authors acknowledge computational facilities of the Servei d’Informàtica de la Universitat de València in the ‘Tirant’ supercomputer, which is part of the Spanish Supercomputing Network.
dc.format.extent17 p.ca_CA
dc.format.mimetypeapplication/pdfca_CA
dc.language.isoengca_CA
dc.publisherRoyal Society of Chemistryca_CA
dc.relation.isPartOfOrganic & Biomolecular Chemistry 10(28):5395-400ca_CA
dc.rights© Royal Society of Chemistry 2016ca_CA
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/*
dc.subjectM.PvuIIca_CA
dc.subjectDNA methyltransferaseca_CA
dc.subjectProteus vulgarisca_CA
dc.titleSubstrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insightca_CA
dc.typeinfo:eu-repo/semantics/articleca_CA
dc.identifier.doihttp://dx.doi.org/10.1039/c2ob07021a
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_CA
dc.relation.publisherVersionhttp://pubs.rsc.org/en/content/articlelanding/2012/ob/c2ob07021a#!divAbstractca_CA
dc.type.versioninfo:eu-repo/semantics/publishedVersionca_CA


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