Substrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insight
Ver/ Abrir
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7013
comunitat-uji-handle3:10234/8638
comunitat-uji-handle4:
INVESTIGACIONMetadatos
Título
Substrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insightFecha de publicación
2012Editor
Royal Society of ChemistryISSN
1477-0520; 1477-0539Cita bibliográfica
ARANDA, 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.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.rsc.org/en/content/articlelanding/2012/ob/c2ob07021a#!divAbstractVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
M.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 ... [+]
M.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. [-]
Publicado en
Organic & Biomolecular Chemistry 10(28):5395-400Derechos de acceso
© Royal Society of Chemistry 2016
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
Aparece en las colecciones
- QFA_Articles [813]