Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/81170
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Synthesis of (di)nucleoside polyphosphates by the ubiquitin activating enzyme E1 |
Autor: | Günther Sillero, María A.; Diego, Anabel de CSIC; Silles, Eduardo CSIC; Sillero, Antonio CSIC | Fecha de publicación: | 2005 | Editor: | Elsevier | Citación: | FEBS Letters 579(27): 6223-6229 (2005) | Resumen: | Previous work from this laboratory had shown that ligases may catalyze the synthesis of (di)nucleoside polyphosphates. Here, we show that one of the enzymes of the proteasome system (E1 or the ubiquitin (Ub) activating enzyme, EC 6.3.2.19) catalyzes very effectively (kcat = 0.29 ± 0.05 s-1) the transfer of AMP from the E-AMP-ubiquitin complex to tripolyphosphate or tetrapolyphosphate with formation of adenosine tetra- or pentaphosphate (p4A or p5A), respectively. Whereas the concomitant formation of AMP is stimulated by the presence of dithiothreitol in a concentration dependent manner, the synthesis of p4A is only slightly inhibited by this compound. Previous treatment of the enzyme (E1) with iodoacetamide inhibited only partially the synthesis of p4A. p 4A can substitute for ATP as substrate of the reaction to generate the ubiquityl adenylate complex. A small amount of diadenosine pentaphosphate (Ap5A) was also synthesized in the presence of p4A. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | Descripción: | Open Access. | Versión del editor: | http://dx.doi.org/10.1016/j.febslet.2005.10.003 | URI: | http://hdl.handle.net/10261/81170 | DOI: | 10.1016/j.febslet.2005.10.003 | Identificadores: | doi: 10.1016/j.febslet.2005.10.003 issn: 0014-5793 e-issn: 1873-3468 |
Aparece en las colecciones: | (IIBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Synthesis of di.pdf | 296,72 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
2
checked on 27-mar-2024
SCOPUSTM
Citations
10
checked on 24-abr-2024
WEB OF SCIENCETM
Citations
10
checked on 23-feb-2024
Page view(s)
315
checked on 24-abr-2024
Download(s)
215
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.