English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/7040
Compartir / Impacto:
Add this article to your Mendeley library MendeleyBASE
Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título : Kinetic Properties of p53 Phosphorylation by the Human Vaccinia-Related Kinase 1
Autor : Barcia, R.; López-Borges, Susana; Vega, Francisco M.; Lazo, Pedro A.
Palabras clave : VRK1
Fecha de publicación : mar-2002
Editor: Elsevier
Citación : Arch. Biochem. Biophys. 399: 1-5 (2002)
Resumen: The vaccinia-related kinase 1 (VRK1) protein is a nuclear Ser-Thr kinase that phosphorylates p53 in Thr18. We have determined the enzyme properties regarding its different substrates. VRK1 has a high affinity for ATP (Km 50 M) and is thus saturated by the intracellular concentration of ATP in vivo. VRK1 uses preferentially magnesium, but is also functional with manganese and zinc. The VRK1 protein is autophosphorylated in multiple residues without effect on its activity. One autophosphorylated residue, T355, is within the VRK1 regulatory carboxy terminus. The kinase phosphorylates p53 with a Km of 1 M and is well suited to respond to the variations of intracellular p53 concentration, which fluctuates as a response to different types of cellular stress
URI : http://hdl.handle.net/10261/7040
Aparece en las colecciones: (IBMCC) Artículos
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro completo

NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.