English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/13811
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Título

Structural aspects on rat liver S-adenosylmethionine synthesis

AutorPajares, María A. ; Gasset, M. ; Sanz-Aparicio, J. ; Calvete, Juan J. ; Arrondo, José Luis R.
Palabras claveStructure
S-adenosylmethionine synthetase
Methionine adenosyltransferase
S-adenosylmethionine
Fecha de publicación2003
EditorGlobal Research Network
CitaciónResearch Advances in Biological Chemistry: 31-41 (2003)
ResumenMethionine adenosyltransferase is the enzyme that catalyzes the synthesis of S-adenosylmethionine. In mammals three isoenzymes have been purified, two of which. MAT III and I, are products of the same gene MAT1A, but differ in their kinetic constants and oligomerization state. Changes in activity and MAT I/III ratio have been detected in animal models and in human alcohol liver cirrhosis, leading to an increasing interest in the mechanisms that control the protein association state. In this line, data demonstrating the importance of sulfhydryl groups on the activity and oligomerization of the protein have been obtained. These results along with knowledge of the crystal structure of MAT I and the establishment of an overall-folding pathway allow an integrated view for MAT behaviour.
URIhttp://hdl.handle.net/10261/13811
Aparece en las colecciones: (IIBM) Libros y partes de libros
(IQFR) Libros y partes de libros
(IBV) Libros y partes de libros
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
revision MAT India.pdf771,72 kBAdobe PDFVista previa
Visualizar/Abrir
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.