English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/23821
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Título

The role of cysteine-150 in the structure and activity of rat liver S-adenosyl-L-methionine synthetase

AutorPajares, María A. ; Corrales, Fernando; Ochoa, Pilar; Mato, José M.
Fecha de publicación15-feb-1991
EditorPortland Press
Biochemical Society
CitaciónBiochemical Journal 274(1): 225-229 (1991)
ResumenThe present paper reports the tryptic digestion of N-ethylmaleimide-treated S-adenosyl-L-methionine synthetase (high- and low-Mr forms) and the isolation of the modified peptides by h.p.l.c. There is only one site modified after 5 min incubation, and the modification at this site correlates with the main activity decrease. The amino acid composition of this peptide was determined, and its localization in the sequence shows the modified residue as cysteine-150, which is located close to the putative ATP-binding site. Modification of the enzyme for 20 min led to the appearance of a second labelled peptide, which seems to be responsible for about a further 10% of the activity loss. The modification by N-ethylmaleimide of the enzyme was partially prevented in the presence of adenosine 5'-[beta gamma-imido]triphosphate and methionine, further supporting the hypothesis that the modified residues lie within the active site. Urea treatment of the enzyme, followed by modification with N-ethylmaleimide, produces the modification of 7 of the 10 cysteine residues present in the sequence. The results obtained were the same for either of the isoforms.
Descripción5 pages, 3 figures, 3 tables.
Versión del editorhttp://www.biochemj.org/bj/274/bj2740225.htm
URIhttp://hdl.handle.net/10261/23821
ISSN0264-6021
Aparece en las colecciones: (IIBM) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 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.