| http://purl.uniprot.org/citations/10358060 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10358060 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10358060 | http://www.w3.org/2000/01/rdf-schema#comment | "S-Adenosylmethionine serves as the methyl donor for many biological methylation reactions and provides the propylamine group for the synthesis of polyamines. S-Adenosylmethionine is synthesized from methionine and ATP by the enzyme methionine adenosyltransferase. The cellular factors regulating S-adenosylmethionine synthesis have not been well defined. Here we show that in rat hepatocytes S-nitrosoglutathione monoethyl ester, a cell-permeable nitric oxide donor, markedly reduces cellular S-adenosylmethionine content via inactivation of methionine adenosyltransferase by S-nitrosylation. Removal of the nitric oxide donor from the incubation medium leads to the denitrosylation and reactivation of methionine adenosyltransferase and to the rapid recovery of cellular S-adenosylmethionine levels. Nitric oxide inactivates methionine adenosyltransferase via S-nitrosylation of cysteine 121. Replacement of the acidic (aspartate 355) or basic (arginine 357 and arginine 363) amino acids located in the vicinity of cysteine 121 by serine leads to a marked reduction in the ability of nitric oxide to S-nitrosylate and inactivate hepatic methionine adenosyltransferase. These results indicate that protein S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target cysteine."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.24.17075"xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.24.17075"xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Castro C."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Castro C."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Mato J.M."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Mato J.M."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Ruiz F.A."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Ruiz F.A."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Corrales F.J."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Corrales F.J."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Perez-Mato I."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/author | "Perez-Mato I."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/pages | "17075-17079"xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/pages | "17075-17079"xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/title | "Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/title | "Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol."xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10358060 | http://purl.uniprot.org/core/volume | "274"xsd:string |