| http://purl.uniprot.org/citations/11747420 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11747420 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11747420 | http://www.w3.org/2000/01/rdf-schema#comment | "The Sir2 enzyme family is responsible for a newly classified chemical reaction, NAD(+)-dependent protein deacetylation. New peptide substrates, the reaction mechanism, and the products of the acetyl transfer to NAD(+) are described for SIR2. The final products of SIR2 reactions are the deacetylated peptide and the 2' and 3' regioisomers of O-acetyl ADP ribose (AADPR), formed through an alpha-1'-acetyl ADP ribose intermediate and intramolecular transesterification reactions (2' --> 3'). The regioisomers, their anomeric forms, the interconversion rates, and the reaction equilibria were characterized by NMR, HPLC, 18O exchange, and MS methods. The mechanism of acetyl transfer to NAD(+) includes (1) ADP ribosylation of the peptide acyl oxygen to form a high-energy O-alkyl amidate intermediate, (2) attack of the 2'-OH group on the amidate to form a 1',2'-acyloxonium species, (3) hydrolysis to 2'-AADPR by the attack of water on the carbonyl carbon, and (4) an SIR2-independent transesterification equilibrating the 2'- and 3'-AADPRs. This mechanism is unprecedented in ADP-ribosyl transferase enzymology. The 2'- and 3'-AADPR products are candidate molecules for SIR2-initiated signaling pathways."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi011858j"xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Deng H."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Schramm V.L."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Boeke J.D."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Celic I."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Sauve A.A."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/author | "Avalos J."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/pages | "15456-15463"xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/title | "Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions."xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://purl.uniprot.org/core/volume | "40"xsd:string |
| http://purl.uniprot.org/citations/11747420 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11747420 |
| http://purl.uniprot.org/citations/11747420 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11747420 |
| http://purl.uniprot.org/citations/11747420 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11747420 |
| http://purl.uniprot.org/citations/11747420 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11747420 |
| http://purl.uniprot.org/enzyme/2.3.1.286 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11747420 |
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