| http://purl.uniprot.org/citations/7642617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7642617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7642617 | http://www.w3.org/2000/01/rdf-schema#comment | "Polyphosphates are a major constituent of the yeast Saccharomyces cerevisiae. A purification of the enzyme polyphosphate kinase (E.C. 2.7.4.1) from this organism has been reported (Felter, S., and Stahl, A.J.C. (1973) Biochimie (Paris) 55, 245-251). The assay for activity used in this purification was the production of 32P-labeled nucleotide, presumed to be ATP, in the presence of [32P]polyphosphate and ADP. We have found that this assay does not reflect the activity of a polyphosphate kinase but rather the combination of an exopolyphosphatase, releasing free [32P]phosphate from the added [32P]polyphosphate, and the ADP-[32P]phosphate exchange activity of the enzyme diadenosine 5',5"'-P1, P4-tetraphosphate alpha, beta-phosphorylase (Ap4A phosphorylase). We also present direct evidence for the formation of an enzyme-AMP intermediate in the actin of Ap4A phosphorylase."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.33.19377"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.33.19377"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/author | "Guidotti G."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/author | "Guidotti G."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/author | "Booth J.W."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/author | "Booth J.W."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/pages | "19377-19382"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/pages | "19377-19382"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/title | "An alleged yeast polyphosphate kinase is actually diadenosine-5', 5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/title | "An alleged yeast polyphosphate kinase is actually diadenosine-5', 5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase."xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/volume | "270"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://purl.uniprot.org/core/volume | "270"xsd:string |
| http://purl.uniprot.org/citations/7642617 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7642617 |
| http://purl.uniprot.org/citations/7642617 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7642617 |
| http://purl.uniprot.org/citations/7642617 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7642617 |
| http://purl.uniprot.org/citations/7642617 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7642617 |
| http://purl.uniprot.org/uniprot/P16550 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7642617 |
| http://purl.uniprot.org/uniprot/P16550#attribution-FC3627F46E5C692C2B1E2CE1F142CE34 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7642617 |