| http://purl.uniprot.org/citations/8218176 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8218176 | http://www.w3.org/2000/01/rdf-schema#comment | "We have shown previously that 6-phosphofructo-2-kinase in yeast has negligible fructose-2,6-bisphosphatase activity even though resembling in part of its C-terminal sequence the phosphatase domain of the bifunctional liver enzyme. Here we show that exchanging Ser-404 to His-404 in the yeast peptide creates a bifunctional enzyme with a fructose-2,6-bisphosphatase activity involving a phosphoprotein intermediate. Like mammalian bifunctional enzymes, the His-404 mutant protein is readily phosphorylated by fructose 2,6-P2 with a half-saturation of 0.4 microM, the same Km value as for its fructose-2,6-bisphosphatase activity. Protein phosphorylation by the C-subunit of cAMP-dependent protein kinase, presumably at a C-terminal consensus site, increases the Km value to 1.5 microM. The newly created fructose-2,6-bisphosphatase is inhibited competitively by its product fructose 6-P with a K(i) of 0.6 mM. No effect of the His-404 mutation was found on 6-phosphofructo-2-kinase activity, in line with the mutant yeast enzyme having independent kinase and phosphatase domains, like its mammalian wild-type counterparts. The results would fit with the evolution of the PFK26 gene having involved fusion between kinase and phosphatase genes--as proposed for the mammalian enzyme--but with accompanying or later silencing of the fructose-2,6-bisphosphatase activity."xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00092a025"xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/author | "Kretschmer M."xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/author | "Langer C."xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/author | "Prinz W."xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/pages | "11143-11148"xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/title | "Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase."xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://purl.uniprot.org/core/volume | "32"xsd:string |
| http://purl.uniprot.org/citations/8218176 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8218176 |
| http://purl.uniprot.org/citations/8218176 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8218176 |
| http://purl.uniprot.org/uniprot/#_P40433-mappedCitation-8218176 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8218176 |
| http://purl.uniprot.org/uniprot/#_Q12471-mappedCitation-8218176 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8218176 |
| http://purl.uniprot.org/uniprot/P40433 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8218176 |
| http://purl.uniprot.org/uniprot/Q12471 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8218176 |