| http://purl.uniprot.org/citations/9032446 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9032446 | http://www.w3.org/2000/01/rdf-schema#comment | "In a structural model of the 2-kinase domain of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase based on the analogy with adenylate kinase, Lys-174, Asp-179 and Asp-191 residues are located in the putative active site. Asp-179 and Asp-191 are conserved in all known 6-phosphofructo-2-kinase sequences. In contrast, Lys-174 is conserved except in a yeast isoenzyme, fbp26, where it is replaced by glycine. Yeast fbp26 possesses fructose-2,6-bisphosphatase activity, but is devoid of 6-phosphofructo-2-kinase activity. Mutation of Asp-179 and Asp-191 of the rat liver isoenzyme to alanine increased the Km of 6-phosphofructo-2-kinase for fructose 6-phosphate 2000- and 1000-fold respectively, whereas mutation of Lys-174 to glycine decreased the Vmax of 6-phosphofructo-2-kinase more than 4000-fold. In contrast, none of the mutations affected the kinetic parameters of fructose-2,6-bisphosphatase. CD and fluorescence measurements indicated that the mutations had no effect on the structure and stability of the recombinant proteins. The results show that Asp-179 and Asp-191 participate in fructose 6-phosphate binding, whereas Lys-174 is important for catalysis. Therefore the natural mutation of Lys-174 to glycine in the fbp26 yeast isoenzyme could explain the lack of 6-phosphofructo-2-kinase activity. These results support a novel 6-phosphofructo-2-kinase structure model based on adenylate kinase."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3210623"xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Rider M.H."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Di Pietro A."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Vertommen D."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Bertrand L."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Deprez J."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/author | "Hue L."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/pages | "623-627"xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/title | "Site-directed mutagenesis of Lys-174, Asp-179 and Asp-191 in the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://purl.uniprot.org/core/volume | "321"xsd:string |
| http://purl.uniprot.org/citations/9032446 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9032446 |
| http://purl.uniprot.org/citations/9032446 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9032446 |
| http://purl.uniprot.org/uniprot/#_P32604-mappedCitation-9032446 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9032446 |
| http://purl.uniprot.org/uniprot/P32604 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/9032446 |