{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T22:55:23Z","timestamp":1771628123966,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1997,2,1]]},"abstract":"<jats:p>Simultaneous multiple alignment of available sequences of the bifunctional enzyme 6-phosphofructo-2-kinase\/fructose-2,6-bisphosphatase revealed several segments of conserved residues in the 2-kinase domain. The sequence of the kinase domain was also compared with proteins of known three-dimensional structure. No similarity was found between the kinase domain of 6-phosphofructo-2-kinase and 6-phosphofructo-1-kinase. This questions the modelling of the 2-kinase domain on bacterial 6-phosphofructo-1-kinase that has previously been proposed [Bazan, Fletterick and Pilkis (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 9642\u01509646]. However, sequence similarities were found between the 2-kinase domain and several nucleotide-binding proteins, the most similar being adenylate kinase. A structural model of the 2-kinase domain based on adenylate kinase is proposed. It accommodates all the results of site-directed mutagenesis studies carried out to date on residues in the 2-kinase domain. It also allows residues potentially involved in catalysis and\/or substrate binding to be predicted.<\/jats:p>","DOI":"10.1042\/bj3210615","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:52:36Z","timestamp":1439243556000},"page":"615-621","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Modelling the 2-kinase domain of 6-phosphofructo-2-kinase\/fructose-2,6-bisphosphatase on adenylate kinase"],"prefix":"10.1042","volume":"321","author":[{"given":"Luc","family":"BERTRAND","sequence":"first","affiliation":[{"name":"Facult\u00e9s Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium"},{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Didier","family":"VERTOMMEN","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric","family":"DEPIEREUX","sequence":"additional","affiliation":[{"name":"Facult\u00e9s Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Louis","family":"HUE","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark H.","family":"RIDER","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ernest","family":"FEYTMANS","sequence":"additional","affiliation":[{"name":"Facult\u00e9s Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/321\/3\/615\/623615\/bj3210615.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/321\/3\/615\/623615\/bj3210615.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:35:10Z","timestamp":1637714110000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/321\/3\/615\/34118\/Modelling-the-2-kinase-domain-of-6-phosphofructo-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,2,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1997,2,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3210615","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,2,1]]}}}