{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:02:50Z","timestamp":1773658970156,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1989,8,15]]},"abstract":"<jats:p>The two activities of chicken liver 6-phosphofructo-2-kinase\/fructose-2,6-bisphosphatase were inactivated by o-phthalaldehyde. Absorbance and fluorescence spectra of the modified enzyme were consistent with the formation of an isoindole derivative (1 mol\/mol of enzyme subunit). The inactivation of 6-phosphofructo-2-kinase by o-phthalaldehyde was faster than the inactivation of fructose-2,6-bisphosphatase, which was concomitant with the increase in fluorescence. The substrates of 6-phosphofructo-2-kinase did not protect the kinase against inactivation, whereas fructose-2,6-bisphosphate fully protected against o-phthalaldehyde-induced inactivation of the bisphosphatase. Addition of dithiothreitol prevented both the increase in fluorescence and the inactivation of fructose-2,6-bisphosphatase, but not that of 6-phosphofructo-2-kinase. It is proposed that o-phthalaldehyde forms two different inhibitory adducts: a non-fluorescent adduct in the kinase domain and a fluorescent isoindole derivative in the bisphosphatase domain. A lysine and a cysteine residue could be involved in fructose-2,6-bisphosphate binding in the bisphosphatase domain of the protein.<\/jats:p>","DOI":"10.1042\/bj2620097","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:14:08Z","timestamp":1439241248000},"page":"97-102","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Inactivation of liver 6-phosphofructo-2-kinase\/fructose-2,6-bisphosphatase by <i>o<\/i>-phthalaldehyde"],"prefix":"10.1042","volume":"262","author":[{"given":"M H","family":"Rider","sequence":"first","affiliation":[{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and Institute of Cellular and Molecular Pathology, UCL 7529, avenue Hippocrate 75, B-1200 Brussels, Belgium."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L","family":"Hue","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, University of Louvain Medical School, and Institute of Cellular and Molecular Pathology, UCL 7529, avenue Hippocrate 75, B-1200 Brussels, Belgium."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/262\/1\/97\/597577\/bj2620097.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/262\/1\/97\/597577\/bj2620097.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:31:10Z","timestamp":1637865070000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/262\/1\/97\/26149\/Inactivation-of-liver-6-phosphofructo-2-kinase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,8,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1989,8,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2620097","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,8,15]]}}}