{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T17:48:22Z","timestamp":1791395302563,"version":"4.3.3"},"reference-count":208,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2004,8,1]]},"abstract":"<jats:p>Fru-2,6-P2 (fructose 2,6-bisphosphate) is a signal molecule that controls glycolysis. Since its discovery more than 20\u00a0years ago, inroads have been made towards the understanding of the structure\u2013function relationships in PFK-2 (6-phosphofructo-2-kinase)\/FBPase-2 (fructose-2,6-bisphosphatase), the homodimeric bifunctional enzyme that catalyses the synthesis and degradation of Fru-2,6-P2. The FBPase-2 domain of the enzyme subunit bears sequence, mechanistic and structural similarity to the histidine phosphatase family of enzymes. The PFK-2 domain was originally thought to resemble bacterial PFK-1 (6-phosphofructo-1-kinase), but this proved not to be correct. Molecular modelling of the PFK-2 domain revealed that, instead, it has the same fold as adenylate kinase. This was confirmed by X-ray crystallography. A PFK-2\/FBPase-2 sequence in the genome of one prokaryote, the proteobacterium Desulfovibrio desulfuricans, could be the result of horizontal gene transfer from a eukaryote distantly related to all other organisms, possibly a protist. This, together with the presence of PFK-2\/FBPase-2 genes in trypanosomatids (albeit with possibly only one of the domains active), indicates that fusion of genes initially coding for separate PFK-2 and FBPase-2 domains might have occurred early in evolution. In the enzyme homodimer, the PFK-2 domains come together in a head-to-head like fashion, whereas the FBPase-2 domains can function as monomers. There are four PFK-2\/FBPase-2 isoenzymes in mammals, each coded by a different gene that expresses several isoforms of each isoenzyme. In these genes, regulatory sequences have been identified which account for their long-term control by hormones and tissue-specific transcription factors. One of these, HNF-6 (hepatocyte nuclear factor-6), was discovered in this way. As to short-term control, the liver isoenzyme is phosphorylated at the N-terminus, adjacent to the PFK-2 domain, by PKA (cAMP-dependent protein kinase), leading to PFK-2 inactivation and FBPase-2 activation. In contrast, the heart isoenzyme is phosphorylated at the C-terminus by several protein kinases in different signalling pathways, resulting in PFK-2 activation.<\/jats:p>","DOI":"10.1042\/bj20040752","type":"journal-article","created":{"date-parts":[[2004,7,27]],"date-time":"2004-07-27T05:59:52Z","timestamp":1090907992000},"page":"561-579","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":398,"title":["6-Phosphofructo-2-kinase\/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis"],"prefix":"10.1042","volume":"381","author":[{"given":"Mark\u00a0H.","family":"RIDER","sequence":"first","affiliation":[{"name":"Hormone and Metabolic Research Unit, Universit\u00e9 Catholique de Louvain and Christian de Duve Institute of Cellular Pathology, 75, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luc","family":"BERTRAND","sequence":"additional","affiliation":[{"name":"Division of Cardiology, Universit\u00e9 Catholique de Louvain, 55, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Didier","family":"VERTOMMEN","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, Universit\u00e9 Catholique de Louvain and Christian de Duve Institute of Cellular Pathology, 75, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul\u00a0A.","family":"MICHELS","sequence":"additional","affiliation":[{"name":"Research Unit for Tropical Diseases, Universit\u00e9 Catholique de Louvain and Christian de Duve Institute of Cellular Pathology, 75, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guy\u00a0G.","family":"ROUSSEAU","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, Universit\u00e9 Catholique de Louvain and Christian de Duve Institute of Cellular Pathology, 75, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louis","family":"HUE","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, Universit\u00e9 Catholique de Louvain and Christian de Duve Institute of Cellular Pathology, 75, Avenue Hippocrate, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2004,7,27]]},"reference":[{"key":"2021112214571707200_B1","first-page":"315","article-title":"Fructose 2,6-bisphosphate","volume":"59","author":"Van\u00a0Schaftingen","year":"1987","journal-title":"Adv. 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