6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2gene.[1]
The protein encoded by this gene is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. The encoded protein has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. Two transcript variants encoding two different isoforms have been found for this gene.[1]
Hilliker CE, Darville MI, Aly MS, et al. (1991). "Human and rat chromosomal localization of two genes for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by analysis of somatic cell hybrids and in situ hybridization". Genomics. 10 (4): 867–73. doi:10.1016/0888-7543(91)90174-D. PMID1655632.
Goldmuntz EA, Remmers EF, Zha H, et al. (1994). "Genetic map of seven polymorphic markers comprising a single linkage group on rat chromosome 5". Mamm. Genome. 4 (11): 670–5. doi:10.1007/BF00360905. PMID7904197.
Hirata T, Kato M, Okamura N, et al. (1998). "Expression of human placental-type 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase in various cells and cell lines". Biochem. Biophys. Res. Commun. 242 (3): 680–4. doi:10.1006/bbrc.1997.8024. PMID9464277.
Heine-Suñer D, Díaz-Guillén MA, Lange AJ, Rodríguez de Córdoba S (1998). "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)". Eur. J. Biochem. 254 (1): 103–10. doi:10.1046/j.1432-1327.1998.2540103.x. PMID9652401.
Hirata T, Watanabe M, Miura S, et al. (2001). "Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues". Biosci. Biotechnol. Biochem. 64 (10): 2047–52. doi:10.1271/bbb.64.2047. PMID11129574.
Kessler R, Eschrich K (2001). "Splice isoforms of ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in human brain". Brain Res. Mol. Brain Res. 87 (2): 190–5. doi:10.1016/S0169-328X(01)00014-6. PMID11245921.
Soejima H, Kawamoto S, Akai J, et al. (2001). "Isolation of novel heart-specific genes using the BodyMap database". Genomics. 74 (1): 115–20. doi:10.1006/geno.2001.6527. PMID11374908.
Baltrusch S, Lenzen S, Okar DA, et al. (2001). "Characterization of glucokinase-binding protein epitopes by a phage-displayed peptide library. Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel interaction partner". J. Biol. Chem. 276 (47): 43915–23. doi:10.1074/jbc.M105470200. PMID11522786.
Marsin AS, Bouzin C, Bertrand L, Hue L (2002). "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase". J. Biol. Chem. 277 (34): 30778–83. doi:10.1074/jbc.M205213200. PMID12065600.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID15324660.