Biology:PFKFB2

Generic protein structure example

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene.

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.

Interactions

PFKFB2 has been shown to interact with YWHAQ.

Further reading

• "The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing.". Biochem. J. 285 (2): 405–11. 1992. doi:10.1042/bj2850405. PMID 1322130. 
• "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. 1991. doi:10.1016/0888-7543(91)90174-D. PMID 1655632. 
• "Genetic map of seven polymorphic markers comprising a single linkage group on rat chromosome 5.". Mamm. Genome 4 (11): 670–5. 1994. doi:10.1007/BF00360905. PMID 7904197. https://zenodo.org/record/1232430. 
• "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. 1998. doi:10.1006/bbrc.1997.8024. PMID 9464277. 
• "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. 1998. doi:10.1046/j.1432-1327.1998.2540103.x. PMID 9652401. 
• "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. 2001. doi:10.1271/bbb.64.2047. PMID 11129574. 
• "Splice isoforms of ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in human brain.". Brain Res. Mol. Brain Res. 87 (2): 190–5. 2001. doi:10.1016/S0169-328X(01)00014-6. PMID 11245921. 
• "Isolation of novel heart-specific genes using the BodyMap database.". Genomics 74 (1): 115–20. 2001. doi:10.1006/geno.2001.6527. PMID 11374908. 
• "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. 2001. doi:10.1074/jbc.M105470200. PMID 11522786. 
• "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. 2002. doi:10.1074/jbc.M205213200. PMID 12065600. 
• "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase.". EMBO J. 22 (14): 3514–23. 2003. doi:10.1093/emboj/cdg363. PMID 12853467. 
• "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039. 
• "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. 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. 2006. doi:10.1038/nature04727. PMID 16710414. Bibcode: 2006Natur.441..315G. 

{{Navbox

| name = Glycolysis enzymes
| title = Metabolism: carbohydrate metabolism: [[Biology:Glycoglycolysis/gluconeogenesis enzymes
| state = autocollapse
| listclass = hlist

| group1 = Glycolysis

| list1 =

Hexokinase (HK1, HK2, HK3, Glucokinase)→/Glucose 6-phosphatase← Glucose isomerase Phosphofructokinase 1 (Liver, Muscle, Platelet)→/Fructose 1,6-bisphosphatase←

Fructose-bisphosphate aldolase (Aldolase A, B, C) Triosephosphate isomerase

Glyceraldehyde 3-phosphate dehydrogenase Phosphoglycerate kinase Phosphoglycerate mutase Enolase Pyruvate kinase (PKLR, PKM2)

| group2 = Gluconeogenesis only

| list2 =

to oxaloacetate:	Pyruvate carboxylase Phosphoenolpyruvate carboxykinase
from lactate (Cori cycle):	Lactate dehydrogenase
from alanine (Alanine cycle):	Alanine transaminase
from glycerol:	Glycerol kinase Glycerol dehydrogenase

| group4 = Regulatory
| list4 =

• fructose 2,6-bisphosphatase
  • PFKFB1, PFKFB2, PFKFB3, PFKFB4
• Bisphosphoglycerate mutase

}}