6-phosphofructo-2-kinase dimer, Human heart
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
|SCOPe||1bif / SUPFAM|
The systematic name of this enzyme class is ATP:beta-D-fructose-6-phosphate 2-phosphotransferase. Other names in common use include phosphofructokinase 2, 6-phosphofructose 2-kinase, 6-phosphofructo-2-kinase (phosphorylating), fructose 6-phosphate 2-kinase, and ATP:D-fructose-6-phosphate 2-phosphotransferase. This enzyme participates in fructose and mannose metabolism. The enzyme is important in the regulation of hepatic carbohydrate metabolism and is found in greatest quantities in the liver, kidney and heart. In mammals, several genes often encode different isoforms, each of which differs in its tissue distribution and enzymatic activity. The family described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little sequence similarity, although a few residues seem key to their interaction with fructose 6-phosphate.
- Heine-Suñer D, Díaz-Guillén MA, Lange AJ, Rodríguez de Córdoba S (May 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. PMID 9652401.
- Wang X, Deng Z, Kemp RG (September 1998). "An essential methionine residue involved in substrate binding by phosphofructokinases". Biochem. Biophys. Res. Commun. 250 (2): 466–8. doi:10.1006/bbrc.1998.9311. PMID 9753654.
- Van Schaftingen E, Hers HG (1981). "Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP". Biochem. Biophys. Res. Commun. 101 (3): 1078–84. doi:10.1016/0006-291X(81)91859-3. PMID 6458291.
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