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| {{enzyme
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| | Name = 6-phosphofructo-2-kinase
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| | EC_number = 2.7.1.105
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| | CAS_number = 78689-77-7
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| | IUBMB_EC_number = 2/7/1/105
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| | GO_code = 0003873
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| | image =
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| | width =
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| | caption =
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| }}
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| {{Infobox protein family
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| | Symbol = 6PF2K
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| | Name = 6PF2K
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| | image = PDB 1k6m EBI.jpg
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| | width =
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| | caption = crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
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| | Pfam = PF01591
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| | Pfam_clan = CL0023
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| | InterPro = IPR013079
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| | SMART =
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| | PROSITE = PDOC00158
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| | MEROPS =
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| | SCOP = 1bif
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| | TCDB =
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| | OPM family =
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| | OPM protein =
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| | CAZy =
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| | CDD =
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| }}
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| In [[enzymology]], a '''6-phosphofructo-2-kinase''' ({{EC number|2.7.1.105}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] | |
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| :ATP + beta-D-fructose 6-phosphate <math>\rightleftharpoons</math> ADP + beta-D-fructose 2,6-bisphosphate | |
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[beta-D-fructose 6-phosphate]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[beta-D-fructose 2,6-bisphosphate]].
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| This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing groups ([[phosphotransferase]]s) with an alcohol group as acceptor. 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 metabolism|fructose]] and [[Mannose metabolism|mannose metabolism]]. The enzyme is important in the [[regulation]] of [[liver|hepatic]] [[carbohydrate]] [[metabolism#Regulation_and_control|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 (biology)|tissue]] distribution and [[enzyme|enzymatic]] activity.<ref name="pmid9652401">{{cite journal | author = Heine-Suñer D, DÃaz-Guillén MA, Lange AJ, RodrÃguez de Córdoba S | title = Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2) | journal = Eur. J. Biochem. | volume = 254 | issue = 1 | pages = 103–10 |date=May 1998 | pmid = 9652401 | doi = 10.1046/j.1432-1327.1998.2540103.x| url = }}</ref> The [[family (biology)|family]] described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little [[sequence (biology)|sequence]] similarity, although a few [[residue (chemistry)|residues]] seem key to their interaction with [[fructose 6-phosphate]].<ref name="pmid9753654">{{cite journal | author = Wang X, Deng Z, Kemp RG | title = An essential methionine residue involved in substrate binding by phosphofructokinases | journal = Biochem. Biophys. Res. Commun. | volume = 250 | issue = 2 | pages = 466–8 |date=September 1998 | pmid = 9753654 | doi = 10.1006/bbrc.1998.9311 | url = }}</ref>
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| ==Structural studies==
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| As of late 2007, 8 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1BIF}}, {{PDB link|1K6M}}, {{PDB link|2AXN}}, {{PDB link|2BIF}}, {{PDB link|2DWO}}, {{PDB link|2DWP}}, {{PDB link|2I1V}}, and {{PDB link|3BIF}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Van Schaftingen E, Hers HG | year = 1981 | title = Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP | journal = Biochem. Biophys. Res. Commun. | volume = 101 | pages = 1078–84 | pmid = 6458291 | doi = 10.1016/0006-291X(81)91859-3 | issue = 3 }}
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| {{InterPro content|IPR013079}}
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| [[Category:Protein domains]]
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| [[Category:EC 2.7.1]]
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| [[Category:Enzymes of known structure]]
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| {{enzyme-stub}}
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