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The bifunctional 6-phosphofructo-2-kinase ({{EC number|2.7.1.105}})/fructose-2,6-bisphosphatase ({{EC number|3.1.3.46}}) (PFKFB) regulates the steady-state concentration of [[fructose 2,6-bisphosphate]], an activator of a key regulatory enzyme of [[glycolysis]], [[phosphofructokinase]].
The bifunctional 6-phosphofructo-2-kinase ({{EC number|2.7.1.105}})/fructose-2,6-bisphosphatase ({{EC number|3.1.3.46}}) (PFKFB) regulates the steady-state concentration of [[fructose 2,6-bisphosphate]], an activator of a key regulatory enzyme of [[glycolysis]], [[phosphofructokinase]].
Latest research made by scientists at Cancer Research UK’s London Research Institute show that an enzyme called PFKFB4 is essential for balancing these two processes – making sure the cell’s energy needs are met without allowing free radicals to build up and trigger cell death.
Study leader Dr. Almut Schulze, said: “Our study suggests that PFKFB4 acts to fine tune the process by which cells convert glucose into energy. Blocking this enzyme in prostate cancer cells grown in the lab stalled growth and triggered a catastrophic build-up of free-radicals, suggesting that it could be a suitable drug target. Importantly, this route to energy production is common to many different types of cancer, suggesting that drugs to target it could potentially be used to treat a variety of cancers.”


== References ==
== References ==

Revision as of 09:10, 26 March 2012

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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 also known as PFKFB4 is a enzyme which in humans is encoded by the PFKFB4 gene.[1][2]

Function

The bifunctional 6-phosphofructo-2-kinase (EC 2.7.1.105)/fructose-2,6-bisphosphatase (EC 3.1.3.46) (PFKFB) regulates the steady-state concentration of fructose 2,6-bisphosphate, an activator of a key regulatory enzyme of glycolysis, phosphofructokinase. Latest research made by scientists at Cancer Research UK’s London Research Institute show that an enzyme called PFKFB4 is essential for balancing these two processes – making sure the cell’s energy needs are met without allowing free radicals to build up and trigger cell death. Study leader Dr. Almut Schulze, said: “Our study suggests that PFKFB4 acts to fine tune the process by which cells convert glucose into energy. Blocking this enzyme in prostate cancer cells grown in the lab stalled growth and triggered a catastrophic build-up of free-radicals, suggesting that it could be a suitable drug target. Importantly, this route to energy production is common to many different types of cancer, suggesting that drugs to target it could potentially be used to treat a variety of cancers.”

References

  1. ^ Sakai A, Kato M, Fukasawa M, Ishiguro M, Furuya E, Sakakibara R (1996). "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta". J. Biochem. 119 (3): 506–11. PMID 8830046. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Manzano A, Pérez JX, Nadal M, Estivill X, Lange A, Bartrons R (1999). "Cloning, expression and chromosomal localization of a human testis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene". Gene. 229 (1–2): 83–9. doi:10.1016/S0378-1119(99)00037-2. PMID 10095107. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

Further reading