Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.105 extracted from

  • Ros, S.; Floeter, J.; Kaymak, I.; Da Costa, C.; Houddane, A.; Dubuis, S.; Griffiths, B.; Mitter, R.; Walz, S.; Blake, S.; Behrens, A.; Brindle, K.M.; Zamboni, N.; Rider, M.H.; Schulze, A.
    6-Phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 is essential for p53-null cancer cells (2017), Oncogene, 36, 3287-3299 .
    View publication on PubMed
Search for more literature for 2.7.1.105

Application

Application Comment Organism
medicine tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of the allosteric regulator fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuated cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16877 isoform PFKFB4, bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, EC 2.7.1.105 and EC 3.1.3.46, respectively
-

Source Tissue

Source Tissue Comment Organism Textmining
HCT-116 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
PFKFB4
-
 Homo sapiens

Expression

Organism Comment Expression
Homo sapiens p53 downregulates PFKFB4 expression by binding to its promoter and mediating transcriptional repression via histone deacetylases down

General Information

General Information Comment Organism
physiological function tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuates cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth Homo sapiens