Fructose‐2,6‐bisphosphate and control of carbohydrate metabolism in eukaryotes

  title={Fructose‐2,6‐bisphosphate and control of carbohydrate metabolism in eukaryotes},
  author={David A. Okar and Alex J. Lange},
Fructose‐2,6‐bisphosphate is an important intracellular biofactor in the control of carbohydrate metabolic fluxes in eukaryotes. It is generated from ATP and fructose‐6‐phosphate by 6‐phosphofructo‐2‐kinase and degraded to fructose‐6‐phosphate and phosphate ion by fructose‐2,6‐bisphosphatase. In most organisms these enzymatic activities are contained in a single polypeptide. The reciprocal modulation of the kinase and bisphosphatase activities by post‐translational modifications places the… 

Altered fructose-2,6-bisphosphatase levels cause phenotypic changes and shift development in plants

Transgenic plants are produced with altered F2,6P2 levels that are known to be developmentally sensitive to the elevated or decreased amounts of the available sucrose to hipothetized that the detection of phenotypic changes and developmental differences can be realistic applying a highly standardized sampling procedure.

Effects of Altered Fructose 2,6-Bisphosphate Levels on Carbohydrate Metabolism in Carnation

Transgenic plants harboring two modified bifunctional enzyme complementary DNAs of rat liver origin (6-phosphofructo-2-kinase/fructose 2,6-biphosphatase) were generated and altered the key enzyme activities of sucrose and starch metabolism.

6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase and tumor cell glycolysis

  • J. Chesney
  • Biology
    Current opinion in clinical nutrition and metabolic care
  • 2006
Findings demonstrate a key role for the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases in neoplastic transformation and provide rationale for the development of agents that selectively inhibit the PFKFB3 enzyme as antineoplastic agents.

Lack of fructose 2,6-bisphosphate compromises photosynthesis and growth in Arabidopsis in fluctuating environments.

It is suggested that the capacity of Fru-2,6-P2 to modulate partitioning of photoassimilate is an important determinant of growth and fitness in natural environments.

Balancing glycolytic flux: the role of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatases in cancer metabolism

The current understanding of the role of PFKFB proteins in the control of cancer metabolism is reviewed and the emerging interest in these enzymes as potential targets for the development of antineoplastic agents is discussed.

The role of 6-phosphofructo-2-kinase (PFK-2)/fructose 2,6-bisphosphatase (FBPase-2) in metabolic reprogramming of cancer cells.

Many studies have reported a correlation between aberrant PFKFB expression level and the grade of tumour aggressiveness, which directly indicates that these enzymes may play a crucial role in cancerogenesis.

Dual role of phosphofructokinase-2/fructose bisphosphatase-2 in regulating the compartmentation and expression of glucokinase in hepatocytes.

It is concluded that PFK2 has a dual role in regulating glucokinase in hepatocytes: it potentiates glucokin enzyme protein expression by posttranscriptional mechanisms and favors its cytoplasmic compartmentation.

Ras transformation requires metabolic control by 6-phosphofructo-2-kinase

Data indicate that the PFKFB3 protein product may serve as an essential downstream metabolic mediator of oncogenic ras, and it is proposed that pharmacologic inhibition of this enzyme should selectively suppress the high rate of glycolysis and growth by cancer cells.

Physiological relevance of fructose 2,6-bisphosphate in the regulation of spinach leaf pyrophosphate:fructose 6-phosphate 1-phosphotransferase

It was concluded that physiological concentrations of metabolites and Pi increase the Ka of PFP for Fru-2,6-P2 to values approaching the concentration of the activator in vivo, and changes in cytosolic PFP levels could appreciably alter the activation state of P FP in vivo.



Reversible unfolding of fructose 6‐phosphate, 2‐kinase:fructose 2,6‐bisphosphatase

Reversible unfolding of rat testis fructose 6‐phosphate, 2‐kinase:fructose 2,6‐bisphosphatase in guanidine hydrochloride and fluorescence quenching studies showed that the tryptophans, including Trp‐15 in the N‐terminal peptide, were only slightly accessible to iodide but were much more accessible to acrylamide.

Cloning of a second gene encoding 6‐phosphofructo‐2‐kinase in yeast, and characterization of mutant strains without fructose‐2,6‐bisphosphate

Fructose‐2,6‐bisphosphate is an important effector in vivo of the 6‐phosphofructo‐1‐kinase/fructose‐1,6-bisphospha‐tase enzyme pair, and is involved in the initiation of glycolysis during the transition to a fermentative mode of metabolism, but can be effectively replaced by other effectors and regulatory mechanisms during growth on glucose.

Role of fructose 2,6-bisphosphate in the control of heart glycolysis.

A special fructose bisphosphate functions as a cytoplasmic regulatory metabolite in green leaves.

The results suggest that Fru-2,6-P(2) functions in the regulation of glycolysis and gluconeogenesis (carbohydrate synthesis) in the cytoplasm of leaves of C(3) plants.

Mutant studies of phosphofructo-2-kinases do not reveal an essential role of fructose-2,6-bisphosphate in the regulation of carbon fluxes in yeast cells.

F2,6bP is not needed to sustain an adequate glycolytic flux under fermentative conditions, but rather is concerned with the homeostasis of metabolite concentrations and fails to indicate a physiological significance for inhibition of fructose-1,6-bisphosphatase by F2, 6bP.