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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1; 6PF-2-K/fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/fru-2,6-P2ase liver isozyme; includes: 6-phosphofructo-2-kinase; fructose-2,6-bisphosphatase (PFKFB1, F6PK PFRX)

Function: - dual function phosphomonoesterase - synthesis & degradation of fructose-2,6-bisphosphate - phosphorylation results in inhibition of kinase activity ATP + D-fructose-6-phosphate -> ADP + D-fructose-2,6-bisphosphate D-fructose-2,6-bisphosphate + H2O -> D-fructose-6-phosphate + phosphate Structure: - homodimer - in the C-terminal section; belongs to the phosphoglycerate mutase family Expression: liver

General

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase (6PF-2-K/Fru-2,6-Pase) allosteric enzyme oligomerizing protein

Properties

SIZE: entity length = 471 aa MW = 55 kD COMPARTMENT: cytoplasm MOTIF: 6-phosphofructo-2-kinase {1-250} MOTIF: Ser phosphorylation site {S33} ATP-binding site NAME: ATP-binding site SITE: 49-56 binding site SITE: 105-105 FOR-BINDING-OF: fructose-6-phosphate aspartate residue {D131} cysteine residue {C161} binding site SITE: 196-196 FOR-BINDING-OF: fructose-6-phosphate Fructose-2,6-bisphosphatase {251-471} MOTIF: histidine residue {H259} glutamate residue {E328} histidine residue {H393}

Database Correlations

OMIM 311790 UniProt P16118 PFAM correlations Entrez Gene 5207 KEGG correlations ENZYME correlations

References

  1. UniProt :accession P16118
  2. Stryer Biochemistry WH Freeman & Co, New York, 1988 pg 443