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Literature summary extracted from

  • Langer, S.; Okar, D.A.; Schultz, J.; Lenzen, S.; Baltrusch, S.
    Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation (2012), FEBS Lett., 586, 1419-1425.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 S32A/H258A mutant unable to be phosphorylated Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.46 50000
-
2 * 50000, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O Rattus norvegicus
-
D-fructose 6-phosphate + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Rattus norvegicus P07953 bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
3.1.3.46 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.105 phosphoprotein forskolin induces a 40% increase in phosphorylation at residue Ser32. The enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex Rattus norvegicus
3.1.3.46 phosphoprotein the enzyme is phosphorylated at Ser-32 which causes enhancement of the bisphosphatase activity Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 liver
-
Rattus norvegicus
-
3.1.3.46 COS cell
-
Rattus norvegicus
-
3.1.3.46 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O
-
Rattus norvegicus D-fructose 6-phosphate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.7.1.105 More the enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex Rattus norvegicus
3.1.3.46 homodimer 2 * 50000, SDS-PAGE Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.105 PFKFB1
-
Rattus norvegicus
3.1.3.46 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
Rattus norvegicus
3.1.3.46 PFK-2/FBPase-2
-
Rattus norvegicus