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Literature summary for 3.1.3.46 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
Search for more literature for 3.1.3.46

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme is phosphorylated at Ser-32 which causes enhancement of the bisphosphatase activity Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
COS cell
-
 Rattus norvegicus
-
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer 2 * 50000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
-
 Rattus norvegicus
PFK-2/FBPase-2
-
 Rattus norvegicus