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Literature summary for 3.1.3.46 extracted from

  • Langer, S.; Kaminski, M.T.; Lenzen, S.; Baltrusch, S.
    Endogenous activation of glucokinase by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is glucose dependent (2010), Mol. Endocrinol., 24, 1988-1997.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of PFK-2/FBPase-2 in MIN6 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information overexpression of PFK-2/FBPase-2 in MIN6 cells results in increased insulin secretion Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase Rattus norvegicus ?
-
?

Synonyms

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

General Information

General Information Comment Organism
metabolism analysis of glucokinase/6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase complex formation, binding and activation of GK by PFK-2/FBPase-2 in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion Rattus norvegicus
physiological function the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase acts as an endogenous glucokinase activator Rattus norvegicus