Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.105 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
-
Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information engineering of the LKVWT glucokinase-binding motif in the FBPase-2 domain of islet PFK-2/FBPase-2 to HKEWR leads to significantly lower interaction with glucokinase compared with wild-type at 25 mmol/liter glucose Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreatic islet
-
Rattus norvegicus
-

General Information

General Information Comment Organism
physiological function enzyme acts as an endogenous glucokinase activator. Binding and activation of glucokinase by bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 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