Cloned (Comment) | Organism |
---|---|
recombinant expression of GST-tagged liver enzyme in Escherichia coli strain BL21(DE3) | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | - |
Rattus norvegicus | |
fructose-1,6-bisphosphate | at higher concentrations | Rattus norvegicus | |
fructose-2,6-bisphosphate | - |
Rattus norvegicus | |
fructose-6-phosphate | - |
Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | in absence of glucose | Rattus norvegicus | 5737 | - |
nucleus | when the cells are incubated with 25 mM glucose, the enzyme changes its cellular localization, FBPase-1 becomes more concentrated in the nucleus, but the enzyme still shows an important co-localization in the cellular periphery. In presence of 25 mM glucose and 100 nM insulin, FBPase-1 mainly translocates from cytoplasm to the nucleus | Rattus norvegicus | 5634 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates | Rattus norvegicus | |
Mg2+ | activates | Rattus norvegicus | |
Mn2+ | activates | Rattus norvegicus | |
Zn2+ | activates | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36000 | - |
gel filtration | Rattus norvegicus |
36000 | - |
gel filtration, recombinant enzyme | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate + H2O | Rattus norvegicus | - |
D-fructose 6-phosphate + phosphate | - |
? | |
D-fructose 1,6-bisphosphate + H2O | Rattus norvegicus Wistar | - |
D-fructose 6-phosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P19112 | - |
- |
Rattus norvegicus Wistar | P19112 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Rattus norvegicus |
recombinant GST-tagged liver enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hepatocyte | - |
Rattus norvegicus | - |
liver | - |
Rattus norvegicus | - |
additional information | coexpression of aldolase B and FBPase-1 in cultured cells | Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate + H2O | - |
Rattus norvegicus | D-fructose 6-phosphate + phosphate | - |
? | |
D-fructose 1,6-bisphosphate + H2O | - |
Rattus norvegicus Wistar | D-fructose 6-phosphate + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 36000, recombinant enzyme, SDS-PAGE | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
FBPase-1 | - |
Rattus norvegicus |
fructose-1,6-bisphosphatase | - |
Rattus norvegicus |
fructose-1,6-bisphosphatase-1 | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
drug target | the enzyme (FBPase-1) is considered to be a new target for the control of diabetes | Rattus norvegicus |
metabolism | metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes | Rattus norvegicus |
physiological function | fructose-1,6-bisphosphatase is a highly regulated key enzyme in gluconeogenesis and glyconeogenesis (glycogen synthesis from gluconeogenic precursors). The enzyme catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and phosphate in the presence of divalent metal cations. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver FBPase-1 shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate | Rattus norvegicus |