Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
gene FBP1, recombinant expression in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
crystals are obtained in a micro-batch setup by mixing 0.5 ml volumes of 22.5 mg/ml enzyme in 10 mM potassium/sodium phosphate pH 7.4, 2 mM MnCl2, 5 mM MgCl2, 2 mM ZnCl2, 0.5 mM fructose-2,6-bisphosphate with reservoir solution consisting of 0.1 M Tris-HCl pH 8.5, 2 M ammonium sulfate. Crystal structure of human liver enzyme in the R-state conformation is presented, determined at a resolution of 2.2 A | Homo sapiens |
purified liver FBPase in the R-state conformation, micro-batch method, mixing of 500 nl of 22.5 mg/ml protein in 10 mM potassium/sodium phosphate, pH 7.4, 2 mM MnCl2, 5 mM MgCl2, 2 mM ZnCl2, and 0.5 mM fructose 2,6-bisphosphate, with 500 nl of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, and 2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.2 A resolution. Self-Patterson function analysis and various intensity statistics revealed the presence of pseudo-translation and the absence of twinning | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | - |
Homo sapiens | |
D-fructose 2,6-bisphosphate | - |
Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate + H2O | Homo sapiens | - |
D-fructose 6-phosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09467 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
recombinant FBPase 1 from Escherichia coli strain BL21(DE3) by anion and cation exchange chromatography, gel filtration, and dialysis | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate + H2O | - |
Homo sapiens | D-fructose 6-phosphate + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 37000, FBPase is a homotetramer of 222 (D2) symmetry with a major and a minor dimer interface. The dimers connected via the minor interface can rotate with respect to each other, leading to the inactive T-state and active R-state conformations of FBPase. The subunits are labelled C1-C4 and form two functional dimers: C1/C2 and C3/C4. The active site of the C1 subunit is near the C1/C2 interface, while its AMP binding site is near the C1/C4 interface. The C1/C2 and C3/C4 dimers can rotate with respect to each other. Three-dimensional structure analysis, detailed overview. The apoenzyme adopts the active R state | Homo sapiens |
homotetramer | of 222 symmetry with a major and a minor dimer interface. The dimers connected via the minor interface can rotate with respect to each other, leading to the inactive T-state and active R-state conformations | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
FBP1 | - |
Homo sapiens |
FBPase | - |
Homo sapiens |
FBPase 1 | - |
Homo sapiens |
fructose-1,6-bisphosphatase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
drug target | potential drug target for type 2 diabetes | Homo sapiens |
physiological function | fructose 1,6-bisphosphatase (FBPase) is a major control point in gluconeogenesis, catalyzing the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. This step in gluconeogenesis is synergistically downregulated by fructose 2,6-bisphosphate and AMP, which bind to the active site and an allosteric site of FBPase, respectively | Homo sapiens |
physiological function | key regulator of gluconeogenesis | Homo sapiens |