Crystallization (Comment) | Organism |
---|---|
hanging-drop vapour-diffusion method at 19°C. The R state of mammalian muscle enzyme (FBPase) is significantly different from the corresponding form of the liver isozyme. T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structureMuscle FBPase belongs to the family of proteins containing unstructured, intrinsically disordered elements that adopt a highly ordered structure upon interaction with physiological factors (here after interaction with AMP) | Homo sapiens |
purified muscle FBPase in its active R state, hanging drop vapour diffusion method, mixing of 0.0015 ml of 6 mg/ml protein solution with 0.0015 ml of reservoir solution containing 10 mM Tris buffer pH 7.4, 10 mM MgCl2, 2 M NaCl and 10% v/v PEG 6000, 19°C, 3 months, X-ray diffraction structure determination and analysis at 1.67 A resolution, and purified muscle FBPase in its T state without or with bound AMP, hanging drop vapour diffusion method, mixing of 0.0015 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.0, 2 mM MgCl2, and 0.6 mM AMP, with 0.0015 ml of reservoir solution containing 1.8 M ammonium citrate, 19°C, 3 months, X-ray diffraction structure determination and analysis at 1.84 A and 2.99 A resolution, respectively. Molecular replacement | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | inactive, AMP-associated T state of the enzyme, AMP binding results in improved thermal stability of muscle FBPase | Homo sapiens | |
Ca2+ | - |
Homo sapiens | |
additional information | mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme | Homo sapiens | |
NAD+ | - |
Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | 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 | O00757 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the muscle FBPase FBP2 is also present in cells that predominantly express the liver isozyme FBP1, e.g. in the liver itself | Homo sapiens | - |
muscle | - |
Homo sapiens | - |
muscle | muscle isozyme FBP2 | 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 |
---|---|---|
More | three-dimensional structure analysis of muscle FBPase in its active R state, in the R configuration of muscle FBPase, the C1 subunit has rotated towards the viewer relative to the stationary C3-C4 lower dimer, the three stages of refolding of the N-terminal region of muscle FBPase during the T-to-R transition, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
FBP2 | - |
Homo sapiens |
FBPase | - |
Homo sapiens |
fructose-1,6-bisphosphatase | - |
Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
AMP binding results in improved thermal stability of muscle FBPase | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
metabolism | fructose-1,6-bisphosphatase (FBPase) catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate and is a key enzyme of gluconeogenesis and glyconeogenesis | Homo sapiens |
additional information | the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase | Homo sapiens |
physiological function | the physiological role of muscle FBPase goes beyond its enzymatic function, as this isozyme is localized inside cell nuclei and is shown to interact with mitochondria, where it is involved in regulation of the cell cycle. The behaviour of the muscle isozyme differs greatly from the liver isozyme | Homo sapiens |