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Literature summary for 3.1.3.11 extracted from

  • Ruf, A.; Tetaz, T.; Schott, B.; Joseph, C.; Rudolph, M.
    Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase (2016), Acta Crystallogr. Sect. D, 72, 1212-1224 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens
gene FBP1, recombinant expression in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

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

Inhibitors Comment Organism Structure
AMP
-
Homo sapiens
D-fructose 2,6-bisphosphate
-
Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens P09467
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
Homo sapiens D-fructose 6-phosphate + phosphate
-
?

Subunits

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

Synonyms Comment Organism
FBP1
-
Homo sapiens
FBPase
-
Homo sapiens
FBPase 1
-
Homo sapiens
fructose-1,6-bisphosphatase
-
Homo sapiens

General Information

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