Literature summary for 3.1.3.11 extracted from

Barciszewski, J.; Wisniewski, J.; Kolodziejczyk, R.; Jaskolski, M.; Rakus, D.; Dzugaj, A.
T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure (2016), Acta Crystallogr. Sect. D, 72, 536-550 .

Crystallization (Commentary)

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

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

Inhibitors	Comment	Organism
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

Metals/Ions	Comment	Organism	Structure
Mg2+	required	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	O00757	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Source Tissue

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 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
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

Synonyms	Comment	Organism
FBP2	-	Homo sapiens
FBPase	-	Homo sapiens
fructose-1,6-bisphosphatase	-	Homo sapiens

Temperature Stability [°C]

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

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