Literature summary for 3.1.3.11 extracted from

Hines, J.K.; Kruesel, C.E.; Fromm, H.J.; Honzatko, R.B.
Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch (2007), J. Biol. Chem., 282, 24697-24706.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of AMP/glucose 6-phosphate/enzyme complexes are grown by hanging drop in vapor diffusion	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to AMP. Glc-6-P and AMP are synergistic inhibitors	Escherichia coli
D-glucose 6-phosphate	allosteric inhibition. FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to glucose 6-phosphate. Glc-6-P and AMP are synergistic inhibitors	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A993	-	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)