Literature summary for 3.1.3.11 extracted from

Hines, J.K.; Fromm, H.J.; Honzatko, R.B.
Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase (2006), J. Biol. Chem., 281, 18386-18393.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	mechanism of activation involves binding of anionic ligands which bind to allosteric activation sites, which in turn stabilize a tetramer and a polypeptide fold that obstructs AMP binding	Escherichia coli
phosphoenolpyruvate	up to 300% activation	Escherichia coli
sulfate	up to 300% activation	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A993	-	-

Subunits

Subunits	Comment	Organism
tetramer	crystallization data, enzyme is in a quarternary state between canonical R- and T-state of Sus scrofa enzyme	Escherichia coli

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Release 2023.1 (January 2023)