Literature summary for 3.1.3.11 extracted from

Choe, J.Y.; Nelson, S.W.; Arienti, K.L.; Axe, F.U.; Collins, T.L.; Jones, T.K.; Kimmich, R.D.; Newman, M.J.; Norvell, K.; Ripka, W.C.; Romano, S.J.; Short, K.M.; Slee, D.H.; Fromm, H.J.; Honzatko, R.B.
Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors (2003), J. Biol. Chem., 278, 51176-51183.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
OC252 complex of enzyme	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
pseudo-tetrapeptide OC252	the inhibition is synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+ and, uncompetitive with respect to fructose 1,6-bisphosphate	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-fructose 1,6-bisphosphate + H2O	Escherichia coli	enzyme is usually regarded as a regulatory enzyme of gluconeogenesis	D-fructose 6-phosphate + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

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	-	?
D-fructose 1,6-bisphosphate + H2O	enzyme is usually regarded as a regulatory enzyme of gluconeogenesis	Escherichia coli	D-fructose 6-phosphate + phosphate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
22	-	D-fructose 1,6-bisphosphate	pH 7.5	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	pseudo-tetrapeptide OC252	-	Escherichia coli

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Release 2023.1 (January 2023)