Literature summary for 3.1.3.11 extracted from

Choe, J.Y.; Fromm, H.J.; Honzatko, R.B.
Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes (2000), Biochemistry, 39, 8565-8574.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sus scrofa

Crystallization (Commentary)

Crystallization (Comment)	Organism
In presence of AMP, the enzyme crystallizes in the T-state and AMP displaces loop 52-72 from its engaged conformation and abolishes metal association with sites 2 and 3. In the absence of AMP, enzyme is in the R-state and loop 52-72 associates with the active site. Three metal-binding sites are occupied by Zn2+ and two of three metal sites by Mg2+.	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	allosteric inhibitor	Sus scrofa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Sus scrofa
Zn2+	-	Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P00636	-	-

Purification (Commentary)

Purification (Comment)	Organism
the recombinant enzyme	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-fructose 1,6-diphosphate + H2O	-	Sus scrofa	D-fructose 6-phosphate + phosphate	-	?
D-fructose 1,6-diphosphate + H2O	enzyme is usually regarded as a regulatory enzyme of gluconeogenesis	Sus scrofa	D-fructose 6-phosphate + phosphate	-	?

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Release 2023.1 (January 2023)