Literature summary for 3.1.3.11 extracted from

Nelson, S.W.; Choe, J.Y.; Honzatko, R.B.; Fromm, H.J.
Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase (2000), J. Biol. Chem., 275, 29986-29992.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sus scrofa

Protein Variants

Protein Variants	Comment	Organism
A51P	The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged.	Sus scrofa
K50P	The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged, but 40fold loss if specific activity in comparison of wild-type enzyme, the Hill coefficients of Mg2+ are significantly reduced	Sus scrofa
K50P/Y57W	the KI value of AMP is increased, the mutant displays a biphasic bahavior toward AMP, the KM value is unchanged	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP	kinetic mechanism	Sus scrofa
D-fructose-2,6-bisphosphate	kinetic mechanism	Sus scrofa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0013	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant K50P/Y57W	Sus scrofa
0.00175	-	D-fructose 1,6-bisphosphate	pH 7.5, wild-type enzyme	Sus scrofa
0.0021	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant K50P	Sus scrofa
0.0025	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant A51P	Sus scrofa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
K+	-	Sus scrofa
Mg2+	-	Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-fructose 1,6-bisphosphate + 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
wild-type and mutant enzymes	Sus scrofa

Reaction

Reaction	Comment	Organism	Reaction ID
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate	loop 52-72 is an essential element in the allosteric mechanism of enzyme	Sus scrofa	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Sus scrofa

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
6.7	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant K50P	Sus scrofa
9.2	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant K50P/Y57W	Sus scrofa
12.4	-	D-fructose 1,6-bisphosphate	pH 7.5, mutant A51P	Sus scrofa
22	-	D-fructose 1,6-bisphosphate	pH 7.5, wild-type enzyme	Sus scrofa

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000123	-	D-fructose 2,6-bisphosphate	pH 7.5, wild-type enzyme	Sus scrofa
0.00037	-	D-fructose 2,6-bisphosphate	pH 7.5, mutant K50P/Y57W	Sus scrofa
0.0023	-	D-fructose 2,6-bisphosphate	pH 7.5, mutant K50P	Sus scrofa
0.0034	-	D-fructose 2,6-bisphosphate	pH 7.5, mutant A51P	Sus scrofa

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Release 2023.1 (January 2023)