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Literature summary extracted from

  • Kurbanov, F.T.; Choe, J.; Honzatko, R.B.; Fromm, H.J.
    Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition (1998), J. Biol. Chem., 273, 17511-17516.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 D68E mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme Sus scrofa
3.1.3.11 D74A 50000fold reduced turnover number relative to wild type enzyme Sus scrofa
3.1.3.11 D74E mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive Sus scrofa
3.1.3.11 D74N 2000fold reduced turnover number relative to wild type enzyme Sus scrofa
3.1.3.11 K71A mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme Sus scrofa
3.1.3.11 K71M/K72M mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme, 175fold increased inhibition constant for AMP, 2fold increased affinity for Mg2+ Sus scrofa
3.1.3.11 N64A mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive Sus scrofa
3.1.3.11 N64Q mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.00103
-
 fructose 1,6-diphosphate mutant enzyme D74E, pH 8.5 Sus scrofa
3.1.3.11 0.00131
-
 fructose 1,6-diphosphate mutant enzyme D68E, pH 7.5 Sus scrofa
3.1.3.11 0.00142
-
 fructose 1,6-diphosphate mutant enzyme N64A, pH 8.5 Sus scrofa
3.1.3.11 0.0016
-
 fructose 1,6-diphosphate mutant enzyme K71M/K72M, pH 7.5 Sus scrofa
3.1.3.11 0.0017
-
 fructose 1,6-diphosphate mutant enzyme N64E, pH 8.5 Sus scrofa
3.1.3.11 0.0022
-
 fructose 1,6-diphosphate wild type enzyme, pH 8.5 Sus scrofa
3.1.3.11 0.0028
-
 fructose 1,6-diphosphate wild type enzyme, pH 7.5 Sus scrofa
3.1.3.11 0.0028
-
 fructose 1,6-diphosphate mutant enzyme K71A, pH 7.5 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.11 D-fructose 1,6-diphosphate + H2O
-
 Sus scrofa D-fructose 6-phosphate + phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 0.0004
-
 fructose 1,6-diphosphate mutant enzyme D74A, pH 8.5 Sus scrofa
3.1.3.11 0.01
-
 fructose 1,6-diphosphate mutant enzyme D74N, pH 8.5 Sus scrofa
3.1.3.11 1.2
-
 fructose 1,6-diphosphate mutant enzyme D74E, pH 8.5 Sus scrofa
3.1.3.11 5.4
-
 fructose 1,6-diphosphate mutant enzyme N64E, pH 8.5 Sus scrofa
3.1.3.11 6.4
-
 fructose 1,6-diphosphate mutant enzyme D68E, pH 7.5 Sus scrofa
3.1.3.11 7.1
-
 fructose 1,6-diphosphate mutant enzyme N64A, pH 8.5 Sus scrofa
3.1.3.11 9.1
-
 fructose 1,6-diphosphate wild type enzyme, pH 8.5 Sus scrofa
3.1.3.11 16
-
 fructose 1,6-diphosphate mutant enzyme K71A, pH 7.5 Sus scrofa
3.1.3.11 21
-
 fructose 1,6-diphosphate wild type enzyme, pH 7.5 Sus scrofa
3.1.3.11 34
-
 fructose 1,6-diphosphate mutant enzyme K71M/K72M, pH 7.5 Sus scrofa