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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 expression in Escherichia coli Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 A51P The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged. Sus scrofa
3.1.3.11 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
3.1.3.11 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.0013
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant K50P/Y57W Sus scrofa
3.1.3.11 0.00175
-
 D-fructose 1,6-bisphosphate pH 7.5, wild-type enzyme Sus scrofa
3.1.3.11 0.0021
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant K50P Sus scrofa
3.1.3.11 0.0025
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant A51P Sus scrofa

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Sus scrofa P00636
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11 wild-type and mutant enzymes Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.11 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]

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

Substrates and Products (Substrate)

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

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 6.7
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant K50P Sus scrofa
3.1.3.11 9.2
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant K50P/Y57W Sus scrofa
3.1.3.11 12.4
-
 D-fructose 1,6-bisphosphate pH 7.5, mutant A51P Sus scrofa
3.1.3.11 22
-
 D-fructose 1,6-bisphosphate pH 7.5, wild-type enzyme Sus scrofa

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.11 0.000123
-
 D-fructose 2,6-bisphosphate pH 7.5, wild-type enzyme Sus scrofa
3.1.3.11 0.00037
-
 D-fructose 2,6-bisphosphate pH 7.5, mutant K50P/Y57W Sus scrofa
3.1.3.11 0.0023
-
 D-fructose 2,6-bisphosphate pH 7.5, mutant K50P Sus scrofa
3.1.3.11 0.0034
-
 D-fructose 2,6-bisphosphate pH 7.5, mutant A51P Sus scrofa