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Literature summary extracted from

  • Skalecki, K.; Mularczyk, W.; Dzugaj, A.
    Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle (1995), Biochem. J., 310, 1029-1035.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 AMP muscle enzyme is more strongly inhibited than the liver isoenzyme Homo sapiens
3.1.3.11 fructose 1,6-diphosphate
-
 Homo sapiens
3.1.3.11 fructose 2,6-diphosphate
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.00077
-
 fructose 1,6-diphosphate
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.11 Mg2+ required Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11
-
 Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.11 liver
-
 Homo sapiens
-
3.1.3.11 muscle
-
 Homo sapiens
-

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
-
-
 Homo sapiens

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
-
 Homo sapiens D-fructose 6-phosphate + phosphate
-
 ?