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Literature summary for 3.1.3.11 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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-
muscle
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-diphosphate + H2O
-
Homo sapiens D-fructose 6-phosphate + phosphate
-
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