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Literature summary for 3.1.3.11 extracted from

  • Dziewulska-Szwajkowska, D.; Zmojdzian, M.; Dobryszycki, P.; Kochman, M.; Dzugaj, A.
    The interaction of FBPase with aldolase: A kinetic and fluorescence investigation on chicken muscle enzymes (2004), Comp. Biochem. Physiol. B, 137B, 115-129.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
AMP susceptibility of enzyme decreases in complex with aldolase Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
maximum activity at 0.02 mM D-fructose 1,6-bisphosphate, decrease above. Substrate-inhibition model of reaction Gallus gallus

Subunits

Subunits Comment Organism
More enzyme forms a complex with aldolase in 1:1 stoichiometry and a dissociation constant of 0.0038 mM. Interaction decreases sensitivity to inhibitor AMP, but has no effect on pH optimum of enzyme Gallus gallus