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Literature summary extracted from

  • Martini, D.; Ranieri-Raggi, M.; Sabbatini, A.R.; Moir, A.J.; Polizzi, E.; Mangani, S.; Raggi, A.
    Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site (2007), Biochim. Biophys. Acta, 1774, 1508-1518.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.6 ATP at pH 5.9 in the absence of fluoride, ATP exerts a biphasic effect; less than 0.003 mM ATP act as an inhibitor, whereas increasing ATP concentrations above 0.003 mM reverse the inhibition Oryctolagus cuniculus
3.5.4.6 fluoride over the pH range 5.9-7.5 fluoride ion acts as pure uncompetitive inhibitor of AMPD, with the Ki increasing from 1 to 30 mM Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.6 Zn2+ dinuclear cocatalytic Zn site, the two Zn2+ ions in the AMPD metallocenter operate together as a single catalytic unit, but have independent functions Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.6 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.4.6 skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.6 AMP + H2O
-
 Oryctolagus cuniculus IMP + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.4.6 More presence of two species of 173 kDa and 309 kDa being consistent with the existence of a dimer-tetramer equilibrium Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
3.5.4.6 AmpD
-
 Oryctolagus cuniculus