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Literature summary for 3.5.4.6 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
Search for more literature for 3.5.4.6

Inhibitors

Inhibitors Comment Organism Structure
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
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

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
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Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
AmpD
-
 Oryctolagus cuniculus