The promiscuous phosphomonoestearase activity of Af-CopA is characterized and compared with the principal ATPase activity.
The enzyme is more efficient for capturing ATP, but pNPP would be better placed at the catalytic site.
Both activities are enhanced by Mg2 + (essential) and phospholipids (non-essential),
Salts and Cu+ have opposite effects on the ATPase and phosphatase activities.
Catalysis of both substrates is driven by an enthalpy lowering mechanism.