Copper-transporting ATPase (Cu-ATPase) is a copper transporting protein that transport copper ions into and out of cells to balance the copper level in the body using the energy from ATP hydrolysis. Copper plays a very important role in cell metabolism. And it acts as a cofactor of key enzymes involved in respiration, photosynthesis, detoxification of free radicals, iron uptake, neurotransmitter biosynthesis and so on. Structure analysis of Cu-ATPases suggests it has a characteristic catalytic domain which contains an evolutionarily conserved aspartate residue phosphorylated by ATP to form a phosphoenzyme intermediate. The pass-membrane region of Cu-ATPases contains a cation-binding cysteine-proline-cysteine/histidine/serine (CPx) motif responsible for catalytic activation and cation translocation. Besides, the N-terminal of Cu-ATPases contains the binding sites of copper ions.
Here shows part of Cu-ATPase in humans including ATP7A and ATP7B, encoded by ATP7A and ATP7B, respectively. The two subtypes of Cu-ATPase are present in the trans-Golgi network. They are both the essential copper pumps that maintain the intracellular copper homeostasis. And their functions are associated with the distinct intracellular targeting of the transporters.
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