Literature summary for 7.2.2.9 extracted from

DiDonato,M.; Narindrasorasak, S.; Sarkar, B.
Expression, purification, and metal binding characteristics of the putative copper binding domain from the Wilson disease copper transporting ATPase (ATP7B) (1999), Adv. Exp. Med. Biol., 448, 165-173.

Search for more literature for 7.2.2.9

Cloned(Commentary)

Cloned (Comment)	Organism
construction and expression of the fusion protein of glutathione-S-transferase and Wilson-disease protein and expression in Escherichia coli	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + Cu2+/in	Homo sapiens	responsible for ligating the copper atoms prior to transport across the membrane	ADP + phosphate + Cu2+/out	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
fusion protein of glutathione-S-transferase and Wilson-disease protein expressed in Escherichia coli	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + Cu2+/in	copper bound to the domain exists in the +1 oxidation state, upon binding, Cu(II) atoms are reduced to Cu(I) by some mechanism, binding of copper by the domain is cooperative in nature	Homo sapiens	ADP + phosphate + Cu2+/out	-	?
ATP + H2O + Cu2+/in	responsible for ligating the copper atoms prior to transport across the membrane	Homo sapiens	ADP + phosphate + Cu2+/out	-	?

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Release 2023.1 (January 2023)