Literature summary for 7.2.2.8 extracted from

Gourdon, P.; Sitsel, O.; Lykkegaard Karlsen, J.; Birk M?ller, L.; Nissen, P.
Structural models of the human copper P-type ATPases ATP7A and ATP7B (2012), Biol. Chem., 393, 205-216.

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the enzyme's heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition; the enzyme's heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35670	ATP7B	-
Homo sapiens	Q04656	ATP7A	-

Synonyms

Synonyms	Comment	Organism
ATP7A	-	Homo sapiens
ATP7B	-	Homo sapiens
copper P-type ATPase	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the P-type ATPases	Homo sapiens
malfunction	enzyme missense mutations are involved in Menkes disease	Homo sapiens
malfunction	enzyme missense mutations are involved in Wilson's disease	Homo sapiens
additional information	the enzyme shows six sequential heavy-metal binding domains (HMBD1-HMBD6) and a type-specific constellation of transmembrane helices, the heavy-metal binding domains, HMBD5 and HMBD6 are the most crucial for function, the heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition. Homology structure modeling based on the existing structure of the soluble domain and the structure of the homologous LpCopA from the bacterium Legionella pneumophila. The domains and residues involved in the catalytic phosphorylation events and copper transfer are highly conserved	Homo sapiens

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Release 2023.1 (January 2023)