Any feedback?
Literature summary for 7.2.2.9 extracted from
- Zinc binding to the NH2-terminal domain of the Wilson disease copper-transporting ATPase: implications for in vivo metal ion-mediated regulation of ATPase activity (2002), J. Biol. Chem., 277, 13409-13414.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli as a GST fusion protein | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | zinc binds with a stoichiometry of 6 to 1 and induces a conformational change in the N-terminal domain that is different from those observed for copper binding, leading to a loss of secondary structure in the domain | Homo sapiens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + Cu2+/in | - |
Homo sapiens | ADP + phosphate + Cu2+/out | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP7B | - |
Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
