EC Number   |
Inhibitors |
Structure |
|---|
   7.2.2.8 | Bathocuproine disulfonate |
i.e. BCS, Cu(I) chelator, reduces enzyme activity |
   |
| 7.2.2.8 | C12E8 |
- |
|
| 7.2.2.8 | cisplatin |
comparison of different metal-binding domains of ATPases based on their reactivity towards cisplatin. The rate of platination is generally greater for holo-metal-binding domains than for apo-metal-binding domains. The platinum binding weakens the CuI coordination, but does not expel the copper ion from metal-binding domains; comparison of different metal-binding domains of ATPases based on their reactivity towards cisplatin. The rate of platination is generally greater for holo-metal-binding domains than for apo-metal-binding domains. The platinum binding weakens the CuI coordination, but does not expel the copper ion from metal-binding domains |
|
| 7.2.2.8 | glucagon |
physiological concentrations of insulin increase endogenous ATP7B activity in cultured hepatic cells and in tissues by 40%, whereas glucagon inhibits this activity by 70%. The opposite effects of the hormones on ATP7B activity involve receptor-mediated signaling pathways and membrane-bound kinases PKA and PKB/Akt |
|
| 7.2.2.8 | glyoxal-bis(N-4,4-pyrolidine-3-thiosemicarbazonato)copper(II) |
treatment of SKOV-3 cells with micromolar concentrations leads to trafficking of the endogenous copper transporter ATP7A from the Golgi network to the cell membrane |
|
| 7.2.2.8 | glyoxal-bis(N-4-methyl-3-thiosemicarbazonato)copper(II) |
treatment of SKOV-3 cells with micromolar concentrations leads to trafficking of the endogenous copper transporter ATP7A from the Golgi network to the cell membrane |
|
| 7.2.2.8 | hydroxylamine |
sensitive to |
|
| 7.2.2.8 | KOH |
sensitive to |
|
| 7.2.2.8 | more |
ATPase activity os almost completely suppressed by incubating CopA (1 mg/ml or 0.00633 mM) for 1 h in a solution containing 1 mM MgCl2, 0.1 mM AlCl3, 2 mM potassium fluoride in the presence of either 0.02 mM Cu+,1 mM ADP, and 0.02mM Cu+, or 0.5 mM bathocuproine disulfonate |
|
| 7.2.2.8 | more |
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 |
|
