EC Number   |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Reference |
|---|
   7.2.2.9 | -999 |
- |
11 missense variants of ATP7B identified in Wilson disease patients analyzed by capacity of functional complementation of a yeast mutant strain disrupted by the ATP7B gene ortholog CCC2, solution structures and homology of ATP7B domains used to predict effects of each variant |
687041 |
| 7.2.2.9 | -999 |
- |
analysis of ATP7B at the cell surface by expression studies in intact cells, presence of ATP7B at the plasma membrane shown by electron microscopy, freeze-fracture experiments and surface luminescence measurements, delivery to the plasma membrane of oocytes unaffected by deletion of the N-terminal copper-binding domain or the inactivating mutation of catalytic Asp1027, surface targeting decreased for ATP7B variants with mutations in the ATP-binding site or in the copper-binding site, ligand-stabilized conformations important for ATP7B trafficking |
685370 |
| 7.2.2.9 | -999 |
- |
ATP-dependent accumulation of cisplatin indicated, cisplatin shown to induce acyl-phosphorylation of ATP7B but at slower rate than copper, Vmax value for cisplatin shown to be nearly 28fold lower than that for copper |
689075 |
| 7.2.2.9 | -999 |
- |
ATP7A xpressed to a variable degree throughout the kidney, age-dependent intracellular localization, copper elevation results in the in vivo redistribution of ATP7A from intracellular compartments toward the basolateral membrane, ATP7A plays a major role in exporting copper via basolateral membranes and protects renal tissue against copper overload |
684373 |
| 7.2.2.9 | -999 |
- |
biochemical and structural characteristics of human copper-ATPase, unique sequence motifs in regulating ATP7A and ATP7B activity and trafficking, transmembrane organization and catalytic cycle, sequence and predicted folding of transmembrane portion, metal binding pockets of N-terminal domain and ATP-binding domain |
684675 |
| 7.2.2.9 | -999 |
- |
biochemical and structural characteristics of human copper-ATPases, unique sequence motifs in regulating ATP7A and ATP7B activity and trafficking, dual role of copper-transporting ATPase ATP7B in hepatocyte, transmembrane organization and catalytic cycle, sequence and predicted folding of transmembrane portion, metal-binding pockets of N-terminal domain and ATP-binding domain |
684675 |
| 7.2.2.9 | -999 |
- |
connection between copper homeostasis and NMDA receptor activity, ATP7A required for copper-dependent effects |
689738 |
| 7.2.2.9 | -999 |
- |
copper concentration in the mammary gland reduced in transgenic mice, immunofluorescence analysis of mammary gland tissue, tissue copper concentration, mRNA levels of endogenous ATP7A and ATP7B and of ATP7B protein unaltered in mammary gland of transgenic mice, ATP7A plays a role in removing excess copper from mammary epithelial cells rather than supplying copper to milk |
684927 |
| 7.2.2.9 | -999 |
- |
CtrA2 protein shown to have a CPC metal-binding sequence in TM6 and a CxxC metal-binding N-terminal domain, substrate ion-induced activity on lipids, pH, temperature, ionic strength and thiols tested, CtrA2 protein activated by Ag+ and Cu2+, transport of reduced copper ion |
688411 |
| 7.2.2.9 | -999 |
- |
CtrA3 protein has a CPH metal-binding motif in TM6 and a histidine-rich N-terminal metal-binding domain substrate ion-induced activity on lipids, pH, temperature, ionic strength and thiols, eight membrane-spanning alpha-helices per monomer determined by structural analysis, arrangement of the six central helices surrounding the ion-binding site in the membrane conserved, sequence alignment and fitting of domains to the projection map |
688411 |
