EC Number   |
Protein Variants |
Reference |
|---|
   7.2.2.8 | C14A/C17A/C110A/C113A |
increase in affinity for Cu(II) |
656102 |
| 7.2.2.8 | C14S/C17S |
site-directed mutagenesis, a dysfunctional non-copper-binding mutant |
734725 |
| 7.2.2.8 | C27A/C30A |
replacement of Cys in the N-terminal metal binding domain, mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity. The mutant enzyme binds Cu+, Ag+, and ATP with the same high apparent affinities as the wild-type enzyme. Evidence that the N-terminal metal binding domain disruption has no effect on the E1-E2 equilibrium is provided by the normal interaction of ATP acting with low affinity and the unaffected IC50 for vanadate inhibition observed in the C27A/C30A-substituted enzyme |
721587 |
| 7.2.2.8 | C27A/C30A/C751A/C754A |
mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity |
721587 |
| 7.2.2.8 | C380A/C382A |
the mutant enzyme binds ATP, indicating its correct folding and suggesting that enzyme turnover is prevented by the lack of metal binding to the transmembrane site |
721587 |
| 7.2.2.8 | C382A |
the mutant exhibits reduced copper binding activity |
725389 |
| 7.2.2.8 | C479A |
mutation results in lost of resistance to copper |
656102 |
| 7.2.2.8 | C481A |
mutation results in lost of resistance to copper |
656102 |
| 7.2.2.8 | C481H |
mutation results in lost of resistance to copper |
656102 |
| 7.2.2.8 | C575A/C578A |
mutation in the 6th copper site of the NMBD, catalytically inactive, no phosphoenzyme intermediate formed upon addition of ATP |
725000 |
