EC Number   |
Protein Variants |
Reference |
|---|
   7.5.2.B8 | E166A |
mutants shows no significant activity, and shows dimerization in the presence of ATP-Mg2+ |
720227 |
| 7.5.2.B8 | E166A |
the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzymed is defective in dimer dissociation |
724273 |
| 7.5.2.B8 | E166Q |
mutant lost about 80% of the wild-type activity, it shows dimerization in the presence of ATP-Mg2+ or ATP alone |
720227 |
| 7.5.2.B8 | G144A |
mutant is completely inactive and fails to dimerize, indicating an essential role of this residue in stabilizing the productive dimeric state. Although the E166A and G144A mutants each alone are inactive, they produce an active heterodimer, showing that disruption of one active site can be tolerated |
720227 |
| 7.5.2.B8 | G144A | |
the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzyme is unable to dimerize |
724273 |
| 7.5.2.B8 | S142A |
mutant retains considerable activity, and is able to dimerize, thus implying that the interaction of the serine with ATP is not essential for dimerization and catalysis. Although the E166A and G144A mutants each alone are inactive, they produce an active heterodimer, showing that disruption of one active site can be tolerated |
720227 |
