EC Number   |
Protein Variants |
Reference |
|---|
    1.16.1.1 | C11A |
site-directed mutagenesis of NmerA residue of the metal binding site |
714224 |
| 1.16.1.1 | C135A |
site-directed mutagenesis |
728149 |
| 1.16.1.1 | C136A/C141A |
site-directed mutagenesis, the C136A/C141A catalytic core mutant. Mutation of either C136 or C141 or both results in a total loss of Hg2+ reductase activity. CRystal structure determination with bound substrates |
744330 |
| 1.16.1.1 | C140A |
site-directed mutagenesis |
728149 |
| 1.16.1.1 | C14A |
site-directed mutagenesis |
728149 |
| 1.16.1.1 | C14A |
site-directed mutagenesis of NmerA residue of the metal binding site |
714224 |
| 1.16.1.1 | C558A |
mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme the mutant shows a 20fold reduction in turnover number and a 10fold increase in Km |
438084 |
| 1.16.1.1 | C559A |
mutation results in a total disruption of the Hg(II) detoxification pathway in vivo, compared to wild-type enzyme less than a 2fold reduction in turnover number and an increase in Km-value of 4-5fold |
438084 |
| 1.16.1.1 | C561A |
site-directed mutagenesis |
728149 |
| 1.16.1.1 | C628A |
HgX2 substrates with small ligands can rapidly access the redox-active cysteines in the absence of the C-terminal cysteines, but those with large ligands require the C-terminal cysteines for rapid access. The C-terminal cysteines play a critical role in removing the high-affinity ligands before Hg(II) reaches the redox-active cysteines |
-, 438086 |
