EC Number   |
Subunits |
Reference |
|---|
    1.16.1.1 | ? |
x * 66200, recombinant His-tagged MerA, SDS-PAGE |
713700 |
| 1.16.1.1 | ? |
x * 69000, SDS-PAGE |
-, 438088 |
| 1.16.1.1 | dimer |
1 * 54000 + 1 * 69000, SDS-PAGE |
-, 438083 |
| 1.16.1.1 | dimer |
1 * 56000 + 1 * 62000, SDS-PAGE |
-, 438059 |
| 1.16.1.1 | dimer |
1 * 58000 + 1 * 50400, SDS-PAGE |
-, 438066 |
| 1.16.1.1 | dimer |
2 * 56000, SDS-PAGE |
438060 |
| 1.16.1.1 | dimer |
interdomain dynamics in MerA, overview |
744515 |
| 1.16.1.1 | dimer |
the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA |
-, 745894 |
| 1.16.1.1 | dimer |
x * 54000 + x * 62000, SDS-PAGE |
-, 438072 |
| 1.16.1.1 | homodimer |
2 * 50000, SDS-PAGE |
714224 |
