Protein Variants | Comment | Organism |
---|---|---|
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 | Bacillus sp. (in: Bacteria) |
C629A | 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 | Bacillus sp. (in: Bacteria) |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. (in: Bacteria) | - |
- |
- |
Bacillus sp. (in: Bacteria) RC607 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hg2+ + NADPH | - |
Bacillus sp. (in: Bacteria) | Hg + NADP+ + H+ | - |
? | |
Hg2+ + NADPH | - |
Bacillus sp. (in: Bacteria) RC607 | Hg + NADP+ + H+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Bacillus sp. (in: Bacteria) |