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Literature summary for 1.16.1.1 extracted from
- Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide (1983), Biochemistry, 22, 4082-4088.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme shows extensive sequence homology and functional similarities in the active site of mercuric reductase and nicotinamide disulfide oxidoreductase | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
enzyme is encoded by the transposon Tn501 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of the major 14C-labeled peptide from a tryptic digestion of labeled mercuric reductase | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Hg2+ + NADPH | - |
Pseudomonas aeruginosa | Hg + NADP+ + H+ | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | flavoprotein | Pseudomonas aeruginosa | |
| NADPH | - |
Pseudomonas aeruginosa | |
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Release 2023.1 (January 2023)
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