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Literature summary for 1.4.9.1 extracted from
- Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper (2011), J. Inorg. Biochem., 105, 1638-1644.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| amicyanin mutant M98K | mutant acts as a competitive inhibitor in the reaction of native amicyanin with methylamine dehydrogenase indicating that the M98K mutation has not affected the affinity for its natural electron donor. The crystal structure of M98K amicyanin reveals an overall structure very similar to native amicyanin but the type I binding site is occupied by zinc instead of copper | Paracoccus denitrificans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus denitrificans | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Paracoccus denitrificans |
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