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Literature summary extracted from
- Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface (2011), Biochemistry, 50, 1265-1273.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.9.1 | Paracoccus denitrificans | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.9.1 | - |
Paracoccus denitrificans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.9.1 | methylamine + H2O + amicyanin | P96A and P96G mutations in amycyanin do not affect the spectroscopic or redox properties of amicyanin but increase the Kd value for complex formation with MADH and alter the kinetic mechanism for the interprotein elcetron transfer reaction. The crystal structure of P96G amicyanin is very similar to that of native amicyanin, but in addition to the change in Pro96, the side chains of residues Phe97 and Arg99, which make contacts with MADH that are important for stabilizing the amicyanin-MADH complex, are oriented differently | Paracoccus denitrificans | formaldehyde + ammonia + reduced amicyanin | - |
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