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Literature summary for 1.4.9.1 extracted from
- Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone (2008), Biochemistry, 47, 2908-2912.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| MauG | the inactive 119 kDa heterotetrameric precursor of MADH with incompletely synthesized tryptophan tryptophylquinone can be converted to active MADH with mature tryptophan tryptophylquinone in vitro by reaction with MauG, a 42 kDa diheme enzyme | Paracoccus denitrificans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus denitrificans | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| HiLoad Superdex 200 gel filtration | Paracoccus denitrificans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methylamine + acceptor + H2O | - |
Paracoccus denitrificans | formaldehyde + NH3 + reduced acceptor | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MADH | - |
Paracoccus denitrificans |
| methylamine dehydrogenase | - |
Paracoccus denitrificans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| tryptophan tryptophylquinone | - |
Paracoccus denitrificans | |
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