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Literature summary for 1.4.9.1 extracted from
- Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex (2012), Biochemistry, 51, 6942-6949.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Rhodobacter sphaeroides | Paracoccus denitrificans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus denitrificans | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Paracoccus denitrificans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MADH | - |
Paracoccus denitrificans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| tryptophan tryptophylquinone | MauG is a diheme enzyme that catalyzes the final steps in the biosynthesis of the cofactor tryptophan tryptophylquinone in the enzyme | Paracoccus denitrificans |  |
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Release 2023.1 (January 2023)
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