EC Number   |
Subunits |
Reference |
|---|
    1.14.13.128 | ? |
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm), the native Ndm enzyme is probably composed of the two subunits (40000 Da (NdmA) and 35000 Da (NdmB)) in a hexameric configuration |
-, 709854 |
| 1.14.13.128 | ? |
x * 41000, theobromine demethylase, SDS-PAGE, x * 36600-43500, caffeine demethylase complex, SDS-PAGE |
717407 |
| 1.14.13.128 | ? |
x * 67000, SDS-PAGE |
-, 722538 |
| 1.14.13.128 | More |
NdmC forms a large multi-subunit complex comprising 2 monomeric units of each NdmC, NdmD, and NdmE and follows the typical electron flow pattern of Rieske oxygenases. The Rieske domain present in NdmD serves to function as an electron transfer domain during catalysis by NdmC as it lacks its own Rieske domain |
763990 |
| 1.14.13.128 | More |
the enzyme occurs as a Rieske nonheme iron oxygenase (RO)-reductase complex, the NdmCDE heterotrimer. NdmCDE domain architecture analysis, NdmC contains the ligand-binding domain, and the remaining Rieske domain must be nonfunctional because the metal coordinating residues are not conserved. Instead, a potentially functional, unique Rieske domain is located at the N-terminus of NdmD. In addition to the N-terminal Rieske domain, NdmD is composed of a flavin mononucleotide (FMN)-binding domain, an NADH-binding domain, and a C-terminal plant-type ferredoxin domain. NdmE has no discernable function, but exhibits high structural similarity to many glutathione-S-transferases. NdmE might facilitate complex formation by structural alignment |
-, 765239 |
