EC Number   |
Cofactor |
Reference |
|---|
   1.1.2.7 | more |
MxaJ, a chaperone-like protein facilitating the assembly of MDH, additional component MxaJ together with a MDHI can facilitate the methanol oxidation process |
763672 |
| 1.1.2.7 | phenazine methosulfate |
mediates reduction of 2,6-dichlorophenol-indophenol |
687417 |
| 1.1.2.7 | phenazine methosulfate |
mediates reduction of 2,6-dichlorophenolindophenol |
687417 |
| 1.1.2.7 | pyrroloquinoline quinone |
- |
676902, 723854, 725300 |
| 1.1.2.7 | pyrroloquinoline quinone |
binding structure in the active site, overview |
689139 |
| 1.1.2.7 | pyrroloquinoline quinone |
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview |
673048 |
| 1.1.2.7 | pyrroloquinoline quinone |
dependent on |
687417 |
| 1.1.2.7 | pyrroloquinoline quinone |
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group |
690095 |
| 1.1.2.7 | pyrroloquinoline quinone |
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer |
667721 |
| 1.1.2.7 | pyrroloquinoline quinone |
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure |
688333 |
